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/ aittaleb-2003-1 Structure and function of archaeal box C/D sRNP core proteins. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Aittaleb M., Rashid R., Chen Q., Palmer JR., Daniels CJ., Li H. Archaea - Interaction dataset based on Archaea proteins Nat. Struct. Biol. (1072-8368) 2003 PDBe - Data obtained from the Protein Data Bank Europe groll-2003-1 Investigations on the maturation and regulation of archaebacterial proteasomes. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Groll M., Brandstetter H., Bartunik H., Bourenkow G., Huber R. Archaea - Interaction dataset based on Archaea proteins groll@biochem.mpg.de J. Mol. Biol. (0022-2836) 2003 PDBe - Data obtained from the Protein Data Bank Europe flpa_arcfu Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase flpA AF_2087 protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MKELMRNVYLLDDTLVTKSKYGSHYGEKVFDGYREWVPWRSKLAAMILKGHRLKLRGDERVLYLGAASGTTVSHLADIVDEGIIYAVEYSAKPFEKLLELVRERNNIIPLLFDASKPWKYSGIVEKVDLIYQDIAQKNQIEILKANAEFFLKEKGEVVIMVKARSIDSTAEPEEVFKSVLKEMEGDFKIVKHGSLMPYHRDHIFIHAYRF psb_arcfu Proteasome subunit beta psmB AF_0481 20S proteasome beta subunit Proteasome core protein PsmB protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MSMIEEKIYKGTTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIATLTSNLLNSYRYFPYLVQLLIGGIDSEGKSIYSIDPIGGAIEEKDIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVRAIYSAMKRDSASGDGIDVVKITEDEFYQYSPEEVEQILAKFRK o28191_arcfu Nop domain-containing protein AF_2088 protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MSKLRYNLWFGVYDGKEIKLSENFEESFLKAENPSPLPFNVSEVGAKALGKDYYRILRKTALAVSEKMVEKELRREDRYVVALVKALEEIDESINMLNEKLEDIRAVKESEITEKFEKKIRELRELRRDVEREIEEVMEKIAPNMTELVGAKVAAKLLERAGSMERLVRLPASKIQVIGAEKSLYKAFARMKKGKKAKIPKHGIIFLHPFIRTLPKAKRGKMARFLAAKLAIAAKIDYFRGEIDESLYESIRRRYEELRRK psa_arcfu Proteasome subunit alpha psmA AF_0490 20S proteasome alpha subunit Proteasome core protein PsmA protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MHLPQMGYDRAITVFSPDGRLFQVEYAREAVKRGATAIGIKCKEGVILIADKRVGSKLLEADTIEKIYKIDEHICAATSGLVADARVLIDRARIEAQINRLTYDEPITVKELAKKICDFKQQYTQYGGVRPFGVSLLIAGVDEVPKLYETDPSGALLEYKATAIGMGRNAVTEFFEKEYRDDLSFDDAMVLGLVAMGLSIESELVPENIEVGYVKVDDRTFKEVSPEELKPYVERANERIRELLKK flpa-o28191-1 Crystal structure of fibrillarin-nop5p complex 513622 N/A 513623 unspecified role unspecified role neutral component neutral component region 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: 1.0 N/A 513624 unspecified role unspecified role neutral component neutral component region 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: 1.0 direct interaction direct interaction false false false octameric, multimeric working 74.300%, free 67.700% 2.9A psma-psmb-1 20s proteasome in complex with calpain-inhibitor i from archaeoglobus fulgidus 513630 N/A 513631 unspecified role unspecified role neutral component neutral component region 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: 7.0 N/A 513632 unspecified role unspecified role neutral component neutral component region 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: 7.0 direct interaction direct interaction false false false heptameric, multimeric working 75.900%, free 72.100% 2.83A 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 yamagata-2007-1 Hexameric structures of the archaeal secretion ATPase GspE and implications for a universal secretion mechanism. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Yamagata A., Tainer JA. EMBO J. (0261-4189) 2007 2009-01-08 Only protein-protein interactions imex curation o29909_arcfu AF_0338 protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MLNGIVTENCLWYNKPPHDERMIEQYKMFFNVHFVILSLLHETFFNFKYRNLLMPTLRFSFKKKEDEVPRRTAVFEIIKKGAKEEFLGEETYRTLSKRLSQEFEPPEGWIEVEGYPVYGRFVISSVHILYNEEDNEFIYHVNEPKLSEEEEKIVKNVIGRLEYYAANPKEIGDKVGTLKKKIDSILEAYRVNLEGSDYFRVLYHIFKRTILYGKITPIMYDPMIEDISCNGYGKYIYIFHRKYTNLRTNVIFDDPDELDSFVVNLAQKCGKHISIAEPMVDATMPDGSRIQMTLGREVTDHGSTFTIRKFREEPVTPIDLIAWKTFSSEQMAYLWLCIENKKSLIFAGGTASGKTTSMNAISLFIPRRSKIVTIEDTRELMLPHENWIPAVTRDAFHGEKGAVDMYDLLRAALRQRPEYIIVGEVRGREALTLFQAMATGHTTYSTLHADSISGAIHRLENPPIGVPRPMLEALDIISIQAQTYVGDRRVRRNMEIAEIVGLDAHTKMLRTSTVFQWDSVKDEHAMVGTSKALEEIRRQRGWSVRELNEELERRRRVLEFMLSNGIRMFKDVSAVIHTYQVNPERAMKRLGVEEL mint o29909-o29909 594324 o29909_arcfu GspE 594325 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role neutral component neutral component purified purified o29909_arcfu GspE 594325 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false F3 GspE has an hexameric structure. 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/ till-2007-4 in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Till S., Lejeune E., Thermann R., Bortfeld M., Hothorn M., Enderle D., Heinrich C., Hentze MW., Ladurner AG. DIP original experiment: DIP-68101X Nature structural & molecular biology 2007 IMEx A conserved motif in Argonaute-interacting proteins mediates functional interactions through the Argonaute PIWI domain. Till S., Lejeune E., Thermann R., Bortfeld M., Hothorn M., Enderle D., Heinrich C., Hentze MW., Ladurner AG. Only protein-protein interactions imex curation parizotto-2013-1 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Parizotto EA., Lowe ED., Parker JS. DIP original experiment: DIP-252915X Nature structural & molecular biology 2013 IMEx Structural basis for duplex RNA recognition and cleavage by Archaeoglobus fulgidus C3PO. Parizotto EA., Lowe ED., Parker JS. Only protein-protein interactions imex curation parizotto-2013-2 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Parizotto EA., Lowe ED., Parker JS. DIP original experiment: DIP-252916X Nature structural & molecular biology 2013 IMEx Structural basis for duplex RNA recognition and cleavage by Archaeoglobus fulgidus C3PO. Parizotto EA., Lowe ED., Parker JS. Only protein-protein interactions imex curation majumder-2019-1 in vitro In vitro 3d-em 3D electron microscopy 3D-EM electron tomog experimental particp experimental participant identification experimental particp Majumder P., Rudack T., Beck F., Danev R., Pfeifer G., Nagy I., Baumeister W. baumeist@biochem.mpg.de Proceedings of the National Academy of Sciences of the United States of America 2019 imex curation Only protein-protein interactions imex curation johnson-2005-1 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Johnson E., Cascio D., Sawaya MR., Gingery M., Schröder I. DIP original experiment: DIP-132757X Structure (London, England : 1993) 2005 IMEx Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic archaeon Archaeoglobus fulgidus. Johnson E., Cascio D., Sawaya MR., Gingery M., Schröder I. Only protein-protein interactions imex curation johnson-2005-2 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Johnson E., Cascio D., Sawaya MR., Gingery M., Schröder I. DIP original experiment: DIP-132758X Structure (London, England : 1993) 2005 IMEx Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic archaeon Archaeoglobus fulgidus. Johnson E., Cascio D., Sawaya MR., Gingery M., Schröder I. Only protein-protein interactions imex curation johnson-2005-3 ecolx Escherichia coli electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Johnson E., Cascio D., Sawaya MR., Gingery M., Schröder I. DIP original experiment: DIP-132759X Structure (London, England : 1993) 2005 IMEx Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic archaeon Archaeoglobus fulgidus. Johnson E., Cascio D., Sawaya MR., Gingery M., Schröder I. Only protein-protein interactions imex curation ferris-2011-1 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Ferris HU., Dunin-Horkawicz S., Mondéjar LG., Hulko M., Hantke K., Martin J., Schultz JE., Zeth K., Lupas AN., Coles M. DIP original experiment: DIP-218791X Structure (London, England : 1993) 2011 IMEx The mechanisms of HAMP-mediated signaling in transmembrane receptors. Ferris HU., Dunin-Horkawicz S., Mondéjar LG., Hulko M., Hantke K., Martin J., Schultz JE., Zeth K., Lupas AN., Coles M. Only protein-protein interactions imex curation ferris-2011-2 ecolx Escherichia coli nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Ferris HU., Dunin-Horkawicz S., Mondéjar LG., Hulko M., Hantke K., Martin J., Schultz JE., Zeth K., Lupas AN., Coles M. DIP original experiment: DIP-218792X Structure (London, England : 1993) 2011 IMEx The mechanisms of HAMP-mediated signaling in transmembrane receptors. Ferris HU., Dunin-Horkawicz S., Mondéjar LG., Hulko M., Hantke K., Martin J., Schultz JE., Zeth K., Lupas AN., Coles M. Only protein-protein interactions imex curation romo-2011-1 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Romão CV., Ladakis D., Lobo SA., Carrondo MA., Brindley AA., Deery E., Matias PM., Pickersgill RW., Saraiva LM., Warren MJ. DIP original experiment: DIP-249065X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization. Romão CV., Ladakis D., Lobo SA., Carrondo MA., Brindley AA., Deery E., Matias PM., Pickersgill RW., Saraiva LM., Warren MJ. Only protein-protein interactions imex curation fukunaga-2007-1 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Fukunaga R., Yokoyama S. DIP original experiment: DIP-66658X Nature structural & molecular biology 2007 IMEx Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea. Fukunaga R., Yokoyama S. Only protein-protein interactions imex curation fukunaga-2007-2 ecolx Escherichia coli cosedimentation cosedimentation predetermined predetermined participant predetermined Fukunaga R., Yokoyama S. DIP original experiment: DIP-66659X Nature structural & molecular biology 2007 IMEx Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea. Fukunaga R., Yokoyama S. Only protein-protein interactions imex curation naganuma-2014-1 ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Naganuma M., Sekine S., Chong YE., Guo M., Yang XL., Gamper H., Hou YM., Schimmel P., Yokoyama S. DIP original experiment: DIP-262106X Nature 2014 IMEx The selective tRNA aminoacylation mechanism based on a single G•U pair. Naganuma M., Sekine S., Chong YE., Guo M., Yang XL., Gamper H., Hou YM., Schimmel P., Yokoyama S. Only protein-protein interactions imex curation naganuma-2014-2 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Naganuma M., Sekine S., Chong YE., Guo M., Yang XL., Gamper H., Hou YM., Schimmel P., Yokoyama S. DIP original experiment: DIP-262107X Nature 2014 IMEx The selective tRNA aminoacylation mechanism based on a single G•U pair. Naganuma M., Sekine S., Chong YE., Guo M., Yang XL., Gamper H., Hou YM., Schimmel P., Yokoyama S. Only protein-protein interactions imex curation naganuma-2009-1 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Naganuma M., Sekine S., Fukunaga R., Yokoyama S. DIP original experiment: DIP-134218X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Unique protein architecture of alanyl-tRNA synthetase for aminoacylation, editing, and dimerization. Naganuma M., Sekine S., Fukunaga R., Yokoyama S. Only protein-protein interactions imex curation wu-2008-27 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Wu CC., Rice WJ., Stokes DL. DIP original experiment: DIP-110777X Structure (London, England : 1993) 2008 IMEx Structure of a copper pump suggests a regulatory role for its metal-binding domain. Wu CC., Rice WJ., Stokes DL. Only protein-protein interactions imex curation wu-2008-28 ecolx Escherichia coli 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Wu CC., Rice WJ., Stokes DL. DIP original experiment: DIP-110778X Structure (London, England : 1993) 2008 IMEx Structure of a copper pump suggests a regulatory role for its metal-binding domain. Wu CC., Rice WJ., Stokes DL. Only protein-protein interactions imex curation hollenstein-2007-1 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Hollenstein K., Frei DC., Locher KP. DIP original experiment: DIP-253264X Nature 2007 IMEx Structure of an ABC transporter in complex with its binding protein. Hollenstein K., Frei DC., Locher KP. Only protein-protein interactions imex curation hollenstein-2007-2 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Hollenstein K., Frei DC., Locher KP. DIP original experiment: DIP-253266X Nature 2007 IMEx Structure of an ABC transporter in complex with its binding protein. Hollenstein K., Frei DC., Locher KP. Only protein-protein interactions imex curation hollenstein-2007-3 ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Hollenstein K., Frei DC., Locher KP. DIP original experiment: DIP-253267X Nature 2007 IMEx Structure of an ABC transporter in complex with its binding protein. Hollenstein K., Frei DC., Locher KP. Only protein-protein interactions imex curation hollenstein-2007-4 in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Hollenstein K., Frei DC., Locher KP. DIP original experiment: DIP-253265X Nature 2007 IMEx Structure of an ABC transporter in complex with its binding protein. Hollenstein K., Frei DC., Locher KP. Only protein-protein interactions imex curation cbix_arcfu Sirohydrochlorin cobaltochelatase cbiX CbiXS cbiXS protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MRRGLVIVGHGSQLNHYREVMELHRKRIEESGAFDEVKIAFAARKRRPMPDEAIREMNCDIIYVVPLFISYGLHVTEDLPDLLGFPRGRGIKEGEFEGKKVVICEPIGEDYFVTYAILNSVFRIGRDGKGEE o29424_arcfu AF_0834 protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MASISEKMVEALNRQINAEIYSAYLYLSMASYFDSIGLKGFSNWMRVQWQEELMHAMKMFDFVSERGGRVKLYAVEEPPSEWDSPLAAFEHVYEHEVNVTKRIHELVEMAMQEKDFATYNFLQWYVAEQVEEEASALDIVEKLRLIGEDKRALLFLDKELSLRQFTPPAEEEK DD55E5B59B7A30F5 psb_arcfu Proteasome subunit beta psmB AF_0481 20S proteasome beta subunit Proteasome core protein PsmB protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MSMIEEKIYKGTTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIATLTSNLLNSYRYFPYLVQLLIGGIDSEGKSIYSIDPIGGAIEEKDIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVRAIYSAMKRDSASGDGIDVVKITEDEFYQYSPEEVEQILAKFRK psa_arcfu Proteasome subunit alpha psmA AF_0490 20S proteasome alpha subunit Proteasome core protein PsmA protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MHLPQMGYDRAITVFSPDGRLFQVEYAREAVKRGATAIGIKCKEGVILIADKRVGSKLLEADTIEKIYKIDEHICAATSGLVADARVLIDRARIEAQINRLTYDEPITVKELAKKICDFKQQYTQYGGVRPFGVSLLIAGVDEVPKLYETDPSGALLEYKATAIGMGRNAVTEFFEKEYRDDLSFDDAMVLGLVAMGLSIESELVPENIEVGYVKVDDRTFKEVSPEELKPYVERANERIRELLKK pan_arcfu Proteasome-activating nucleotidase pan Proteasomal ATPase Proteasome regulatory ATPase Proteasome regulatory particle AF_1976 protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MGDSEIQYLLEKLKKLEEDYYKLRELYRRLEDEKKFIESERIRYEREVRRLRSEVERLRSPPLLVGVVSDILEDGRVVVKSSTGPKFVVNTSQYINEEELKPGARVALNQQTLAIVNVLPTSKDPMVYGFEVEEKPEVSYEDIGGLDVQIEEIREAVELPLLKPELFAEVGIEPPKGVLLYGPPGTGKTLLAKAVANQTRATFIRVVGSEFVQKYIGEGARLVREVFQLAKEKAPSIIFIDELDAIAARRTNSDTSGDREVQRTMMQLLAELDGFDPRGDVKVIGATNRIDILDPAILRPGRFDRIIEVPLPTFEGRIQIFKIHTRKMKLAEDVDFKELARITEGASGADIKAICTEAGMFAIREERAKVTMLDFTKAIEKVLKKTTPIPDLKGVMFV copa_arcfu Probable copper-exporting P-type ATPase copA Cu(+)-exporting ATPase pacS AF_0473 Copper-exporting P-type ATPase A protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MVKDTYISSASKTPPMERTVRVTGMTCAMCVKSIETAVGSLEGVEEVRVNLATETAFIRFDEKRIDFETIKRVIEDLGYGVVDEQAAVSAEVEHLSRMKRKLYVAAFAGVLLLFLAHFISLPYEDFVQLLIALPAIFYSGSSIFKAAFSALRRRTLNMDVMYSMGVGAAFLASVLSTAGVLPREYSFYETSVLLLAFLLLGRTLEARAKSRTGEAIKKLVGLQAKTAVVIRDGKEIAVPVEEVAVGDIVIVRPGEKIPVDGVVVEGESYVDESMISGEPVPVLKSKGDEVFGATINNTGVLKIRATRVGGETLLAQIVKLVEDAMGSKPPIQRLADKVVAYFIPTVLLVAISAFIYWYFIAHAPLLFAFTTLIAVLVVACPCAFGLATPTALTVGMGKGAELGILIKNADALEVAEKVTAVIFDKTGTLTKGKPEVTDLVPLNGDERELLRLAAIAERRSEHPIAEAIVKKALEHGIELGEPEKVEVIAGEGVVADGILVGNKRLMEDFGVAVSNEVELALEKLEREAKTAVIVARNGRVEGIIAVSDTLKESAKPAVQELKRMGIKVGMITGDNWRSAEAISRELNLDLVIAEVLPHQKSEEVKKLQAKEVVAFVGDGINDAPALAQADLGIAVGSGSDVAVESGDIVLIRDDLRDVVAAIQLSRKTMSKIKQNIFWALIYNVILIPAAAGLLYPIFGVVFRPEFAGLAMAMSSVSVVANSLLLRNYVPPIRRGGDSVEKIVLELSGLSCHHCVARVKKALEEAGAKVEKVDLNEAVVAGNKEDVDKYIKAVEAAGYQAKLRS 610EB948C1D6B16F o28769_arcfu HAMP domain-containing protein AF_1503 protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MKLTPQIVLIVVVASLVPLSVLGYLTIAGMTSSAEEAKQGVTTVSQEYLTKAGEEAVRMKAQDLALAVQTYIEAKMKLENKTMLTTFDLIQDPKFRSLGAQRWGAKEYTWVGAGNKVAGRDVAVILTHPAFTGQYEKYLGVDVAMLRWNETMPELYNLLLKITENPEAPKPVCGYYHWDDPETPEKEEIPKYLCHYPTTIKVYDPISKGQLWVVVGTSAYIDGYFQYLTQNPANPAENIASEISKSVEGAIQQVYYALGIAAAIAIVFVIVLAVFTTSTITRPIIELSNTADKIAEGNLEAEVPHQNRADEIGILAKSIERLRRSLKVAMESLEEALK D2D1AFD80353C87E o28024_arcfu AF_2260 protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MRLEECRKRLEELEAAREELLKVLREMRIHSTKSIALIHAGKVEEAEQELKKAIELLEKVKAYREYPEIYFYLCNDAMQELVEAIAFKNAISGEFTFEIDLEVTPAAFLNGFADAVGELRRYALTKLIEGDFKSAERMLEVMEKIYERLMEFTTFPDKLVSGLRKKLDVARGGIERTKSDYIAAKVARLNESLGGN sya_arcfu Alanine--tRNA ligase alaS Alanyl-tRNA synthetase AF_2255 protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MTLDEEYLDITFLTENGFVRKRCPKCGKHFWTADPEREICGDPPCESYSFIGNPVFKKPFELDEMREYYLNFFERRGHGRIERYPVVARWRTDIYLTIASIADFQPFVTSGVAPPPANPLTISQPCIRLDDLDSVGRTGRHLTLFEMMAHHAFNYPGKEIYWKNETVAYCTELLNELGVKKEDIVYKEEPWAGGGNAGPCLEAIVGGLEVATLVFMNLEEHPEGDIEIKGARYRKMDNYIVDTGYGLERFVWASKGTPTVYDAIFPEVVDTIIDNSNVSFNREDERVRRIVAESSKLAGIMGELRGERLNQLRKSVADTVGVSVEELEGIVVPLEKVYSLADHTRCILFMLGDGLVPSNAGAGYLARLMIRRSLRLAEELELGLDLYDLVEMHKKILGFEFDVPLSTVQEILELEKERYRTTVSKGTRLVERLVERKKKLEKDDLIELYDSHGIPVELAVGIAAEKGAEVEMPKDIYAELAKRHSKAEKVQEKKITLQNEYPATEKLYYDDPTLLEFEAEVIGVEGDFVILNRSAFYPESGGQDNDVGYLIANGGKFEVVDVLEADGVVLHVVKGAKPEVGTKVKGVIDSDVRWRHMRHHSATHVLLYSLQKVLGNHVWQAGARKEFSKARLDVTHFRRPSEEEIKEIEMLANREILANKPIKWEWMDRIEAERKFGFRLYQGGVPPGRKIRVVQVGDDVQACGGTHCRSTGEIGMLKILKVESIQDGVIRFEFAAGEAAIEAVEEMERLLREASSILRVEPAKLPKTVERFFEEWKDQRKEIERLKSVIADLWADILMERAEEFDSMKVVAEVVDADMQALQKLAERLAEKGAVGCLMAKGEGKVFVVTFSGQKYDARELLREIGRVAKGSGGGRKDVAQGAVQQLLDREEMLDVIFRFLSEHEG 2AD39B7B65C72C8B q9upq9-2 Trinucleotide repeat-containing gene 6B protein TNRC6B KIAA1093 protein protein human Homo sapiens Human MQTNEGEVSEESSSKVEQEDFVMEGHGKTPPPGEESKQEKEQEREEQLMEDKKRKKEDKKKKEATQKVTEQKTKVPEVTKPSLSQPTAASPIGSSPSPPVNGGNNAKRVAVPNGQPPSAARYMPREVPPRFRCQQDHKVLLKRGQPPPPSCMLLGGGAGPPPCTAPGANPNNAQVTGALLQSESGTAPVWSKSTPPAPDNGTSAWGEPNESSPGWGEMDDTGASTTGWGNTPANAPNAMKPNSKSMQDGWGESDGPVTGARHPSWEEEEDGGVWNTTGSQGSASSHNSASWGQGGKKQMKCSLKGGNNDSWMNPLAKQFSNMGLLSQTEDNPSSKMDLSVGSLSDKKFDVDKRAMNLGDFNDIMRKDRSGFRPPNSKDMGTTDSGPYFEKGGSHGLFGNSTAQSRGLHTPVQPLNSSPSLRAQVPPQFISPQVSASMLKQFPNSGLSPGLFNVGPQLSPQQIAMLSQLPQIPQFQLACQLLLQQQQQQQLLQNQRKISQAVRQQQEQQLARMVSALQQQQQQQQRQPGMKHSPSHPVGPKPHLDNMVPNALNVGLPDLQTKGPIPGYGSGFSSGGMDYGMVGGKEAGTESRFKQWTSMMEGLPSVATQEANMHKNGAIVAPGKTRGGSPYNQFDIIPGDTLGGHTGPAGDSWLPAKSPPTNKIGSKSSNASWPPEFQPGVPWKGIQNIDPESDPYVTPGSVLGGTATSPIVDTDHQLLRDNTTGSNSSLNTSLPSPGAWPYSASDNSFTNVHSTSAKFPDYKSTWSPDPIGHNPTHLSNKMWKNHISSRNTTPLPRPPPGLTNPKPSSPWSSTAPRSVRGWGTQDSRLASASTWSDGGSVRPSYWLVLHNLTPQIDGSTLRTICMQHGPLLTFHLNLTQGTALIRYSTKQEAAKAQTALHMCVLGNTTILAEFATDDEVSRFLAQAQPPTPAATPSAPAAGWQSLETGQNQSDPVGPALNLFGGSTGLGQWSSSAGGSSGADLAGASLWGPPNYSSSLWGVPTVEDPHRMGSPAPLLPGDLLGGGSDSI piwi_arcfu Piwi protein AF_1318 AfAgo PIWI/MID domain protein AF_1318 AfPiwi protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MMEYKIVENGLTYRIGNGASVPISNTGELIKGLRNYGPYEVPSLKYNQIALIHNNQFSSLINQLKSQISSKIDEVWHIHNINISEFIYDSPHFDSIKSQVDNAIDTGVDGIMLVLPEYNTPLYYKLKSYLINSIPSQFMRYDILSNRNLTFYVDNLLVQFVSKLGGKPWILNVDPEKGSDIIIGTGATRIDNVNLFCFAMVFKKDGTMLWNEISPIVTSSEYLTYLKSTIKKVVYGFKKSNPDWDVEKLTLHVSGKRPKMKDGETKILKETVEELKKQEMVSRDVKYAILHLNETHPFWVMGDPNNRFHPYEGTKVKLSSKRYLLTLLQPYLKRNGLEMVTPIKPLSVEIVSDNWTSEEYYHNVHEILDEIYYLSKMNWRGFRSRNLPVTVNYPKLVAGIIANVNRYGGYPINPEGNRSLQTNPWFL F925081F3AFB47CD wtpa_arcfu Molybdate/tungstate-binding protein WtpA wtpA modA AF_0094 protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MHIGGGVVKIRILILLMLALFLLGCSSNVNTNVKLKVFHAGSLTEPMKAFKRAFEEKHPNVEVQTEAAGSAATIRKVTELGRKADVIATADYTLIQKMMYPEFANWTIMFAKNQIVLAYRNDSRYADEINSQNWYEILKRPDVRFGFSNPNDDPCGYRSLMAIQLAELYYNDPTIFDELVAKNSNLRFSEDNGSYVLRMPSSERIEINKSKIMIRSMEMELIHLVESGELDYFFIYKSVAKQHGFNFVELPVEIDLSSPDYAELYSKVKVVLANGKEVTGKPIVYGITIPKNAENRELAVEFVKLVISEEGQEILRELGQEPLVPPRADTAVPSLKAMVEVS wtpb_arcfu Molybdate/tungstate transport system permease protein WtpB wtpB modB AF_0093 protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MRLLFSALLALLSSIILLFVLLPVAATVTLQLFNFDEFLKAASDPAVWKVVLTTYYAALISTLIAVIFGTPLAYILARKSFPGKSVVEGIVDLPVVIPHTVAGIALLVVFGSSGLIGSFSPLKFVDALPGIVVAMLFVSVPIYINQAKEGFASVDVRLEHVARTLGSSPLRVFFTVSLPLSVRHIVAGAIMSWARGISEFGAVVVIAYYPMIAPTLIYERYLSEGLSAAMPVAAILILLSLAVFVALRIIVGREDVSEGQG wtpc_arcfu Molybdate/tungstate import ATP-binding protein WtpC wtpC modC AF_0092 protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MFLKVRAEKRLGNFRLNVDFEMGRDYCVLLGPTGAGKSVFLELIAGIVKPDRGEVRLNGADITPLPPERRGIGFVPQDYALFPHLSVYRNIAYGLRNVERVERDRRVREMAEKLGIAHLLDRKPARLSGGERQRVALARALVIQPRLLLLDEPLSAVDLKTKGVLMEELRFVQREFDVPILHVTHDLIEAAMLADEVAVMLNGRIVEKGKLKELFSAKNGEVAEFLSARNLLLKVSKILD seps_arcfu O-phosphoserine--tRNA(Cys) ligase sepS Non-canonical O-phosphoseryl-tRNA(Cys) synthetase O-phosphoseryl-tRNA(Cys) synthetase AF_0110 protein protein arcfu Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) MKFDPQKYRELAEKDFEAAWKAGKEILAERSPNELYPRVGFSFGKEHPLFATIQRLREAYLSIGFSEVVNPLIVEDVHVKKQFGREALAVLDRCFYLATLPKPNVGISAEKIRQIEAITKREVDSKPLQEIFHRYKKGEIDGDDLSYLIAEVLDVDDITAVKILDEVFPEFKELKPISSTLTLRSHMTTGWFITLSHIADKLPLPIKLFSIDRCFRREQGEDATRLYTYFSASCVLVDEELSVDDGKAVAEALLRQFGFENFRFRKDEKRSKYYIPDTQTEVFAFHPKLVGSSTKYSDGWIEIATFGIYSPTALAEYDIPYPVMNLGLGVERLAMILYGYDDVRKMVYPQIHGEIKLSDLDIAREIKVKEVPQTAVGLKIAQSIVETAEKHASEPSPCSFLAFEGEMMGRNVRVYVVEEEENTKLCGPAYANEVVVYKGDIYGIPKTKKWRSFFEEGVPTGIRYIDGFAYYAARKVEEAAMREQEEVKVKARIVENLSDINLYIHENVRRYILWKKGKIDVRGPLFVTVKAEIE ED762519450D50E2 tnrc6b-afpiwi-1 3161524 N/A 3161532 unspecified role unspecified role prey prey ecolx Escherichia coli N/A 3161528 unspecified role unspecified role bait bait 198-219 binding region 198-219 binding region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false GST Tag GST Tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag predetermined featur predetermined feature predetermined featur undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ecolx Escherichia coli direct interaction direct interaction false false false o28024_arcfu-1 3249873 N/A 3249875 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false o28024_arcfu-2 3249874 N/A 3249875 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false pan-psma-1 4088218 N/A 4088219 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) Stoichiometry: 6.0 N/A 4088220 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified binding region binding region 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: 14.0 N/A 4088221 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) Stoichiometry: 14.0 physical association physical association false false false Fig 1, Fig S1 pan-psma-2 4088218 N/A 4088219 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) Stoichiometry: 6.0 physical association physical association false false false Fig 1, Fig S1 pan-psma-3 4088218 N/A 4088220 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified binding region binding region 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: 14.0 N/A 4088221 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) Stoichiometry: 14.0 physical association physical association false false false Fig 1, Fig S1 afftn-1 3137751 N/A 3137754 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false afftn-2 3137752 N/A 3137754 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false afftn-3 3137753 N/A 3137754 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false af1503-1 3223348 N/A 3223350 unspecified role unspecified role unspecified role unspecified role HAMP domain Region 278-331 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 af1503-2 3223349 N/A 3223350 unspecified role unspecified role unspecified role unspecified role HAMP domain Region 278-331 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 cbix-1 3219531 N/A 3219533 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false seprs-1 3153479 N/A 3153483 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli direct interaction direct interaction false false false seprs-2 3153480 N/A 3153483 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli direct interaction direct interaction false false false alas-2 3266868 N/A 3266870 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false alas-3 3266869 N/A 3266870 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false alars-1 3190434 N/A 3266870 unspecified role unspecified role unspecified role unspecified role Region 736-906 Region 736-906 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false copa-9 3172923 N/A 3172925 unspecified role unspecified role unspecified role unspecified role Region 94-737 Region 94-737 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 copa-2 3172924 N/A 3172925 unspecified role unspecified role unspecified role unspecified role Region 94-737 Region 94-737 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 wtpa-wtpb-1 3153364 N/A 3153368 unspecified role unspecified role unspecified role unspecified role Region 32-342 Region 32-342 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3153369 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3153370 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association false false false wtpb-wtpc-1 3153365 N/A 3153369 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3153370 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false wtpb-wtpc-2 3153366 N/A 3153369 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false ecolx Escherichia coli N/A 3153370 unspecified role unspecified role prey prey ecolx Escherichia coli physical association physical association false false false wtpa-wtpb-2 3153367 N/A 3153368 unspecified role unspecified role unspecified role unspecified role Region 32-342 Region 32-342 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3153369 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3153370 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association false false false