IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ http://www.ebi.ac.uk/ farhoud-2005-1 Protein complexes in the archaeon Methanothermobacter thermautotrophicus analyzed by blue native/SDS-PAGE and mass spectrometry. metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum bn-page blue native page bn-page de novo protein sequence de novo protein sequencing by mass spectrometry de novo protein sequence Farhoud MH., Wessels HJ., Steenbakkers PJ., Mattijssen S., Wevers RA., van Engelen BG., Jetten MS., Smeitink JA., van den Heuvel LP., Keltjens JT. Archaea - Interaction dataset based on Archaea proteins M. thermautotrophicus (DSM1053) was cultured in a 12-liter fed-batch fermentor containing 10 liters of medium. Cells were cultured under two different conditions. In one treatment cells (MCR 1) were cultured in N medium (15) at 65 �C with a gas flow of 2.0 liters/min of 80% H2, 20% CO2 (v/v) and harvested at an optical density at 600 nm of 5. In the other treatment (MCR II) cells were grown at 55 �C with a gas flow of 5.0 liters/min of 80% H2, 20% CO2 (v/v) and harvested at an optical density at 600 nm of 1.8. Table 1. Table 2. Figure 1. Figure 2. P.Steenbakkers@science.ru.nl Mol. Cell Proteomics (1535-9476) 2005 hall-2004-1 Interactions between RNase P protein subunits in archaea. metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Hall TA., Brown JW. Archaea - Interaction dataset based on Archaea proteins james_brown@ncsu.edu Archaea (1472-3646) 2004 Only protein-protein interactions imex curation ye-2006-2 Crystal structures of a ligand-free MthK gating ring: insights into the ligand gating mechanism of K+ channels. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Ye S., Li Y., Chen L., Jiang Y. youxing.jiang@utsouthwestern.edu Cell (0092-8674) 2006 Only protein-protein interactions 3 imex curation ye-2006-1 Crystal structures of a ligand-free MthK gating ring: insights into the ligand gating mechanism of K+ channels. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Ye S., Li Y., Chen L., Jiang Y. youxing.jiang@utsouthwestern.edu Cell (0092-8674) 2006 Only protein-protein interactions 3 imex curation mthk_metth Calcium-gated potassium channel MthK mthK MTH_1520 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MVLVIEIIRKHLPRVLKVPATRILLLVLAVIIYGTAGFHFIEGESWTVSLYWTFVTIATVGYGDYSPSTPLGMYFTVTLIVLGIGTFAVAVERLLEFLINREQMKLMGLIDVAKSRHVVICGWSESTLECLRELRGSEVFVLAEDENVRKKVLRSGANFVHGDPTRVSDLEKANVRGARAVIVDLESDSETIHCILGIRKIDESVRIIAEAERYENIEQLRMAGADQVISPFVISGRLMSRSIDDGYEAMFVQDVLAEESTRRMVEVPIPEGSKLEGVSVLDADIHDVTGVIIIGVGRGDELIIDPPRDYSFRAGDIILGIGKPEEIERLKNYISA rnp4_metth Ribonuclease P protein component 4 rnp4 Rpp21 MTH_1618 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MRRGKRPRWMLKIAEERIDILFRMADREFSANPHRSHRYTELARNIAMKYRVRIPREWRRRFCRKCYSFLKPGANCTVRIADGKVNFRCHECGHIMRFPYIREKKDRRRNKIESHTTKEGTDEQITVGAHNKCGESQSDR rnp2_metth Ribonuclease P protein component 2 rnp2 Pop5 MTH_687 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MKILPPTLRVPRRYIAFEVISERELSREELVSLIWDSCLKLHGECETSNFRLWLMKLWRFDFPDAVRVRGILQCQRGYERRVMMALTCAHHHSGVRVAIHILGLSGTIRSATQKFIKPSKKDKY rnp1_metth Ribonuclease P protein component 1 rnp1 Rpp29 MTH_11 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MITPRNIFRHELIGLSVRIARSVHRDIQGISGRVVDETRNTLRIEMDDGREITVPKGIAVFHFRTPQGELVEIDGRALVARPEERIKKKFRKP rnp3_metth Ribonuclease P protein component 3 rnp3 Rpp30 MTH_688 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MIPQRILMKFFDFHIQGRDHDSSLRLLLEASRLGYQGGVLVYPSERYPDLKSDLESLRENPELQDFEIARGVMINASDPRDMRRSVNKFRKKADVIYVSGGNLKVNRAACESRRVDVLSAPYTSRRDPGINHVLAREAARNNVAVELPLADVIGSWLKVRARVLEQFREILKLHRKFGFPLLLTSRASSIYDLRTPGDIMNLAECFGMESSEAEESLTSTPASILEDSGNRHLLIAEGVRLLPES fpaa_metth Type A flavoprotein FprA Flavoprotein A fpaA fprA MTH_1350 FMN protein FprA protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MKARAEKIADGLYWTGVLDWDIRNYHGYTLQGTTYNAYLVFGDEGVALIDNSYPGTFQELMARMEDAFNREGREMRVDFIVQNHVERDHSGVLVELHRRFPEAEIHCTEVAVEGLLKHYPALEGTEFRTVKTGDSIDLGGRTLTFLEAPLLHWPDSMFTFLDTGILFSNDAFGQHLCYPQRLDTEIPEYILMDAAKKFYANLITPLSKLVLRKFDEVKELGLLDKIGMIAPSHGQIWTEPMKIIEAYTAWATGKVKKKVTVIYDTMHHSTAMMAHAIAEGAMSEGADVRVYYLHEDDRSEIVKDILDSHAIALGAPAIYDEPYPSVGDLLMYLRGLKFNRTGQRRAMVFGSMGGRGGATGTMQKLLADAGFDVMEADEIYYVPNNEELDACFEAGRRLAGDLNE hem2_metth Delta-aminolevulinic acid dehydratase Porphobilinogen synthase hemB MTH_744 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MSDNMEFPTKRMRRLRKSPQIRNILRETRLHPSDLIYPMFVSEKLGRGDVEAIDTMPGQFRYSVDDAVSEASRLEDEGLSSVLIFGMPSAKDELASAAHDPHGVVQRTVRRLKEETDLVVMTDVCLCQYTSHGHCGIVVDGEIVNDETLEVLSRIALSHAEAGADVVAPSDMMDGRVAAIRRSLDDAGFQDTLIMSYAVKYASAFYAPFRGAVSSAPAFGDRRSYQMDPANIDEALIEAELDLREGADILMVKPALAYLDVIGKVRERFSVPLAAYNVSGEYSMLKAAIKSGYLTDEAIYESILSIKRAGADLIISHFAPDLLGVI o26729_metth MTH_632 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MITVTGDITVDWIQWSVKGDSDVSEFNWKNHLGFKRKALEGGALLTARMLKNFTEVNHPSIGDEPGNTDPSEFIHSFAELKATGDGYHVKKFMGYTGPDSGLPSMPFSLKEHESPIIVIDDAGNGFREMEERWPSQIMGGDPLIVLKMSSPLFRGSLWEHLLEEHPEKLIVIITADDLREHGANITRRLSWERTAEDFIWQMENNRSLEDLRDLNVVVRIGLEGAINYNRGDVRLFYHPQFFEGDLTERAPGKMQGCGSAFTAAFTAALSEGREMDECIRRGITAAARLLERGFSSEPDYPISDVFMSADDEIGAVEIPQHPRGLWTIASSPPLFDIESVSRYIVINGYSRKKCPLPVAHFGKLITADRREIEGYQSIRNLMVEYMKNDNPERPLCIGVFGPPGAGKSFAVSQLAASVDPERIKHLNFNISQFRCEDDLIDAFHQIRDAVLEGMVPQAFFDEFDSPIGEKKLGWVKYFLAPMQDGEFREGDSMHPLGKCILVFAGGTSSTFQEFESQDPEVLKEAKVRDFISRLRGYVNIIGPDPQHRRDKFFMLRRAILLRSMFERKAPHLFDASGRLRIDEGVLNAFLMIPEYRHGVRSMEAILDMSILQDVRKFEKASLPSAGQLDLHVDGELFHRMAMD adhs_metth 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase aroA' MTH_579 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MIGKRIRIERIINRKTDRTVIVPLDHGVSIGPVRGIIDMAGTIDEVASGGANAVLMHKGMVRSGHRGYGRDIGLIIHLSASTGLGPDPNHKVLVTSVEKALKLGADAVSVHVNVGSEREPEMLIKLGTVAEICDDWGMPLIAMMYPRGKKIDDEHDPEVVKLAARAGAELGADIIKTNYTGDPDTFRDVVKGCPVPVVIAGGPKIETEEELLQMVSDSVEAGGAGVAIGRNIFQADSPANMTGAIAGIVHDGLSVEEAVRILKGGE o27556_metth MTH_1512 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MSTMKVAVYGAGNQKLYVDQLNLPEKYGGEAPYGGSRMAIEFAEAGHDVVLAEPARDMLDDAHWKVVEDAGVTVTDNDAEAASEAEIAVLFTPFGKKTFEIAKNITNHLPEGAVIANTCTVSPVVLYYVLERELRRDRKDLGIASMHPAAVPGTPQHGHYVIGGHSSSELDIATDEQISRCVELAESCGKVAYVVPADVSSAVADMGSLVTAVTLSGVLDYYYVGTQIIRAPKEMVEKQILMTLQTIASLVETSGVNGMLKAMNPELLVRSAKSMHLLEEQEELDAALNTLSDLDDEVNKWIEKGEIRHTDLVAAQALAKEIKNLMGGKAAEGTIRRCMRKMFE trpb2_metth Tryptophan synthase beta chain 2 trpB2 MTH_1476 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MMNKIVLDENEIPKKWYNINPDLPSPLPEPKNPEGGKNIENLPRVFSRGVLEQEMSMERWIKIPREVMDVYKMIGRPTPLFRAKGLEEMLDTPARIYYKREDYSPTGSHKLNTAIAQAYYARKDGAERLTTETGAGQWGTALSLACSLMDLQCKVYMVRVSFNQKPFRKTIMQLYGGEVVPSPSNHTEFGRRMLKEDPEHPGSLGIAISEAMEEALQEENVYYSLGSVLNHVLLHQTVIGLETKKQLEIAGETPDIMIGCVGGGSNFGGAIFPFVKDKLDGKLDCEFIAAEPKSCPTLTAGEYRYDFGDTAGMTPLLKMYTLGHDFVPPSVHAGGLRYHGMSPQVALLVREGVINARAVPQHTIFESGVKFAKAEGVVPAPETCHAISVAIDEARKCRETGEEKTIVISFSGHGLLDLKGYGDYLEGKI mtd_metth F420-dependent methylenetetrahydromethanopterin dehydrogenase Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase MTH_1464 mtd protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MVVKIGIIRCGNIGTSPVLDLLLDERADRPNIDVCVVGSGAKMNPDEIERAVPTMLEMDRDFVIFISPNPGAPGPAKARELLSEADVPAMIIGDAPGLRVKDEIEEQGLGYIIVKADPMIGARREFLDPTEMASFNSDVIKVLAFTGAYRVVQNTIDAMIADVEAGKAPELPQVVIDTDVAVEAAGYENPYAKAKAMAAYEIATKVADIDVKGCFMVQDPDKYIPIVASAHEMLAAAAKLAVEAREIEKANDTVLRTPHGKEGETLSKTDLLAKPE risb_metth 6,7-dimethyl-8-ribityllumazine synthase ribH MTH_1390 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MKKVRIGAVVAEFNYDITHMMLELAKEHARFLDAEITRVIAVPGVFDMPLAVKKLLLEDEIDAVITLGAVIEGATDHDQIVVQHASRKIADLALDYDKPVALGISGPGMTRLEAHQRVDYAKRAVEAAVKMYRRLKEDI mcry_metth Methyl-coenzyme M reductase II subunit beta Coenzyme-B sulfoethylthiotransferase beta mrtB MTH_1132 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MPMYEDRIDLYGADGKLLEEDVPLEAVSPLKNPTIANLVSDVKRSVAVNLAGIEGSLKKAALGGKSNFIPGREVELPIVENAEAIAEKVKRLVQTSEDDDTNIRLINNGQQILVQVPTTRMGVAADYTVSALVTGAAVVQAIIDEFDVDMFDANAVKTAVMGRYPQTVDFTGANLSTLLGPPVLLEGLGYGLRNIMANHVVAITRKNTLNASALSSILEQTAMFETGDAVGAFERMHLLGLAYQGLNANNLLFDLVKENSKGTVGTVIASLVERAIEDRVIKVASEMKSGYKMYEPADWALWNAYAATGLLAATIVNVGAARAAQGVASTVLYYNDILEYETGLPGVDFGRAMGTAVGFSFFSHSIYGGGGPGIFHGNHVVTRHSKGFALPCVAAAMCLDAGTQMFSVEKTSGLIGSVYSEIDYFREPIVNVAKGAAEIKDQL mcra_metth Methyl-coenzyme M reductase subunit alpha Coenzyme-B sulfoethylthiotransferase alpha mcrA MTH_1164 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MADKLFINALKKKFEESPEEKKTTFYTLGGWKQSERKTEFVNAGKEVAAKRGIPQYNPDIGTPLGQRVLMPYQVSTTDTFVEGDDLHFVNNAAMQQMWDDIRRTVIVGLNHAHAVIEKRLGKEVTPETITHYLETVNHAMPGAAVVQEHMVETHPALVADSYVKVFTGNDEIADEIDPAFVIDINKQFPEDQAETLKAEVGDGIWQVVRIPTIVSRTCDGATTSRWSAMQIGMSMISAYKQAAGEAATGDFAYAAKHAEVIHMGTYLPVRRARGENEPGGVPFGYLADICQSSRVNYEDPVRVSLDVVATGAMLYDQIWLGSYMSGGVGFTQYATAAYTDNILDDFTYFGKEYVEDKYGLCEAPNTMDTVLDVASEVTFYGLEQYEEYPALLEDQFGGSQRAAVVAAAAGCSTAFATANAQTGLSGWYLSMYLHKEQHSRLGFYGYDLQDQCGASNVFSIRGDEGLPLELRGPNYPNYAMNVGHQGEYAGISQAPHAARGDAFVFNPLVKIAFADDNLVFDFTNVRGEFAKGALREFEPAGERALITPAK mcrg_metth Methyl-coenzyme M reductase I subunit gamma Coenzyme-B sulfoethylthiotransferase gamma mcrG MTH_1165 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MAQYYPGTSKVAQNRRNFCNPEYELEKLREISDEDVVKILGHRAPGEEYPSVHPPLEEMDEPEDAIREMVEPIDGAKAGDRVRYIQFTDSMYFAPAQPYVRSRAYLCRYRGADAGTLSGRQIIETRERDLEKISKELLETEFFDPARSGVRGKSVHGHSLRLDEDGMMFDMLRRQIYNKDTGRVEMVKNQIGDELDEPVDLGEPLDEETLMNKTTIYRVDGEAYRDDTDAVEIMQRIHVLRSQGGYNPE mcrb_metth Methyl-coenzyme M reductase I subunit beta Coenzyme-B sulfoethylthiotransferase beta mcrB MTH_1168 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MAKFEDKVDLYDDRGNLVEEQVPLEALSPLRNPAIKSIVQGIKRTVAVNLEGIENALKTAKVGGPACKIMGRELDLDIVGNAESIAAAAKEMIQVTEDDDTKVELLGGGKRALVQVPSARFDVAAEYSAAPLVTATAFVQAIINEFDVSMYDANMVKAAVLGRYPQSVEYMGANIATMLDIPQKLEGPGYALRNIMVNHVVAATLKNTLQAAALSTILEQTAMFEMGDAVGAFERMHLLGLAYQGMNADNLVFDLVKANGKEGTVGSVIADLVERALEDGVIKVEKELTDYKVYGTDDLAMWNAYAAAGLMAATMVNQGAARAAQGVSSTLLYYNDLIEFETGLPGVDFGKVEGTAVGFSFFSHSIYGGGGPGIFNGNHIVTRHSKGFAIPCVAAAMALDAGTQMFSPEATSGLIKEVFSQVDEFREPLKYVVEAAAEIKNEI o27601_metth MTH_1559 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MEVIIMEYVKNVVCPFCGTLCDDIICKVEGNEIVGTINACRIGHSKFVHAEGAMRYTKPLIRKNGEFVEVSYDEAIDKAAKILAESKRPLMYGWSCTECEAQAVGVELAEEAGAVIDNTASVCHGPSVLALQDVGYPICTFGEVKNRADVVVYLGCNPMHAHPRHMSRNVFARGFFRERGRSDRTLIVVDPRKTDSAKLADIHLQLDFDHDYELLDAMRSCLLGHEILYDEVAGVPREQIEEAVEVLKNAQFGILFFGMGITHSRGKHRNIDTAIMMVQDLNDYAKWTLIPMRGHYNVTGFNQVCTWESGYPFCVDFSEGEPRYNPGETGANDLLQNREADSMMVIASDPGAHFPQRALERMAEIPVIAIEPHRTPTTEMADIIIPPAIVGMEAEGTAYRMEGVPIRMKKVVDTDLLSDREILEKLLEKVREYKASK o27599_metth MTH_1557 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MEYIIKNGFVYCPLNNVDGEKMDICVKDGKIVESVSDSAKVIDASGKMVMPGGVDPHSHIAGAKVNVGRMYRPEDSRRDAEKFRAGRAGSGFSVPSTFMTGYRYAQMGYTTAMEAAMPPLLARHTHEEFHDTPIIDHAAYPLFGNNWFVMEYLKDGDVDACAAYASWLLRATKGYAIKIVNPAGTEAWGWGGNVHGIYDPAPYFDITPAEIIKGLAEVNEKLQLPHSIHLHCNDLGHPGNYETTLASFDVPKNIKPDPATGERDTVLYATHVQFHSYGGTTWRDFVSEAPKVADYVNRNDHVVIDVGQITLDETTTMTADGPMEYDLHSLNGLKWANCDVELETGSGVVPFIYSARAPVPAVQWAIGMELFLLIDDPGKVCLTTDSPNAGPFTRYPRVIAWLMSNKYRMNLIEGELHKWAQRKSTIATIDREYTFSEIAQITRVTSAKVLGLSETKGHLGAGADADIAVYNINPETVDPSADYMAIEEGFSRAAYVLKDGEIVVKDGEVVASPHGRTYWIDTQVDESLYNEVLASVESKFKQYYSVNFANYPVQDEYLPKSAPVKGVML mcrx_metth Methyl-coenzyme M reductase II subunit alpha Coenzyme-B sulfoethylthiotransferase alpha mrtA MTH_1129 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MDEKKLFLTALKKKFEVEDPDEKYTNFYCFGGWEQSARKKEFTEYAKKAAEKRGGIPFYNPDIGVPLGQRKLMAYRVSGTDAYVEGDDLHFVNNAAIQQMVDDIKRTVIVGMDTAHAVLEKRLGVEVTPETINEYMEAINHALPGGAVVQEHMVEVHPGLVEDCYAKIFTGDDNLADELDKRILIDINKEFPEEQAEQLKSYIGNRTYQVNRVPTIVVRTCDGGTVSRWSAMQIGMSFISAYKLCAGEAAIADFSYAAKHADVIEMGTIMPARRARGPNEPGGVAFGTFADIVQASRVSDDPAKISLEVIAGAAALYDQVWLGSYMSGGVGFTQYATAAYTDDILDDFVYYGMEYVDDKYGICGTKPTMDVVRDISTEVTLYSLEQYEEYPTLLEDHFGGSQRAAVAAAAAGCSTAFATGNSNAGINGWYLSQILHKEAHSRLGFYGYDLQDQCGASNSLSIRSDEGLIHELRGPNYPNYAMNVGHQPEYAGIAQAPHAARGDAFCTNPLIKVAFADKDLSFDFTSPRKSIAAGALREFMPEGERDLIIPAGK mcrz_metth Methyl-coenzyme M reductase II subunit gamma Coenzyme-B sulfoethylthiotransferase gamma mrtG MTH_1130 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MTYKAQYTPGETQIAENRRKHMDPDYEFRKLREVSDEDLVKVLGHRNPGESYKSVHPPLDEMDFEEDIVRDMVEPIQGAKEGVRVRYIQFADSMYNAPAQPYDRARTYMWRYRGVDTGTLSGRQVIEMRELDLEGVSKELVETELFDPATTGIRGATVHGHSLRLDENGLMFDALQRYVFDEEKGHVVYVKDQVGRPLDEPVDMGQPLGEDELKKITTIYRKDNIAMRDDKEAIEVVENIHTGRTMGGFGMDVFKDDLRKRLGDD mtrd_metth Tetrahydromethanopterin S-methyltransferase subunit D N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit D mtrD MTH_1162 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MDPLLLIGAITAGGVLIGGGVHFVPVGGAPAAMATATGVGTGTAMLAAGAGLTGLITAAAMTGQSPLMIMAAGAVGSMLMIGITMLVGNLIYVYGVGTVPVSAKVAVDPLTGMEQEKYVTPGTEGHGLPTVCFVSGIIGGALGGIGGGLIYWALNEALKTLSYGAIGAAGVAAIFAVGIFFINAVIASYNIGGTIEGFHDPKFKRIGRGIVACLIASIVAGALSTLLVYGGVF mtre_metth Tetrahydromethanopterin S-methyltransferase subunit E N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit E mtrE MTH_1163 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MDPMITGLGVVALMGAAATIAGAAEDLESDVGSQSNPNSQVQLAPQMGHLHRIINKAVSGEPVAYGTWCGIAGSVAYVLMQSMQLPVIMAIAVGAVIAAMVHTTYAVTSHMGRIVSQSQFNQPLFMDMLVQHLGPIAGHGFIVTFCIVGLSYLMTLPIPGFAHPFPLPLLAVLWGITIGAIGSSTGDVHYGAEREYQQYPFGGGIPVAIHGDITTKAELGARNSMDVVHFCAKYGGPLTGFAFGAIVFLSFWNTIVFGITGGIISGLIIVLLLIILNNRLEVFARNRYGPYKEDE mtrh_metth Tetrahydromethanopterin S-methyltransferase subunit H N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit H mtrH MTH_1156 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MFRFDKEQIVLDIAGTKIGGQPGEYPTVLAGTIFYGGHSIIEDEKAGVFDKDKAEALIKTQEEMSDVTGNPHIVQTFGQTPEAIVKYLEFVGDVTDAPFFIDSTSGEARIAGANYASEVGLEDRAIYNSVNMAADEAELEALKETKLSASIVLGFNPMDPTVDGKIGIWEDGAGTIDKGLLEMAAECGIDKYLMDVAVTPLGQGAGVAVRTSFAVKSKWGYPVGSGIHNVPSAWDWLREYKKDHKEAWPVCDVGSNLIQQMAGGDFVLYGPIENAKMAFPACAMADIFISEAAKDIGTEPVEDHPFFKLL fwdc_metth Tungsten-containing formylmethanofuran dehydrogenase 2 subunit C Tungsten-containing formylmethanofuran dehydrogenase II subunit C fwdC MTH_1558 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MSEIILTPKEQPEVPLEAPNIKPDVFAGKSIDEIRNIQIMHGNEVVKLGDFFEVSGEPADSAADIKIIIDGDVYNTKRIGQDMTAGEILVKGNVNMYVGAGMKGGKITVEGNAKSWAGQDMRGGELEIFGDAGDYVGSSYRGDWRGMSGGVITVHGNAGNEIGEYMNGGKIIIKGDVNIMPGIHMNNGLIIIEGNAVARVGGEMAGGTIVVKGMIEEFLPGFKYLGVEKDIEVNGETFPGAYYKFEGDHAIKGAKGMVYAAVGCNGHIEP mtrc_metth Tetrahydromethanopterin S-methyltransferase subunit C N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit C mtrC MTH_1161 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MSVAAGGPAGAAIPESRLMALGIIGGLGGIYASTVNPVIGPVFASLGAVCAIIWGADAIRRVASYGLGTGVPSIGYMSVSIGIVGVVAGLASVFTLPALAAPVVGLILAMILGVVVAVLGKKIVKMKIPILEKCTAEISGAAALSVLGFSAAIAGSYTMQAVLTSVIATGFIGLLFILNTMAIQHPFNACLGPNENQTRTLKLAASTGFISMAIAGLLGIGLNPGWWLVSLVGALCWVVAFKSFVSASFEEAASVKWSGLWPKEEEQ mtrf_metth Tetrahydromethanopterin S-methyltransferase subunit F N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit F mtrF MTH_1158 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MIILSNKPNIRGIKRVVEDIKYRNQLIGRDGRLFAGLIATRISGIAIGFLLAVLLVGVPAMMSILGVI mtrg_metth Tetrahydromethanopterin S-methyltransferase subunit G N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit G mtrG MTH_1157 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MSEEDKTTIPRVLVSADEFNKANERLDDIEEKVEFTVGEYSQRIGQQIGRDIGILYGIVIGLIILAVTNILFAGLLKGLLKSLFGL mtra1_metth Tetrahydromethanopterin S-methyltransferase subunit A 1 mtrA1 N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit A 1 MTH_1159 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MVEKKSPAEGWPVVNGDYIVGDPESPVAATTLASHIEDVPVEAGAAIAGPCKTENLGIEKMIANLISNPNIRFLILCGSEVQGHITGQSIEALHQNGVDPDKRNIIGATGAIPYIENIPDEGIERFQKQLEIVNLIDVEDADAIKAKVKECIEKDPGAFEEEAMVIKVEEGGEEEEGEEVKPVAPETALIEARMRNIQTQVKMIGSTNRMFAGMYSGKVQGIMIGLAFTLTLGILLLV mvha_metth F420-non-reducing hydrogenase subunit A Methyl viologen-reducing hydrogenase subunit alpha mvhA MTH_1134 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MVKLTMEPVTRIEGHAKITVHLDDAGNVEDTRLHVMEFRGFEKFLQGRPIEEAPRIVPRICGICDVQHHLAAAKAVDACFGFEPEDVLPAAYKMREIMNWGSYMHSHGLHFYFLAAPDFIAGKDRKTRNVFQIIKDAPDIALQAIELRKNALELVRATGGRPIHPTSSTPGGISTELDDETQKDLLKKAQRNVELAEATLELAVPIFEENIDLVNSLGNIETYHTGLVKDGVWDVYDGIVRIKDKEGNMFREFKPADYADTIAEHVKPYSWLKFPYIKDLGYPDGVYRVSPLSRLNVADKMPDAAPKAQEHFKEFRENFGYAQQTLLYHWARLIELLACAECAADALEGDLSGEKFPDSLERQAGDGVGIVEAPRGTLTHHYTCDENGLITKANIVVATIQNNPAMEMGIQKVAQDYIKPGVEVDDKIFNLMEMVIRAYDPCLSCATHTIDSQMRLATLEVYDSEGDLVKRI hdrb_metth H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit B hdrB CoB--CoM heterodisulfide reductase subunit B MTH_1879 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MEIAYFLGCIMNNRYPGIEKATRVLFDKLGIELKDMEGAFCCPAPGVFGSFDKTTWAAIAARNITIAEEMGSDVMTECNGCFGSLFEANHLLKEDEEMRAKINEILKEAGREYKGEINVRHLAEILYNDVGLDKLSEVVEKPLNLNVAVHYGCHFLKPSEEINIDNPERPTILDELVEVTGAKSVDYKDKMMCCGAGGGVRSRDLDVALDFTMEKLRNMKEAGVDAIVNVCPFCHLQFDVGQMEIKDKFGEEFDIPVLHLAQLLGLAMGLPKEDLVVDAHQVCVDECLEKLEELDRLAPGSG hdrc_metth H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit C hdrC CoB--CoM heterodisulfide reductase iron-sulfur subunit C MTH_1878 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MTLLQREENIIRKGNIDKEFSEKIKAAGGDSLEYCFQCGTCTGSCPSGRRTPYRVRQIIRKANVGLKDEIISDPALWMCTTCYSCQERCPRKVKIVDVVKLARNEAAKAGFMAPAHKAVGSFVIKTGHGVPINDATMELRKAVGLGELPPTTHQFPEALEEVQKIIKATGFDQLIGYNWETGELE hdra_metth H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit A hdrA CoB--CoM heterodisulfide reductase iron-sulfur subunit A MTH_1381 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MAEEKKEETMEEPRIGVYVCHCGVNIGGVVDIEAVRDYAAKLPNVVVSKDYKYYCSDPGQLEIQKDIKELGLNRVVVAACSPRLHEPTFRRCVEEAGLNQFLFEFANLREQDSWVHMDDPEGATEKAKDLVRMAVAKARLLEPLEASKVSVDDKALVIGGGVAGIQTALDLADMGFKTYMVEKRPSISGRMGQLDKTFPTLDCSMCILAPKMVDVGKHDNIELITYAEVKEVDGYIGNFKVKIEKKPRYIDEDLCTGCGSCVEVCPIEMPNYFDEGIGMTKAVYIPFPQAVPLCATIDKDYCIECMLCDEICERGAVKHDQEPEEIEIEVGTIIVATGYDAYDPTEKLEYGYGRHTNVITGLELERMINASGPTDGKVIKPSDGEKPKRVAFIHCVGSRDEQIGKPYCSRVCCMYIMKNAQLIKDKMPDTEVTLYYMDIRAFGKGFEEFYKRSQEKYGIKFIRGRPAEILENPDLTLTVRSEDTLLGKVTEYDYDMVVLGVGLVPPEGSEKLRQTIGLSKSADGFLMEAHPKLRPVDTLTDGVYLAGVAQGPKDIPDAVAQASGAAARAAIPMVKGEVEIEPIVAVTDSDVCGGCEVCIELCPFGAISIEEGHANVNVALCKGCGTCVAACPSGAMDQQHFRTEQIMAQIEAALNEQAK frhb_metth Coenzyme F420 hydrogenase subunit beta 8-hydroxy-5-deazaflavin-reducing hydrogenase subunit beta frhB MTH_1297 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MVLGTYKEIVSARSTDREIQKLAQDGGIVTGLLAYALDEGIIEGAVVAGPGKEFWKPEPMVAMTSDELKAAAGTKYTFSPNVLMLKKAVRQYGIEKLGTVAIPCQTMGIRKAQTYPFGVRFVADKIKLLVGIYCMENFPYTSLQTFICEKLGLNMELVEKMDIGKGKFWVYTQDDVYTLPLKETHGYEQAGCKICKDYVAELADVSTGSVGSPDGWSTVITRTDSGDSILKQAVEAGIFETKPIEEVKPGLGLLEKLSAQKKEKAEKNIAARKEMGLPTPY frhg_metth Coenzyme F420 hydrogenase subunit gamma 8-hydroxy-5-deazaflavin-reducing hydrogenase subunit gamma frhG MTH_1298 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MAEENAKPRIGYIHLSGCTGDAMSLTENYDILAELLTNMVDIVYGQTLVDLWEMPEMDLALVEGSVCLQDEHSLHELKELREKAKLVCAFGSCAATGCFTRYSRGGQQAQPSHESFVPIADLIDVDLAIPGCPPSPEIIAKAVVALLNNDMEYLQPMLDLAGYTEACGCDLQTKVVNQGLCTGCGTCAMACQTRALDMTNGRPELNSDRCIKCGICYVQCPRSWWPEEQIKKELGL mvhd_metth F420-non-reducing hydrogenase iron-sulfur subunit D Methyl viologen-reducing hydrogenase subunit delta mvhD MTH_1136 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MAEDDIKIVMFCCNWCSYGGADTAGTARMQYPTNIRVIRVMCSGRIEPQFVLKAFREGADGVLVTGCHHGDCHYDAGNYKLDRRMRLIYKLADELGIGRERIHHDWISASEGEKFAETVKMMVNRIKDLGPSPIKKQLAEA mvhg_metth F420-non-reducing hydrogenase subunit G Methyl viologen-reducing hydrogenase subunit gamma mvhG MTH_1135 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MAEKIKIGTMWLGGCSGCHLSIADFHEKIIDVMEHADFEFSPVLMDTKYDEIPELDVVIIEGGIVNDENREFAEELREKAKFVISYGTCAVYGGIPGLRNLWDKDEVIEEAYINSITTPNEEGVIPSEDVPHLEGRVKPLGEVIDVDFEVPGCPPRSDVAAEAVMALLTGEEIELPETNLCEVCPREKPPEGLAMDFIKRQFEVGKPEDDLCLIPQGLICMGPATVSICGAECPSIAIPCRGCYGPTARVEDQGAKMISAIASDYKVEEDKTVDPEEVAEQLDDIVGTFYTFTLPAALIPMKIQKEGK vatb_metth V-type ATP synthase beta chain atpB MTH_954 V-ATPase subunit B protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MNVNIKTREYTTVTEVSGPLMIVEGVEGVAYSEIVEIETPTGEKRRGQVLEVREDLAVVQVFEGTSDLNTETTKIRFTGETAKIGVSLDMMGRIFDGTGKPIDGGPEIIPEKELDINGSPMNPAAREFPAEFIQTGISTIDGMNTLVRGQKLPIFSGSGLPHNELAAQIARQAKVLAEESEFAVIFAAMGITHEEANYFMRDFERTGALERVTVFMNLADDPAIERIITPRMALTTAEYFAFEHDMHVLVILTDLTNYCEALREISAAREEVPGRRGYPGYMYTDLASLYERAGRIVGKEGSITQMPILVMPQDDITHPIPDLTGYITEGQIVLSRDLHRKGIYPPVDVLPSLSRLMSGGIGEGRTREDHSGVSDQLYSAYAEGRDLRDLMAVVGEEALTERDRKFLKFADEFEKRFITQARDEDRSIEETLNLGWELLSLLPRSELKRVREEHIPKYLPGAE vatd_metth V-type ATP synthase subunit D atpD MTH_953 V-ATPase subunit D protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MAQEMIEGINPTRMELLKLKQREKLAVKGYSLLKEKRNALIMEFFNILERVKGSREKVEEHLKEAFSDLTEAQVLMGDTAVERAAMSVRESVEVDIDSRSIMGVVVPVVDARATQRTVVERGYGLVDTSVKLDEAARKFEESLALIIELGEIEKTIRLLAGEIESTKRRVNALEHIIIPRLKNTVKYIEMRLEEMERENFVRLKMIKKSMEME vatf_metth V-type ATP synthase subunit F atpF MTH_956 V-ATPase subunit F protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MSSNIAVVGDRDTVTGFRLGGVREGYVVETPDEAEETIRNLIRDGFSIIIVTEKIGDELREFIEETTSSSALPMIIEIPDKTGPSERETDPLRDLIKRVIGVEMVK frha_metth Coenzyme F420 hydrogenase subunit alpha 8-hydroxy-5-deazaflavin-reducing hydrogenase subunit alpha frhA MTH_1300 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MSERIVISPTSRQEGHAELVMEVDDEGIVTKGRYFSITPVRGLEKIVTGKAPETAPVIVQRICGVCPIPHTLASVEAIDDSLDIEVPKAGRLLRELTLAAHHVNSHAIHHFLIAPDFVPENLMADAINSVSEIRKNAQYVVDMVAGEGIHPSDVRIGGMADNITELARKRLYARLKQLKPKVDEHVELMIGLIEDKGLPKGLGVHNQPTLASHQIYGDRTKFDLDRFTEVMPESWYDDPEIAKRACSTIPLYDGRNVEVGPRARMVEFQGFKERGVVAQHVARALEMKTALARAIEILDELDTSAPVRADFDERGTGKLGVGAIEGPRGLDVHMAQVENGKIQFYSALVPTTWNIPTMGPATEGFHHEYGPHVIRAYDPCLSCATHVMVVDDEDRSVIRDEMVRL vate_metth V-type ATP synthase subunit E atpE MTH_958 V-ATPase subunit E protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MSSGAEKIVSSIMSEAQAKADAIIREAEDEAAGIVDEGEKRARMASERILESARKQADMRYQQIISEAKMNARRAELEAREEVIQEAFKKAEEELKNLASTSQEEYVSALRGMIKEAAVEIGGGDLVVSMREDDRSLDLGLDKIAAEVEAETGKKTTLKVGDSIRTIGGAVVRTEDGLIEVNNTIEARMSRFRKALRSEVARVLFE vati_metth V-type ATP synthase subunit I atpI MTH_960 V-ATPase subunit I protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MSDMFLPARMRKLKIITLDQYSDSVVRSLHEEGVTQIDDISERIQQDAEWRQILKPSRATPYTGRVSSLLMKTSGILDFLGSVAAEEKGLRDTIREFINPPIFEKREVEELDTESLIERAEETLGRVESETRVMEEKLNELDSERSAVESSLSVAEKLKDFDIDFSDLQDSEYITGIAGRITAENLPELRDKLADITDELVISDREGENKAERILIIVTLKKHADSIASVLRRMEFERFEISELQGRPSEIISSSKTRLEEISRERKEIISKLRDINAEWEDELLVLREQLEIEKERNEVFSLFGETRKTVMLEAWVPLKEADRVIAVVEESSEGTALTDLEDPDPEEVPVLLDNPRFAKPYETFVEMYSPLKYNEIDPTIFMAFVFPFFFGFCLTDAGYGIIDALIGFILYRGLGKVNNFMRNFGIIMMSCGVWAFILGMVTNGFIGDFFPRFFNITLPTVIPAIDAFVNPQNILIMALTVGVLHINFGLILGARNNIRLGNMREALGSQIVWLILELGIILYLVGGMIFGAPLIILAFAMLLYYNGLFGLMDVSGFLGTLLSYARLLALCLSTGGIAMTVNILTGLSYEMIPVIGVVLAPIIFVFGHIANNAFQSLGAFINSLRLHYVEFFAQFYMGGKNKFNAFRAERNFTKIRR vatc_metth V-type ATP synthase subunit C atpC MTH_957 V-ATPase subunit C protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MADSITTIVTALGFPSIESFIGVLLLGGAIIGAIVVIATIRPILDLFPFAYPNARVRARIGRLLNEKQLSEILETESMEEFKNYLRGLPDYAKYIDRFPIEKALESQLAETYEMVSQIAPASIRDPFRANLKRWDVRNIKSLITAKAAGLSAEETVNLLVPGGEVYEIIEGLADASSVQEVVTGLEATEYAGVLEDALSGYEETGMLLPIEAALDRKFLEGLIRTVGSPSDDNTKILHTYFGTMVDISNLKIILRAKADGLSYDDISPYIVPHGYQIREWKLKDLMESEDVSGVVSGLEGTDYGQMLSEALSEYTSTGSVAVFERVLEDNLNRMARNFALKKPFGVGPMIGFLSRKEVEVKNLKVIARSKREPGFPEAMVKEMLA vata_metth V-type ATP synthase alpha chain atpA MTH_955 V-ATPase subunit A protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MTQEGRIIKIAGPVIIAEGMRGSQMYEMVKVGEDKLIGEIIELEGDTATIQVYEETAGIKPGETVERTGGPLSVELGPGILGSIFDGIQRPLENIKALTGDYIERGVDVPSLPKDKKWTFKPTAREGQMVKGGDIIGEVEETSSITHRIMIPPNVEGKLTMIAPQGEYTVLDDIAEVETESGTEKIQMLQKWPVRKGRPYKKKLDPDVPLVTGQRAQDTFFSVAKGGTAAIPGPFGSGKTVTQQQLAKWADADIIVYVGCGERGNEMTEVLKEFPELEDPKTGNPLMDRTVLIANTSNMPVAAREACVYTGITIAEYFRDMGYDVALMADSTSRWAEAMREISGRLEEMPGEEGYPAYLASRLAQFYERAGRVTTIGSEDKIASVSVVGAVSPPGGDLSEPVTQNTLRICKVFWALDASLADKRHFPSIDWLQSYSLYIDSVQEWWASNVDPEWRKFRDEAMALLQKEAELQEIVQLVGPDALPDRERITLETTRMIREDFLQQNAYHEVDTYCSPSKQFEMLRTIIMFHRNATAALEKGAPAADIISLPVKEDIGRMKYIPEEEFPARIKEIQERIVKECSEV acdg_metth Acetyl-CoA decarbonylase/synthase complex subunit gamma ACDS complex methyltransferase Corrinoid/iron-sulfur component large subunit cdhE MTH_1713 5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MQVTAMDVYRLLPKTNCGKCNEASCMAFATKLIEKEVTLDDCPQLSGDERQKLENLLAPAVKEITFGPEENQVVVGGDEVLYRYELTYYNPTALVVDLPDDLPSEELLNRAQRIMELEFERTGEKLTLDAIALRNRSGSPEKFAEAAEAISKLNFPVVLCTFDVEAMKAALEVLGDQKPLLYAAREDNLGEMAELSVSYGCPLVLFSPGDLEEMKNLSRRLRSLGVTEIVLDPGTFTGEGIGDTIDNFVMIRRLAVEDGDDDFRFPIMGIPALSRLTVSDKIEANIREATVAATLMNRYADILILAGTEIWEIMPVLTLRQGLYTDPRKPQAVDPGVYEFGDVDENSPVILTTNFSLTYYTVEGDLKSGDVTAYLLVLDTEGRAVDVSLAGGQLNGPAVADLIKETGIEERVRDKVMIIPGLAAPASGEIEDDTGWRVLVGPRDSSGIPDYLDKLASE acdb_metth Acetyl-CoA decarbonylase/synthase complex subunit beta ACDS complex acyltransferase cdhC MTH_1710 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MFEDIPVDVSPMHEGERIRSANMFVELAGPKSIGAELVQVKDEVEDGKVEVKGPEIDEMEQGQVYPFAINVEVAGSELEEELESVIERRLHELCNYVKGFMHLNQRDQIWCRVSTEAKDAGFRLEHLGKALSVLFREEFPIIESIAVTLMTDEAAVQEFLETAREKYETRDSRARELSDEDVDVFYGCLMCQSFAPTHVCIVTPDRTALCGAINWFDCRAAYKMDPDGPIFEIEKGEVLDPERGEYANVNAAVEENSQGTTDRVYLHSVFGYPHTSCGCFEAVAFYIPELDGIGIVNRDFRGETPLGIPFSAMAGQCSGGKQVEGFSGLSLEYMRSPKFLQADGGYHRVIWMPRELKESVLEFIPEDVRDKIATEEDATSIKDLRRFLRDNEHPVLERAAVEETEPEEEEVEEAYPEETPIPEGVPVMAAPEMTLPAAGGFRIVLKNAKIYAEKVIIKRK acda_metth Acetyl-CoA decarbonylase/synthase complex subunit alpha cdhA ACDS complex carbon monoxide dehydrogenase subunit alpha MTH_1708 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MIDVAPESKKAKDLKGDFWDAKNIQISIGEIITEEKPPEEEVKGPKPRPHVTDLRSWDMKLLERYEPFYAPFCDMCCLCTYGKCELLGKKGACGIDAATQQARTVLLACLIGTAAHAGHARHLVDHLIERLGEDYKIDLGSNVDIEAPITRTVMGKRPATLGDLREVMDYAEEQMSHLLSACHTGQEGDSKDFESKAFHAGLMDDLTREVADLAQIVALDLPKGDEDAPLVELGFGTIDTEKPVVLCIGHNVLPGADIVDYLDENEMEDQVEVCGICCAAIDVTRYNEAAKVVGPLSKQLRFIRSGVADVIVVDEQCVRTDVLEEALKNRSAVIATTDKMCLGLPDMTDEDPDKIVNDLINGNIEGALILDPEKVGEVAVKTAMKLAPIRKSLKKLPDIDEIIELASECTDCGWCQRVCPNSLPVMDAVKKAADGDLSKLEEMAIEELCYTCGRCEQECERNIPIVSMVTKAGERRVKDEKYRIRAGRGPAQDVEIRRVGAPIVLGDIPGVVAFVGCSNYPEGGKDVALMAKEFLERNYIVVTTGCGAMSIGEYRDEDGQTLYEKYGGQFDAKGLVNMGSCVSNAHVSGAAIKIANIFAQKPLEGNFEEIADYILNRVGACGVAWGAYSQKAAAIATGVNRWGIPVVLGPHGSKYRRLFLGRADDEEKWKLKDLRTGEVIDGEPAPEHLLYAAENREEATVMIAKLCIRPTDTPKGRQMKLSNYIDLHRKYLGTIPDDIDRFIRTEKDIPIVYKRDVMKILEEKNWKPRELPKEPSLLER o27042_metth MTH_961 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MIHMTTISEAITTIKKAENDADRLIQEAREKSSQLLDDARNRSAELLEKAEREASEKGDEIIAEAEERARKEAIEISGKAKREVETMKSAAMGKVPEAASIIVKSIL syfa_metth Phenylalanine--tRNA ligase alpha subunit pheS Phenylalanyl-tRNA synthetase alpha subunit MTH_742 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MMDLDRIIDQLHIYEKKVLKAFEGSDKPLKPEEIAESQKIDIKSVMSASGALESRGFVRVMKDADEVVSLTEDGESCAREGLPERRLIEALKGEEELEMSELSRRAGLDKKEAGIGIGWLMRKGWGRISQGMVSAVSDETPERGADERLLELLLERGSVRIRELPDELRGALKDLKGRKGIVDIRKIKRHTIELTTEGRKLLERGIEIVEEATQVTHEHLKSGAWRKLHYRGYNIDAEYPLVYPGKMHPLRRIIDEIRSIFLKLGFTESRGPIVESAFWNFDCLFQPQDHAAREMQDTFYVKNPAVTDLPCEDLVRAVQDAHETGGSTGSEGWQYEWDRDVARQSVLRTHTTCVSARFLSENEPPLKMFSVGRVFRRETITYKHLPEFHQVEGIVAGDEVNFRNLLGILREFYRKLGFEVRFRPAYFPYTYLSTECEIYLPEKKSWIELGGAGMFRPEVLEPLGVETPVAAFGLGIERLAMIRFDIKDIRMLYQSDLGWLRGLPVTGDLEL syfb_metth Phenylalanine--tRNA ligase beta subunit pheT Phenylalanyl-tRNA synthetase beta subunit MTH_770 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MPVITFDYDDLKELGIDIDREKLLDVLPMMGSDIEDFDDESIKVEFFPNRPDLLSVEGVARSLRGFLGIEKGMPSYDVHDSGVEVTVDESVLDVRPYLGMAVIEDVQFTDKKLKQVMEFQEDLHWVIGRDRRKVAIGIHDLDRVEPPFLYSGVEPEGVTFTPLDSVCEMTPHEILEEHPKGVSYAHLLRDHDRYPLITDKNGDVLSMPPIINGELTKLTVNTRRILVDVTGTDDRAVRQTLNIICTSFAEAGGRIGSVRVKRPDGELHLPDLTPREMRVSVSEASRITGLELSADEVMDLLMKARMDARRTSDDEVVAVIPAYRVDILHEVDLVENIAVQHCIGRIEPELPDIATIAEEDTWSRADASIREVMVGLGFQEVMSLMLTSEESHYRRMRLEEDERVEVAQPISQDRTMIRKSLLNGLLEFFEDNKHEDLPQKIFEVGDVVYINPESETRSRVVTKLACAVTHSSAGFTEIKSLAAAVVENLGYEFRIEPLEHPSFIEGRCAAIESEGKSSAIGGFFGEVHPEVVTNFNLEYPVIALEIEFK y792_metth UPF0219 protein MTH_792 MTH_792 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MAGIVGYGVYIPSYRIKVEEIARVWGDDPQAISRGLVVEEKSVPGPDEDTATISVEAARNALRRSQIDPSEIGAVYVGSESHPYAVKPTATIVAEAVEATPEMTAADLEFACKAGTAGIQACMGLVDSGIIKYGLAVGADTAQGAPGDALEYTASAGGAAYVIGGKNCLADIKETYSFTTDTPDFYRREGMPYPRHGGRFTGEPAYFKHVLGAARGMMEKTGLSADDFDYAVFHQPNGKFYLKAARKLGFESEQVKPGLLTPVIGNTYSGATPVGLAATLDVAEPGARILAVSYGSGAGSDAFIIEVNDLIEERRDLAPSVAEIIKNKRYVDYALYAKFKGKLRMA y793_metth Uncharacterized protein MTH_793 MTH_793 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MRDVAVIGVSQTKFGELWDVSFRDMITEAGLGAIEDAGVEGADLDAMYVGNMSAGLFIKQEHISSLIADHAGLTPIPSTRVEAACASGGLALRSGIMAVASGYHDIVIAAGVEKMTDVVDPTPAIATASDQEWEAQQGVTFPSLYAMMARRHMYEYGTTREQLAMVSVINHENASNNPRAQFPMKVTVEQVMNSTMVADPLRLLDCSPISDGAAAVILCPADMAREYTDTPVYVKASAQASGTIALHDRRDITRIDATVNAARNAFKMAKLTPGDIDLVEVHDCFSINGILAVEDLGFVEKGEGGRAFEDGMTRIDGDIPVNPSGGLKARGHPLGATGIAQAAEVVWQLRGEAGKRQVEGAEIGMTHNIGGTGGTAAVHIFSR psb_metth Proteasome subunit beta 20S proteasome beta subunit psmB MTH_1202 Proteasome core protein PsmB protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MNDKNTLKGTTTVGITCKDGVVFATERRASMGNLIAHKATDKIFKIDEHIAATIAGSVADAQSLMKYLKAEAALYRMRNSEKISIEAAAALAANILHSSRFYPFIVQTLLGGVDENGAKIYSLDPSGGMIPDKFVSTGSGSPVAYGVLEDRYSDELYVDEAVDVAIRAIKSAMERDTYSGNGILVATVTEEEGFRMLSEEEIQKRIENLN psa_metth Proteasome subunit alpha 20S proteasome alpha subunit psmA MTH_686 Proteasome core protein PsmA protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MQPLQSAGYDRAITVFSPDGRLFQVEYAREAVKRGTTSLGVKSKEGIVLVVDKRPTSKLVEPKSIEKIFQIDEHIGAATSGLVADARAIIEKARLEAQINRITYNEPIRVESLAKKICDMKQMYTQHGGVRPFGTALIIGGVNGRGCRLFETDPSGALIEYKATAIGAGRPAAMEEFEKKYSDDMNLNQAIELALDAVYEATEGKTTPESVEIAVIEAADKKYRRLPDDEIRDHVEELLIRKEKEEEE yb50_mettw UPF0051 protein MTH1150 homolog ORF2 protein protein mettw Methanobacterium thermoautotrophicum (strain Winter) MLRDTLKKAEKARDKKALYGEDIDLERFIKEEAGEHEEVPRAREVPKKVQETLLKVGVDPEERERAGTFIQVDQSGICTTCASESIEIMGMNVALDRYSWLKDYMWKAVAVDTDKYTATTALREAEGEMGGYFIRSMPGSREVFPLQACMFIGDENVMQTAHNIIIAEENSELHIITGCATGQDVSSALHVGVSEFYLKKGAKITFTMVHNWAEQVEVRPRTGIMVGDDATYISNYILTSPVKSIQSYPTAYCTGENSRVVFQSILGGQKDSVLDMGSRVILEGRGSSAEMVSRAVSKDASQIYSRGHLAGRVPEVKGHLECHGLVLSDDSMIYAVPELEGSATELEMSHEAAVGKIAEEEVMYLTSRGLTEDEAASMIVRGFLSMDITGLPPELAAETKRMLDMSLKGM o27217_metth MTH_1149 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MLLEITDLAVEVSGKQVLKDIDLYIDRGETHVLLGPNGSGKSTLFMTILGFPKYRVTNGQIIFKGEDITDLSTTERVRMGIGVSFQNPPAIRGVKLMDLLKVESGLETEDELTPELRGLAAKMKFDESFLERDVNLGFSGGEVKRSEILQLLAQKPDFIMFDEPDSGVDIENVELLAEEINVLLDKDKKPGLRKKAGLLITHLGYILNFVSADTAHVLMDGRIACSGNPQEIIEDIRKDGFKGCVECCGIH dnag_metth DNA primase DnaG dnaG MTH_891 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MGKEEISTTKYLIHAQINANGIVEKPDVVGAIFGQTEGLLSNDLDLREFQKTGRIGRIKVNITSRGGKSKGEIIIPSSLDRVETAILAASLETINRVGPCEAYIQVTKVEDVRAVKRKRVVERAKEIYASMMEEVTPESLKMIEEVKEAMRVHEITEYGEEKLPAGPNVETSDAILVVEGRSDVLNLLKYGIKNAIAVEGVSVPKTVADLTRKKTVTAFVDGDRGGELILKELLQVGEIDYVTRAPKGKEVEDLEKDEIMMALRNKVPVEQFYHDLGMKKEKKKTEDKMVLLRNILKELEGTGNAEILDDALNILREVKVENLYDELSRVNNHPYAVVFDGVITQRLVDLSFEKGLRYLVAVRSGDIVKKPHNLKLITGHT enda_metth tRNA-splicing endonuclease tRNA-intron endonuclease endA MTH_250 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MRVEGQLGDEVVTIKATSIARRLHGKSHYGKMYEDRLQLSLIEAAYLMERGKLKLMKDDDEVSPEEFISLLGERGLYSKYLVYRDLRNRGYIVKTGFKYGAEFRLYERGGAPGRTHSAYLVRVISENDTIHALDFSSYVRVAHGVNKKLLMAFLDDEEDITYYLVDWIRP rad50_metth DNA double-strand break repair Rad50 ATPase rad50 MTH_540 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MIIRSLELKNIRSYESGRVEFDDGVTLFEGDIGSGKTTLLLAVEFALFGLGDQRGDSLLRATSNSGSVKLTFTVDGEEYTVYRELKRGSSGVQQGELYIRKQGVVKKLSAKELKAEVLEILGYREPLNPRARSRIYRYAVFTPQEQMKSIIEAPKNDRLERLRKAFDLEKYSRAADNANLVSRRIRRESESLEDRSYDLEDKKRELEGLLGEKEKLESEKKQLDSDIEGIEAEIAKLKSEMEVLQREKNRIESAEREIESLQNEIETLRSSSERLMERNRSIEEEYRRSLDELQKCSDIREKLQEELNSLGERISALELKRESLMDDSRRFREASIQYRNLVSELENLIKTGRDLEDEISGLEDYTDRIKSKIESMESIEDPGYTEDEVEAGIRKLEVEVSDLQQELGGIHGKIEDYESIGRRGVCPTCDQEVNPDYINDKLSSARERKGSVESRIADLRNEIMNKNELMKRIAEYKRSREELRLLREDLEKRIKECHRRRESLDNIRERIRQIEEGKAESEKLIEELKDAESDFNKVEHELKSLREMESGYSSKLAAASGRMDQLRTRITELNPETSREYRDNLKKIDENESNIAEKRAKIRENEEALKNRDEVESSIHDLTQSICEMENLRDEKRDRRAAVEGKIEEKQRQIGNLESEIAKKRELRKRARELGNYVTWLNEYFIPAMDDIETHVMAQINHEFNERFQKWFRVLVDDPGKSVRIDEDFTPIVEQDGYEQNLEYLSGGERTSIALAYRLALNMVVQRLTDVRSDILILDEPTDGFSKEQLYKLRDIFDELESRQIILVSHEEELENLADHIYRVEKSDGTSIIEKTG pan_metth Proteasome-activating nucleotidase Proteasomal ATPase pan MTH_728 Proteasome regulatory ATPase Proteasome regulatory particle protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MENNSQNVLKKIEDLKKEVRMLKEENSKTKRNLMWKIRKLEKDKLLIENERTRLDREVKSLRGEIERFRTPPLVIATVTEVLDDHRVAVKSTTGPHFVINYSRFIDRKQLEPGARVALNQQTFSIVDVLPSEKDPVVTGMEVEEKPDVSYEQIGGLEEQVREVKETVELPLKKPELFEKIGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIKIVASEFVRKYIGEGARLVRGVFELAKEKSPSIIFIDEIDAVAAKRLKSSTSGDREVQRTLMQLLAELDGFESRGNVGIVAATNRPDILDPALLRPGRFDRFIEVPLPNEDGRREILKIHTSGMALAEEVDIELLARITDGASGADLKAICTEAGMFAIRDERDEVTMADFMDAVDKIMGVEKEEEYKQETGVMFG rrp4_metth Exosome complex component Rrp4 rrp4 MTH_684 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MLLVNEKDLVVPGQVLAENEYFPGRGTFKEDNRICSSFVGLVSVRNKKINVIPLQSKYIPKRGDVVIGEITDIRFSMWGLDINSPYTGLLPASEVFGKDKRELESVFDIVDVLLLRVVDVDEVKKVKLGLKGRGLGKFRDGILVYITPTKVPRLIGKRGSMINMVKEKTHCDIVVGQNGVVWIKGEPDMERIAEKVVLMIDREAHTSGLTDRVRELLDRLTGVEPEIQVEESEGTEKPETPESEDFEEASDYSEDVEVSPESEDIEEVSDESEDLEVESEDVEEGTDTPAAEEDDGEAGDAEVKDENNSER rrp42_metth Exosome complex component Rrp42 rrp42 MTH_682 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MVNKMDIIPEITRKSITDLINNKERIDGRSLHEFRDISIETGVISKAEGSSRVKLGNTQIIVGVKPQIGEPFPDTPEMGVILTNSELLPMASPTFEPGPPDERSVELSRVVDRCIRESRMIDLEKLCIIEGSKVWMLFLDLHIIDYDGNLFDAAVLATVAALLDTRIPAAEVEDGEVVINREKMQPLPVNRKALMCTFAKIGNEIVLDPSLEEEDILTARISIGVTEEGSICAMQKGGEGPLTRDDVLKAVSIAVEKVPQLIEYLDKSMTP rrp41_metth Exosome complex component Rrp41 rrp41 MTH_683 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MITIITQDQLKTSPSVREDGRAFDELRPLKIEAGILERADGSSYLEFGGNKILVAVYGPREAQIRKLQRPDRAVIRCRYNMAPFSVEERKRPGPDRRSVEISKITAEALRPALILEKFPRSVIDVFIEVLEAEGGTRCAGITAASVALADAGIPMRDMVVACAAGKVGDQVVLDLSEEEDKEGQADVPVAILPRTREITLLQSDGNLTPEEFERALDLAVEGCLRIHEVQKEALRKRYGE mth579-mth579 Fructose-1-6-bisphosphate aldolase complex 256311 N/A 256312 unspecified role unspecified role neutral component neutral component Stoichiometry: 10.0 physical association physical association false false false The Fructose-1-6-bisphosphate aldolase homomeric complex was reported as having 10 subunits A 300kDa Fructose-1-6-bisphosphate aldolase homomeric complex was detected. Reaction catalsed by complex D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate annotated by amino acid sequence similarity to characterised proteins in other species. mth632-mth632 Putative phosphofructo-(sugar) kinase complex 256311 N/A 256313 unspecified role unspecified role neutral component neutral component Stoichiometry: 10.0 physical association physical association false false false Putative phosphofructo-(sugar) kinase homomeric complex was reported as having 10 subunits A 700 kDa putative phosphofructo-(sugar) kinase complex was detected. Annotated by amino acid sequence similarity to characterised proteins in other species. Function unknown. mth744-mth744 Porphobilinogen synthase complex 256311 N/A 256314 unspecified role unspecified role neutral component neutral component Stoichiometry: 8.0 physical association physical association false false false Porphobilinogen synthase homomeric complex was reported as having 8 subunits A 300 kDa porphobilinogen synthase complex was detected. Annotated by amino acid sequence similarity to characterised proteins in other species. fpaa-fpaa Flavoprotein A1 complex 256311 N/A 256315 unspecified role unspecified role neutral component neutral component Stoichiometry: 4.0 physical association physical association false false false Flavoprotein A1 homomeric complex was reported as having 4 subunits A 150 kDa flavoprotein A1 complex was detected. Annotated by amino acid sequence similarity to characterised proteins in other species. mth1390-mth1390 Riboflavin synthase beta subunit complex 256311 N/A 256316 unspecified role unspecified role neutral component neutral component Stoichiometry: 50.0 physical association physical association false false false Riboflavin synthase beta subunit homomeric complex was reported as having 50 subunits A 800 kDa Riboflavin synthase beta subunit complex was detected. Annotated by amino acid sequence similarity to characterised proteins in other species. mtd-mtd F420-dependent methylenetetrahydromethanopterin dehydrogenase complex 256311 N/A 256317 unspecified role unspecified role neutral component neutral component Stoichiometry: 6.0 physical association physical association false false false F420-dependent methylenetetrahydromethanopterin dehydrogenase (MTD) homomeric complex was reported as having 6 subunits A 100 kDa flavoprotein A1 complex was detected. Annotated by amino acid sequence similarity to characterised proteins in other species. trpb2-trpb2 Tryptophan synthase beta chain 2 (TrpB2) complex 256311 N/A 256318 unspecified role unspecified role neutral component neutral component Stoichiometry: 2.0 physical association physical association false false false Tryptophan synthase beta chain 2 complex was reported as having 2 subunits A 100 kDa tryptophan synthase beta chain 2 complex was detected. Annotated by amino acid sequence similarity to characterised proteins in other species. mth1512-mth1512 H(2)-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase homolog complex 256311 N/A 256319 unspecified role unspecified role neutral component neutral component Stoichiometry: 3.0 physical association physical association false false false H(2)-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase homolog homomeric complex was reported as having 3 subunits A 100 kDa H(2)-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase homolog complex was detected. Annotated by amino acid sequence similarity to characterised proteins in other species. unc_22mrcb Methyl coenzyme M reductase 1 complex 256311 N/A 256320 unspecified role unspecified role neutral component neutral component N/A 256321 unspecified role unspecified role neutral component neutral component N/A 256322 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 250kDa methyl coenzyme M reductase 1 complex was detected. Reaction catalsed by complex reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and an heterodisulfide. There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contains mostly MCR I. unc_22mrcb-1 Methyl coenzyme M reductase II complex 256311 N/A 256323 unspecified role unspecified role neutral component neutral component N/A 256324 unspecified role unspecified role neutral component neutral component N/A 256325 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 250kDa methyl coenzyme M reductase II complex was detected. Reaction catalsed by complex reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and an heterodisulfide. There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contains mostly MCR I. fwdc-mth1558 Tungsten-dependent formylmethanofuran dehydrogenase complex 256311 N/A 256326 unspecified role unspecified role neutral component neutral component N/A 256327 unspecified role unspecified role neutral component neutral component N/A 256328 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 100kDa tungsten-dependent formylmethanofuran dehydrogenase complex was detected. Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). Can only oxidise formylmethanofuran. This enzyme is oxygen-labile fwdc-mth1558-1 Methyltransferase complex 256311 N/A 256329 unspecified role unspecified role neutral component neutral component N/A 256330 unspecified role unspecified role neutral component neutral component N/A 256331 unspecified role unspecified role neutral component neutral component N/A 256332 unspecified role unspecified role neutral component neutral component N/A 256333 unspecified role unspecified role neutral component neutral component N/A 256334 unspecified role unspecified role neutral component neutral component N/A 256335 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 900kDa methyltransferase complex was detected. The complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin hdra-hdrb Heterodisulphide reductase complex 256311 N/A 256336 unspecified role unspecified role neutral component neutral component N/A 256337 unspecified role unspecified role neutral component neutral component N/A 256338 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 300kDa and a 400kDa heterodisulphide reductase complex was detected. a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B). Subunit A (O27434) may act as the catalytic subunit (By similarity). Cells cultured under MCR I conditions (N medium (15) at 65 �C with a gas flow of 2.0 liters/min of 80% H2, 20% CO2 (v/v) and harvested at an optical density at 600 nm of 5) had a 3-fold increase in the complex than cells grown under MCR II conditions (55 �C with a gas flow of 5.0 liters/min of 80% H2, 20% CO2 (v/v) and harvested at an optical density at 600 nm of 1.8). Auhors state that the higher molecular weight complex detected represented an association between of the heterosulphide reductase and methylviologen-reducing hydrogenase complexes. mvha-mvhd Methylviologen-reducing hydrogenase complex 256311 N/A 256339 unspecified role unspecified role neutral component neutral component N/A 256340 unspecified role unspecified role neutral component neutral component N/A 256341 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 100 kDa Methylviologen-reducing hydrogenase complex was detected. A complex that provides reducing equivalents for heterodisulfide reductase. MvhD may form the contact site to heterodisulfide reductase (By similarity). frhb-frhg F420 reducing hydrogenase complex 256311 N/A 256342 unspecified role unspecified role neutral component neutral component N/A 256343 unspecified role unspecified role neutral component neutral component N/A 256344 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 1000 kDa F420-reducing hydrogenase complex was detected. A complex that reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen. atpa-atpb A1 subcomplex ATP synthase complex 256311 N/A 256345 unspecified role unspecified role neutral component neutral component N/A 256346 unspecified role unspecified role neutral component neutral component N/A 256347 unspecified role unspecified role neutral component neutral component N/A 256348 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 400 kDa subcomplex of the ATP synthase complex was detected. A complex that produces ATP from ADP in the presence of a proton gradient across the membrane. atc-atpe-1 A0 subcomplex ATP synthase complex 256311 N/A 256349 unspecified role unspecified role neutral component neutral component N/A 256350 unspecified role unspecified role neutral component neutral component N/A 256351 unspecified role unspecified role neutral component neutral component N/A 256352 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 600 kDa subcomplex of the ATP synthase complex was detected. A complex that produces ATP from ADP in the presence of a proton gradient across the membrane. o27042 is annotated as A0 subcomplex ATP synthase subunit H by authors cdha-cdhc Acetyl-CoA decarbonylase/synthase complex 256311 N/A 256353 unspecified role unspecified role neutral component neutral component N/A 256354 unspecified role unspecified role neutral component neutral component N/A 256355 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 1200 kDa acetyl-CoA decarbonylase/synthase complex was detected. A complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2) . mth792-mth793 Lipid biosynthesis precursor complex 256311 N/A 256356 unspecified role unspecified role neutral component neutral component N/A 256357 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 300 kDa lipid biosynthesis precursor complex was detected. A complex that converts acetyl-CoA to hydroxy-3-methylglutaryl-CoA , a precursor of lipid biosynthesis. phes-phet Phenylalanyl-tRNA synthetase complex 256311 N/A 256358 unspecified role unspecified role neutral component neutral component N/A 256359 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 300 kDa Phenylalanyl-tRNA synthetas complex was detected. A complex that catalyses the following reaction ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). mth1149-mth1150 Fe-S cluster assembly complex 256311 N/A 256360 unspecified role unspecified role neutral component neutral component N/A 256361 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 200 kDa Fe-S cluster assembly complex was detected. A complex that may be involved in protection of iron sulphur clusters of proteins under oxidative stress. Proteins O27217 and Q50519 is annotated by authors as homologues of E.coli proteins SufC and SufB respectively which are involved in the bacterial iron uptake system. psma-psmb Proteasome complex 256311 N/A 256362 unspecified role unspecified role neutral component neutral component N/A 256363 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 800 kDa proteasome complex was detected. A complex that may be involved in protein degradation. rad50-pan Proteasome regulation complex 256311 N/A 256364 unspecified role unspecified role neutral component neutral component N/A 256365 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 800 kDa peoteasome regulatory complex was detected. A complex that may be involved in regulation of protein degradation. mth682-mth683 Exosome complex 256311 N/A 256366 unspecified role unspecified role neutral component neutral component N/A 256367 unspecified role unspecified role neutral component neutral component N/A 256368 unspecified role unspecified role neutral component neutral component N/A 256369 unspecified role unspecified role neutral component neutral component N/A 256370 unspecified role unspecified role neutral component neutral component physical association physical association false false false A 900 kDa exosome complex was detected. A complex that may be involved in the 3'->5' degradation of a variety of RNA species fwdc-mth1558-2 Methyltransferase/ATP synthase supercomplex 256311 N/A 256349 unspecified role unspecified role neutral component neutral component N/A 256350 unspecified role unspecified role neutral component neutral component N/A 256330 unspecified role unspecified role neutral component neutral component N/A 256331 unspecified role unspecified role neutral component neutral component N/A 256333 unspecified role unspecified role neutral component neutral component N/A 256335 unspecified role unspecified role neutral component neutral component physical association physical association false false false A putative supercomplex containing subunits of the methyltransferase complex and subunits of the ATP synthase complex was detected. mp3-mp2 Association between mp3 (Mth688p) and mp2 (Mth687p) in a yeast two-hybrid assay 872144 n/a 872145 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast n/a 872146 unspecified role unspecified role bait bait yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association false false false The pACT2-MTH688/pLexA-MTH687 interaction was stronger than the pACT2-MTH687/pLexA-MTH688 interaction. Figs. 3and 4 mp2-mp3 Association between mp2 (Mth687p) and mp3 (Mth688p) in a yeast two-hybrid assay 872144 n/a 872146 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast n/a 872145 unspecified role unspecified role bait bait yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association false false false The pACT2-MTH688/pLexA-MTH687 interaction was stronger than the pACT2-MTH687/pLexA-MTH688 interaction. Figs. 3 B and 4 B mp4-mp1 Association between mp4 (Mth1618p) and mp1 (Mth11p) in a yeast two-hybrid assay 872144 n/a 872147 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast n/a 872148 unspecified role unspecified role bait bait yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association false false false The pACT2-MTH1618/pLexA-MTH11 interaction was stronger than the pACT2-MTH11/pLexA-MTH1618 interaction. Figs. 3 A and 4 A mp1-mp4 Association between mp4 (Mth1618p) and mp1 (Mth11p) in a yeast two-hybrid assay 872144 n/a 872148 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast n/a 872147 unspecified role unspecified role bait bait yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association false false false The pACT2-MTH1618/pLexA-MTH11 interaction was stronger than the pACT2-MTH11/pLexA-MTH1618 interaction. Figs. 3 A and 4 A mthk-1 542348 N/A 542350 unspecified role unspecified role neutral component neutral component c-terminal RCK domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 8.0 physical association physical association false false false 6 A The RCK domains formed octamers at pH 7.5 and dimers at pH 6.5. A mixture of theswe two forms was found at pH 7.0. mthk-2 542348 N/A 542350 unspecified role unspecified role neutral component neutral component c-terminal RCK domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 physical association physical association false false false 6 A The RCK domains formed octamers at pH 7.5 and dimers at pH 6.5. A mixture of theswe two forms was found at pH 7.0. mthk 542349 N/A 542350 unspecified role unspecified role neutral component neutral component glu215 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false c-terminal RCK domain sufficient to bind sufficient binding region sufficient to bind mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false O27564:p.Asp184Asn mutation mutation mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false ile192 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false his193 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false his193 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false asp163 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 N/A 542350 unspecified role unspecified role neutral component neutral component arg213 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false val167 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false c-terminal RCK domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false O27564:p.Asp184Asn mutation mutation mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false leu196 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false ser189 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false asn216 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 N/A 542350 unspecified role unspecified role neutral component neutral component c-terminal RCK domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false O27564:p.Asp184Asn mutation mutation mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false glu125 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false lys150 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false arg154 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false ile192 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false his193 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false his193 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 N/A 542350 unspecified role unspecified role neutral component neutral component c-terminal RCK domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false O27564:p.Asp184Asn mutation mutation mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false arg166 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false glu146 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false his161 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false leu196 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false ser189 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false asn216 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 542367 542365 542368 542359 542371 542362 542372 542363 542373 542364 542386 542377 542387 542378 542388 542379 542389 542380 542390 542381 542391 542382 direct interaction direct interaction false false false 1, Table S1 All of the bonding between the amino acids specified is stated to occur by the authors. However, it is not clear in all cases which bonds coexist in one particular subunit. MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint hausmann-2008-2 Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex. in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Hausmann CD., Ibba M. FEBS Lett. (0014-5793) 2008 Only protein-protein interactions imex curation hausmann-2008-1 Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex. in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Hausmann CD., Ibba M. FEBS Lett. (0014-5793) 2008 Only protein-protein interactions imex curation syl_metth Leucine--tRNA ligase Leucyl-tRNA synthetase MTH_1508 leuS protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MDIERKWRDRWRDAGIFQADPDDREKIFLTVAYPYPSGAMHIGHGRTYTVPDVYARFKRMQGYNVLFPMAWHVTGAPVIGIARRIQRKDPWTLKIYREVHRVPEDELERFSDPEYIVEYFSREYRSVMEDMGYSIDWRREFKTTDPTYSRFIQWQIRKLRDLGLVRKGAHPVKYCPECENPVGDHDLLEGEGVAINQLTLLKFKLGDSYLVAATFRPETIYGATNLWLNPDEDYVRVETGGEEWIISRAAVDNLSHQKLDLKVSGDVNPGDLIGMCVENPVTGQEHPILPASFVDPEYATGVVFSVPAHAPADFIALEDLRTDHELLERYGLEDVVADIEPVNVIAVDGYGEFPAAEVIEKFGVRNQEDPRLEDATGELYKIEHARGVMSSHIPVYGGMKVSEAREVIADELKDQGLADEMYEFAERPVICRCGGRCVVRVMEDQWFMKYSDDAWKDLAHRCLDGMKIIPEEVRANFEYYIDWLNDWACSRRIGLGTRLPWDERWIIEPLTDSTIYMAYYTIAHRLREMDAGEMDDEFFDAIFLDDSGTFEDLREEFRYWYPLDWRLSAKDLIGNHLTFHIFHHSAIFPESGWPRGAVVFGMGLLEGNKMSSSKGNVILLRDAIEKHGADVVRLFLMSSAEPWQDFDWRESEVIGTRRRIEWFREFGERVSGILDGRPVLSEVTPAEPESFIGRWMMGQLNQRIREATRALESFQTRKAVQEALYLLKKDVDHYLKRVEGRVDDEVKSVLANVLHAWIRLMAPFIPYTAEEMWERYGGEGFVAEAPWPDFSDDAESRDVQVAEEMVQNTVRDIQEIMKILGSTPERVHIYTSPKWKWDVLRVAAEVGKLDMGSIMGRVSAEGIHDNMKEVAEFVRRIIRDLGKSEVTVIDEYSVLMDASDYIESEVGARVVIHSKPDYDPENKAVNAVPLKPAIYLE mint syp_metth Proline--tRNA ligase Prolyl-tRNA synthetase MTH_611 proS protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MQKPIKKDPNRYHGEKMTEFSEWFHNILEEAEIIDQRYPVKGMHVWMPHGFMIRKNTLKILRRILDRDHEEVLFPLLVPEDELAKEAIHVKGFEDEVYWVTHGGLSKLQRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETKHTRPLIRVREITTFKEAHTIHATASEAEEQVERAVEIYKEFFNSLGIPYLITRRPPWDKFPGSEYTVAFDTLMPDGKTLQIGTVHNLGQTFARTFEIKFETPEGDHEYVHQTCYGLSDRVIASVIAIHGDESGLCLPPDVAAHQVVIVPIIFKKAAEEVMEACRELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGEKVTADLQGIEETLRELMKDILENLRTRAWERMESEIREAETLEEASRIVDEKRGIISFMWCGEEECGMDVEEKVRVDILGIQEEGSGTCINCGREAPTGLTLPEHIS Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can inadvertently accommodate and process cysteine mint syk_metth Lysine--tRNA ligase Lysyl-tRNA synthetase MTH_1542 lysS protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MKFTHFFVALILSRFLQVISLKHWIERIADELKERDVEEHVVASGTSISGSIHIGNSCDVFIASSIAKSLKKDGFKSRTVWIADDHDPLRKVPYPLPESYEKYLGVPYSMIPCPEGCCESFVEHFQRPFLEALERFRIGVEHYSGARMYTEGLYNDYIRTSLERAPEIREIFNRFRDRPLRDDWLPYNPICEKCGRVNTTEAYDFSGDTVRYRCECGFDGEMDIKSGLGKLTWRVEWAARWKILGVTCEPFGKDHAASGGSYDVSSIISEEIFDYPAPYPVPYEWITLRGEAMSKSRGVFFTPGQWLEIGPPESLNYFIFRSKPMKHKDFNPDMPFLDLMDQFDRTERIYYGMEDAASEKEEQKLRNIYRVSMIEEFDLPLRPSYRFMTVACQIAGDDPERLYDILRRNSQLPEELMDLELDQLTDKQLEQLNERIENVKNWLRLYAPEFVKFQVQEELPDVELSEPQLKFLQDVADLMESREMSAEELHDEMYSILRRHGLKPQKAFQAIYRVLIGKKMGPRAASFLLSLERDFVIRRLRLEA mint ef1a_metth Elongation factor 1-alpha tuf MTH_1058 Elongation factor Tu protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MAKEKEHMNLAFIGHVDHGKSTLVGHLLLQAGAIAEQQLAEGEDKFRFVMDRLSEERERGVTIDLAHAKFETDKYEFTIVDCPGHRDFVKNMITGASQADAAVLVVAVDDGVMPQTKEHVFLSRTLGINQLIVAINKMDLVNYDEEKFNALKDEVAALIKTVGYKPSDVEFIPLSAFEGDNITSKSENTPWYKGKTLVEALDDLEAPEKPVDLPLRIPIQDVYSITGVGTVPVGRVETGVLKKGENVIFEPAGVSGEVKSIEMHHEMIEQAEPGDNIGFNVRGVGKNDIRRGDVAGHLDNPPKVAKEFTAQIVVLQHPGVITVGYTPVFHCHTAQVACTFLELVQKMNPATGQVEEENPDFLKTGNAAVVKVKPTKPLVIEKIKDIPHMGRFAIRDMGQTVAAGMCIDLVPAK mint This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis leus-tuf 739489 syl_metth LeuRS 739491 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false undefined mutation mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ef1a_metth EF1A 739492 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false direct interaction direct interaction false false false t2 kd 90 nanomolar mint leus-lyss 739489 syk_metth LysRS 739493 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false syl_metth LeuRS 739491 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified undefined mutation mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false direct interaction direct interaction false false false t2 kd 40 nanomolar mint leus-pros 739489 syl_metth LeuRS 739491 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false undefined mutation mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false syp_metth ProRS 739494 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false direct interaction direct interaction false false false t2 kd 80 nanomolar mint leus-lyss-1 739489 syl_metth LeuRS 739491 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false syk_metth LysRS 739493 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false direct interaction direct interaction false false false kd 170 nanomolar t2 mint leus-pros-1 739489 syp_metth ProRS 739494 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false syl_metth LeuRS 739491 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified undefined mutation mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false direct interaction direct interaction false false false t2 kd 110 nanomolar mint leus-pros-2 739489 syl_metth LeuRS 739491 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false undefined mutation mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false syp_metth ProRS 739494 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false direct interaction direct interaction false false false t2 kd 110 nanomolar mint leus-lyss-2 739489 syl_metth LeuRS 739491 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false undefined mutation mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false syk_metth LysRS 739493 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false direct interaction direct interaction false false false t2 kd 50 nanomolar mint leus-tuf-1 739489 syl_metth LeuRS 739491 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false undefined mutation mutation disrupting interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ef1a_metth EF1A 739492 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false direct interaction direct interaction false false false kd 150 nanomolar t2 mint tuf-leus 739490 syl_metth LeuRS 739491 predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false CP1 ef1a_metth EF1A 739492 predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified his tagged his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false direct interaction direct interaction false false false f2 kd 280 nanomolar mint DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ derebe-2011-2 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Derebe MG., Sauer DB., Zeng W., Alam A., Shi N., Jiang Y. DIP original experiment: DIP-249092X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites. Derebe MG., Sauer DB., Zeng W., Alam A., Shi N., Jiang Y. Only protein-protein interactions imex curation smith-2012-1 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Smith FJ., Pau VP., Cingolani G., Rothberg BS. DIP original experiment: DIP-251334X Structure (London, England : 1993) 2012 IMEx Crystal structure of a Ba(2+)-bound gating ring reveals elementary steps in RCK domain activation. Smith FJ., Pau VP., Cingolani G., Rothberg BS. Only protein-protein interactions imex curation kuo-2007-1 ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Kuo MM., Baker KA., Wong L., Choe S. DIP original experiment: DIP-261070X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Dynamic oligomeric conversions of the cytoplasmic RCK domains mediate MthK potassium channel activity. Kuo MM., Baker KA., Wong L., Choe S. Only protein-protein interactions imex curation kuo-2007-2 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Kuo MM., Baker KA., Wong L., Choe S. DIP original experiment: DIP-261067X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Dynamic oligomeric conversions of the cytoplasmic RCK domains mediate MthK potassium channel activity. Kuo MM., Baker KA., Wong L., Choe S. Only protein-protein interactions imex curation kuo-2007-3 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Kuo MM., Baker KA., Wong L., Choe S. DIP original experiment: DIP-261068X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Dynamic oligomeric conversions of the cytoplasmic RCK domains mediate MthK potassium channel activity. Kuo MM., Baker KA., Wong L., Choe S. Only protein-protein interactions imex curation kuo-2007-4 ecolx Escherichia coli sls static light scattering sls predetermined predetermined participant predetermined Kuo MM., Baker KA., Wong L., Choe S. DIP original experiment: DIP-261069X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Dynamic oligomeric conversions of the cytoplasmic RCK domains mediate MthK potassium channel activity. Kuo MM., Baker KA., Wong L., Choe S. Only protein-protein interactions imex curation kuo-2008-1 in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Kuo MM., Maslennikov I., Molden B., Choe S. DIP original experiment: DIP-113265X PLoS biology 2008 IMEx The desensitization gating of the MthK K+ channel is governed by its cytoplasmic amino terminus. Kuo MM., Maslennikov I., Molden B., Choe S. Only protein-protein interactions imex curation kuo-2008-2 in vitro In vitro sls static light scattering sls predetermined predetermined participant predetermined Kuo MM., Maslennikov I., Molden B., Choe S. DIP original experiment: DIP-113266X PLoS biology 2008 IMEx The desensitization gating of the MthK K+ channel is governed by its cytoplasmic amino terminus. Kuo MM., Maslennikov I., Molden B., Choe S. Only protein-protein interactions imex curation kuo-2008-3 in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Kuo MM., Maslennikov I., Molden B., Choe S. DIP original experiment: DIP-113267X PLoS biology 2008 IMEx The desensitization gating of the MthK K+ channel is governed by its cytoplasmic amino terminus. Kuo MM., Maslennikov I., Molden B., Choe S. Only protein-protein interactions imex curation pau-2011-1 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Pau VP., Smith FJ., Taylor AB., Parfenova LV., Samakai E., Callaghan MM., Abarca-Heidemann K., Hart PJ., Rothberg BS. DIP original experiment: DIP-249716X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx Structure and function of multiple Ca2+-binding sites in a K+ channel regulator of K+ conductance (RCK) domain. Pau VP., Smith FJ., Taylor AB., Parfenova LV., Samakai E., Callaghan MM., Abarca-Heidemann K., Hart PJ., Rothberg BS. Only protein-protein interactions imex curation pau-2011-2 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Pau VP., Smith FJ., Taylor AB., Parfenova LV., Samakai E., Callaghan MM., Abarca-Heidemann K., Hart PJ., Rothberg BS. DIP original experiment: DIP-249717X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx Structure and function of multiple Ca2+-binding sites in a K+ channel regulator of K+ conductance (RCK) domain. Pau VP., Smith FJ., Taylor AB., Parfenova LV., Samakai E., Callaghan MM., Abarca-Heidemann K., Hart PJ., Rothberg BS. Only protein-protein interactions imex curation pau-2011-3 ecolx Escherichia coli comigration in sds comigration in sds page comigration in sds weight by comassie molecular weight estimation by coomasie staining weight by comassie Pau VP., Smith FJ., Taylor AB., Parfenova LV., Samakai E., Callaghan MM., Abarca-Heidemann K., Hart PJ., Rothberg BS. DIP original experiment: DIP-249718X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx Structure and function of multiple Ca2+-binding sites in a K+ channel regulator of K+ conductance (RCK) domain. Pau VP., Smith FJ., Taylor AB., Parfenova LV., Samakai E., Callaghan MM., Abarca-Heidemann K., Hart PJ., Rothberg BS. Only protein-protein interactions imex curation dreyfus-2009-1 ecolx Escherichia coli ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Dreyfus C., Lemaire D., Mari S., Pignol D., Arnoux P. DIP original experiment: DIP-134518X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Crystallographic snapshots of iterative substrate translocations during nicotianamine synthesis in Archaea. Dreyfus C., Lemaire D., Mari S., Pignol D., Arnoux P. Only protein-protein interactions imex curation dreyfus-2009-2 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Dreyfus C., Lemaire D., Mari S., Pignol D., Arnoux P. DIP original experiment: DIP-134519X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Crystallographic snapshots of iterative substrate translocations during nicotianamine synthesis in Archaea. Dreyfus C., Lemaire D., Mari S., Pignol D., Arnoux P. Only protein-protein interactions imex curation silva-2011-1 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Silva AP., Chechik M., Byrne RT., Waterman DG., Ng CL., Dodson EJ., Koonin EV., Antson AA., Smits C. DIP original experiment: DIP-218814X Structure (London, England : 1993) 2011 IMEx Structure and activity of a novel archaeal β-CASP protein with N-terminal KH domains. Silva AP., Chechik M., Byrne RT., Waterman DG., Ng CL., Dodson EJ., Koonin EV., Antson AA., Smits C. Only protein-protein interactions imex curation silva-2011-2 ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Silva AP., Chechik M., Byrne RT., Waterman DG., Ng CL., Dodson EJ., Koonin EV., Antson AA., Smits C. DIP original experiment: DIP-218818X Structure (London, England : 1993) 2011 IMEx Structure and activity of a novel archaeal β-CASP protein with N-terminal KH domains. Silva AP., Chechik M., Byrne RT., Waterman DG., Ng CL., Dodson EJ., Koonin EV., Antson AA., Smits C. Only protein-protein interactions imex curation silva-2011-3 ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Silva AP., Chechik M., Byrne RT., Waterman DG., Ng CL., Dodson EJ., Koonin EV., Antson AA., Smits C. DIP original experiment: DIP-218815X Structure (London, England : 1993) 2011 IMEx Structure and activity of a novel archaeal β-CASP protein with N-terminal KH domains. Silva AP., Chechik M., Byrne RT., Waterman DG., Ng CL., Dodson EJ., Koonin EV., Antson AA., Smits C. Only protein-protein interactions imex curation silva-2011-4 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Silva AP., Chechik M., Byrne RT., Waterman DG., Ng CL., Dodson EJ., Koonin EV., Antson AA., Smits C. DIP original experiment: DIP-218816X Structure (London, England : 1993) 2011 IMEx Structure and activity of a novel archaeal β-CASP protein with N-terminal KH domains. Silva AP., Chechik M., Byrne RT., Waterman DG., Ng CL., Dodson EJ., Koonin EV., Antson AA., Smits C. Only protein-protein interactions imex curation silva-2011-5 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Silva AP., Chechik M., Byrne RT., Waterman DG., Ng CL., Dodson EJ., Koonin EV., Antson AA., Smits C. DIP original experiment: DIP-218817X Structure (London, England : 1993) 2011 IMEx Structure and activity of a novel archaeal β-CASP protein with N-terminal KH domains. Silva AP., Chechik M., Byrne RT., Waterman DG., Ng CL., Dodson EJ., Koonin EV., Antson AA., Smits C. Only protein-protein interactions imex curation ye-2010-1 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Ye S., Li Y., Jiang Y. DIP original experiment: DIP-217581X Nature structural & molecular biology 2010 IMEx Novel insights into K+ selectivity from high-resolution structures of an open K+ channel pore. Ye S., Li Y., Jiang Y. Only protein-protein interactions imex curation ye-2010-2 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Ye S., Li Y., Jiang Y. DIP original experiment: DIP-217582X Nature structural & molecular biology 2010 IMEx Novel insights into K+ selectivity from high-resolution structures of an open K+ channel pore. Ye S., Li Y., Jiang Y. Only protein-protein interactions imex curation o27564-2 Calcium-gated potassium channel MthK mthK MTH_1520 RCK domain protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MGLIDVAKSRHVVICGWSESTLECLRELRGSEVFVLAEDENVRKKVLRSGANFVHGDPTRVSDLEKANVRGARAVIVDLESDSETIHCILGIRKIDESVRIIAEAERYENIEQLRMAGADQVISPFVISGRLMSRSIDDGYEAMFVQDVLAEESTRRMVEVPIPEGSKLEGVSVLDADIHDVTGVIIIGVGRGDELIIDPPRDYSFRAGDIILGIGKPEEIERLKNYISA No experimental confirmation available. o26771_metth MTH_675 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MSCYIYWDKIKRIASRLEGMNYHFDEMDTSGVMPLLDEIEEIAHDSTIDFESAKHILDDAEMNHALSLIRKFYVNLGMKLEMEKAQEVIESDSPWETLRSFYFYPRYLELLKNEAALGRFRRGERAVFIGGGPLPLTGILLSHVYGMRVNVVEIEPDIAELSRKVIEGLGVDGVNVITGDETVIDGLEFDVLMVAALAEPKRRVFRNIHRYVDTETRIIYRTYTGMRAILYAPVSDDDITGFRRAGVVLPSGKVNNTSVLVFKCPD o27564-1 Calcium-gated potassium channel MthK mthK MTH_1520 Calcium-gated potassium channel protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MVLVIEIIRKHLPRVLKVPATRILLLVLAVIIYGTAGFHFIEGESWTVSLYWTFVTIATVGYGDYSPSTPLGMYFTVTLIVLGIGTFAVAVERLLEFLINREQMKLMGLIDVAKSRHVVICGWSESTLECLRELRGSEVFVLAEDENVRKKVLRSGANFVHGDPTRVSDLEKANVRGARAVIVDLESDSETIHCILGIRKIDESVRIIAEAERYENIEQLRMAGADQVISPFVISGRLMSRSIDDGYEAMFVQDVLAEESTRRMVEVPIPEGSKLEGVSVLDADIHDVTGVIIIGVGRGDELIIDPPRDYSFRAGDIILGIGKPEEIERLKNYISA rrp41_metth Exosome complex component Rrp41 rrp41 MTH_683 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MITIITQDQLKTSPSVREDGRAFDELRPLKIEAGILERADGSSYLEFGGNKILVAVYGPREAQIRKLQRPDRAVIRCRYNMAPFSVEERKRPGPDRRSVEISKITAEALRPALILEKFPRSVIDVFIEVLEAEGGTRCAGITAASVALADAGIPMRDMVVACAAGKVGDQVVLDLSEEEDKEGQADVPVAILPRTREITLLQSDGNLTPEEFERALDLAVEGCLRIHEVQKEALRKRYGE o27271_metth MTH_1203 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MVSEMLEEIKRTIMQRLPERVQVAKVEFEGPEVVIYTKNPEIITENGNLIRDIAKDIRKRIIIRSDRSVLMDPEKAIRKIHEIVPEEAKITNISFDDVTCEVIIEARKPGLVIGKYGSTSREIVKNTGWAPKILRTPPISSEIIERIRRTLRKNSKERKKILQQLGNRIHQKPKYDNDWARLTAMGGFREVGRSCLYLQTPNSRVLLDCGVNVAGGDDKNSYPYLNVPEFTLDSLDAVIITHAHLDHSGFLPYLYHYGYDGPVYCTAPTRDLMTLLQLDHIDIAHREDEPLPFNVKHVKKSVKHTITLDYGEVTDIAPDIRLTLHNAGHILGSAMAHLHIGDGQHNMVYTGDFKYEQSRLLEAAANRFPRIETLVMESTYGGHEDVQPSRNRAEKELVKTIYSTLRRGGKILIPVFAVGRAQELMIVLEEYIRTGIIDEVPVYIDGMIWEANAIHTARPEYLSKDLRDQIFHMGHNPFISDIFHKVNGMDERREIVEGEPSIILSTSGMLTGGNSLEYFKWLCEDPDNSLVFVGYQAEGSLGRRIQKGWKEIPLKDEDDKMRVYNVRMNIKTIEGFSGHSDRRQLMEYVKRISPKPEKILLCHGDNYKTLDLASSIYRTYRIETKTPLNLETVRIQ rrp42_metth Exosome complex component Rrp42 rrp42 MTH_682 protein protein metth Methanobacterium thermoautotrophicum Methanobacterium thermoautotrophicum MVNKMDIIPEITRKSITDLINNKERIDGRSLHEFRDISIETGVISKAEGSSRVKLGNTQIIVGVKPQIGEPFPDTPEMGVILTNSELLPMASPTFEPGPPDERSVELSRVVDRCIRESRMIDLEKLCIIEGSKVWMLFLDLHIIDYDGNLFDAAVLATVAALLDTRIPAAEVEDGEVVINREKMQPLPVNRKALMCTFAKIGNEIVLDPSLEEEDILTARISIGVTEEGSICAMQKGGEGPLTRDDVLKAVSIAVEKVPQLIEYLDKSMTP mthk-11 3220080 N/A 3220083 unspecified role unspecified role unspecified role unspecified role Pore domain Region 18-99 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mthk-15 3246158 N/A 3220083 unspecified role unspecified role unspecified role unspecified role RCK domain Region 107-336 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mthk-3 3152759 N/A 3220083 unspecified role unspecified role unspecified role unspecified role Region 107-336 Region 107-336 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mthk-4 3152760 N/A 3220083 unspecified role unspecified role unspecified role unspecified role Region 107-336 Region 107-336 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mthk-5 3152761 N/A 3220083 unspecified role unspecified role unspecified role unspecified role Region 107-336 Region 107-336 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mthk-6 3152762 N/A 3220083 unspecified role unspecified role unspecified role unspecified role Region 107-336 Region 107-336 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mthk-7 3179578 N/A 3179581 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false mthk-8 3179579 N/A 3179581 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false mthk-mthk-1 3179580 N/A 3220083 unspecified role unspecified role unspecified role unspecified role Region 1-11 Region 1-11 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false O27564-1:p.Leu3Asp L3D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false in vitro In vitro N/A 3179581 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false mthk-12 3231203 N/A 3220083 unspecified role unspecified role unspecified role unspecified role Region 107-336 Region 107-336 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mthk-13 3231204 N/A 3220083 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false mthk-14 3231205 N/A 3220083 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false o26771_metth-1 3196813 N/A 3196815 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false o26771_metth-2 3196814 N/A 3196815 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false o27271_metth-1 3226183 N/A 3226188 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false rrp41-rrp42-5 3226184 N/A 3226189 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3226190 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false o27271_metth-2 3226185 N/A 3226188 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false o27271_metth-3 3226186 N/A 3226188 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false rrp41-rrp42-6 3226187 N/A 3226189 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3226190 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false mthk-9 3212030 N/A 3220083 unspecified role unspecified role unspecified role unspecified role Pore domain Region 11-101 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mthk-10 3212031 N/A 3220083 unspecified role unspecified role unspecified role unspecified role Pore domain Region 11-101 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false