wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic translation initiation factor 2 subunit 3, X-linked (EC 3.6.5.3) (Eukaryotic translation initiation factor 2 subunit gamma, X-linked) (eIF2-gamma) (eIF2-gamma X) (PP42) (P81795)
Organism: Rattus norvegicus (Rat)
Function: As a subunit of eukaryotic initiation factor 2 (eIF-2), involved in the early steps of protein synthesis. In the presence of GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex and initiation factors eIF-1, eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a step that determines the rate of protein translation. The 43S PIC binds to mRNA and scans downstream to the initiation codon, where it forms a 48S initiation complex by codon-anticodon base pairing. This leads to the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release of Pi, which makes GTP hydrolysis irreversible, causes the release of the eIF-2-GDP binary complex from the 40S subunit, an event that is essential for the subsequent joining of the 60S ribosomal subunit to form an elongation-competent 80S ribosome. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP exchange factor (GEF) eIF-2B (By similarity). Along with its paralog on chromosome Y, may contribute to spermatogenesis up to the round spermatid stage (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09130}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 2, subunit 2
- Eukaryotic translation initiation factor 3 subunit B
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 3 subunit G
- Translation initiation factor eIF2B subunit delta
- Translation initiation factor eIF2B subunit beta
- Eukaryotic translation initiation factor 3 subunit C
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit gamma
Sequence:
MAGGEAGVTLGQPHLSRQDLATLDVTKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLDDPSCPRPECYRSCGSSTPDEFPTDIPGTKGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD
Protein: Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanine tRNA-synthetase beta subunit) (FRS) (PheRS) (Phenylalanyl-tRNA synthetase beta subunit) (A5K464)
Organism: Plasmodium vivax (strain Salvador I)
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NSD9}.
Interaction partners:
- Phenylalanine--tRNA ligase alpha subunit
- Phenylalanyl-tRNA synthetase alpha chain, putative
- phenylalanine--tRNA ligase
- Small ribosomal subunit protein uS2
- 40S ribosomal protein S11, putative
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S14-2, putative
- leucine--tRNA ligase
- leucine--tRNA ligase
- 40S ribosomal protein S3
Sequence:
MPTISVHEEDLIEKLGEKIEEEKLNDICFEFGIEIDDVEYKGEKKIYKIEVPANRYDLVCVEGLCRALKSFIGKYENVSYALLTNSEEACVKEKHFMRVDESVDERRSYVVSAVLKNVKMNENVYNNIIELQEKLHHNLGKKRILLAIGIHDYDKINFPVAYKFEEKEKINFIPLNETQNVNGNNFINFYQDNINLKSYLKIISDFEKFPVIVDAGGQILSLPPIINCDYTKITYDTRNLFIECTAIDRNKAEIAVNIICSMLSEYCTPKYSIHSFFVQYDKNHKAEKGNGYLYPVFKNKTLTCHMDYVRKLSGILNLSVKDVEPLLKKMMITSKVIDSSTFTVDVPFYRSDIMHFCDIVEDIAIAYGYGNIVSEKIEIAKKNSLSACTELFRNVLAECTYTEVMTNALLSKRENYDCMLRKHRSYDDRKINLDEYNPLAPPVQIMNSKTSEYEIVRTSLIVNMLKFVSANKHRELPLRFFEIGDVSYTTYDRTDTNAVNKRYLSVIFADKFTAGLEEAHGMLETVLKEFQLFSDYKIEEKSKENVAIRSDVFYKLVPKEDPSFLNERVVDIVLCPHNLKFGIMGIIHPKVLENFSIDIPVSVIEINIETIMDVLMM
Protein: ESAT-6-like protein (A0A0H3LG02)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MAEMKTDAATLAQEAGNFERISGDLKTQIDQVESTAGSLQGQWRGAAGTAAQAAVVRFQEAANKQKQKLDEISTNIRQAGVQYSRADEEQQQALSSQMGF
Protein: Metallo-beta-lactamase type 2 (EC 3.5.2.6) (B2 metallo-beta-lactamase) (Beta-lactamase type II) (Metallo-beta-lactamase NDM-1) (Metallo-beta-lactamase type II) (New Delhi metallo-beta-lactamase-1) (NDM-1) (C7C422)
Organism: Klebsiella pneumoniae
Function: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
Sequence:
MELPNIMHPVAKLSTALAAALMLSGCMPGEIRPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYANALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR
Protein: Ribosomal silencing factor RsfS (O86327)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01477}.
Interaction partners:
- Large ribosomal subunit protein uL14
- Probable nicotinate-nucleotide adenylyltransferase
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein bL32
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein bL20
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein uL13
Sequence:
MTANREAIDMARVAAGAAAAKLADDVVVIDVSGQLVITDCFVIASGSNERQVNAIVDEVEEKMRQAGYRPARREGAREGRWTLLDYRDIVVHIQHQDDRNFYALDRLWGDCPVVPVDLSANSAGAQ
Protein: Zinc finger transcription factor (Q7K9G4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSSLKTSQSGGMYVKTSSISGISSISGKEAASCYGGFMSPPLSANITANNGEREMFRVPGAKVETNESYACGELQFPDFSHLCFAAETPNSVFSDCHNYAGQDQQQDSDQDDIVCAAAENTGMPYQQGQYTQLNREDIFRFEPEDIARLTGESELPGIAQNSQYAVQPANDSINLDIDYFNYDEINCQSKNQSPCSSPHLDAWLNFNLGEISAAASSSAASPKLGNVFEEQVKEEASPAKLPSMNSTFGTPKCIPMCASNYEDYANLYQQGSGYSTENYHNNMAQVVEKPNREHKAIWTIDELDELMLGEQQQFLQHHLQQQHLQEQQEQLHQPHGQEQQTQNCKDDLVNYLSDEFIKAEEFRSLDSDDDENYNEEEDDLDNDVFAPPAESDPKPDSTCCDPEAEPENEVIPLICRWTGCDEEFPHQQAFVEHIEKCHVDVRKGEDFSCFWLDCPRRYKPFNARYKLLIHMRVHSGEKPNKCPFPGCNKAFSRLENLKIHQRSHTGERPYGCQYKGCLKAFSNSSDRAKHQRTHYDTKPYACQLPGCTKRYTDPSSLRKHVKNHALRNANGQLRRKSAGGASVPPSGPKKAAKTRRHSESALVQRGVGAGVGVAVPSAPGDQRQHRSNSCSEALLLQQHQQQQQQQQQQQKQHQPESPAGPATLATATATTTATATYGNGNMAPAPETEVLSVCSGGGSSNSNSNNNRYNANINQLSELEQLLTTAKPTGTPAASANGISLANNNGRANGDSKCHLSEFVSFEYVTKYLTDVYEPQCKSPQPPANFHLQPEFDNSFDMLDFPQFI
Protein: Transcription initiation factor IIA large subunit (TFIIA large subunit) (Q9USU9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with tbp mediates transcriptional activity (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcription initiation factor IIA subunit 2
- TATA-box-binding protein
- Transcription initiation factor IIB
- General transcription and DNA repair factor IIH subunit ssl1
- Transcription initiation factor IIF subunit beta
- Transcription initiation factor IIE subunit alpha
- Transcription initiation factor IIE subunit beta
- Transcription initiation factor IIF subunit alpha
- DNA-directed RNA polymerase II subunit rpb1
- General transcription and DNA repair factor IIH subunit tfb2
Sequence:
MSNSIVGEVYHHVILDVIANSRSDFEENGVDDATLRELQNLWQSKLVATDVATFPWAQAPVGTFPIGQLFDPVSGLRTDSLDVTAPAVANSPILNNIAAIRAVQQMDTFAQQHGNSNYYSPPTPSLPQSATNISFDSSAIPNVQSNPNNTAPFPSYSSNSLQLPTNQTADSPIINDHSTANVTSTGQEHAPDSSSTNSFGGLLLPNQNSPKKSELGETESSNTTPANSRNDVPQTDGAIHDLDDAGSPSNFESNRFAIAQKADAEIYEVLKKNRILQIDGTIEDNEDEKKPPVDTPSDEAINSDLDDPDSDEAPETEEGSDIGQAIVLCLYDKVNHHKNKWKCVFRDGVVGVNGKDYLFFKANGEFEWI
Protein: Nuclear pore complex protein NUP133 (Nucleoporin 133) (Nucleoporin Nup155-like) (F4IGA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus envelope {ECO:0000305|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
Interaction partners:
- Nuclear pore complex protein NUP85
- Nuclear pore complex protein NUP107
- Nuclear pore complex protein NUP43
- Protein SEH1
- Protein transport protein SEC13 homolog B
- Nuclear pore complex protein NUP96
- Nuclear pore complex protein NUP160
- Nuclear pore complex protein NUP214
- Nucleoporin
- Nuclear pore complex protein NUP62
Sequence:
MFSPLTKRAKQSSRNEKTPRNRVPPPDSPVTPATQNRNNFISDRPATGTPAPWAPRLSVLARVSPGNNGDKGVDSDQLKPVFVGEFPQLLRDEQSYPGDACVSGGMDKETCLSWFITGSKVFVWSHLTTLPSRKCVVLELPVVVLVNEESGSGLQDGKSWLVNVVSWDTSAGAATRASRSRSPVGVVMCNRKTRAVVYWSDIFSGQEAAPAEKARHLIKRQSNGIRSSRAENSDLNSLITTAVAAAERLCIAIACSSNGELWQFTCSPTGVKSNQVQLNISSSSVSEGYPRSLIWRFSQGLARESCWEFLMLTDCDIHCFTIEPYPDLTVSEVWQHEIVGTDGDSGIKKDIASQKQIWPLDLQVDDQGKVITVLVATICMDRASSSSYTQYSLLTLQHKSEMRFADGREEKVLEKQGPIQVIIPKARVEDKDFLFSMRLRVGGRPPGSAIILSGDGTATVCYCHGSSTRLYKFDLPYDAGKVLDASVLSSTDEHEYGAWTVLTEKAGVWAIPEKAVVLGGVEPPERSLSRKNSSNERSTRDETRVTPYGVDRTAGRENSDIQNIEDKGNPKMGFTRQTARDEESEALLGQLFEGFLLSGKVDGSLEKLSQSGAFDRDGEANVFARKSKSIVDTLAKHWTTTRGAEIVAMTVISSQLVEKQQKHENFLHFLALSKCHEELCSKQRHSLQIILENGEKLAAMIQLRELQNMINQNRSARFGSPQAGSEDQVSCALWDLIQFVGERARRNTVLLMDRDNAEVFYSKVSELEEVFYCLNRQLEYIIRADQPLGTQLQRACELSNACVTILQTALDYKNEHQMWYPPLEGLIPWHSQTVVCNGLWCIASFMLHLLTEASRIDISAKSDIYTHLEVLTEVLLEACAGSTFAKLEREEENKGLLNEYWTRRDTIFDSLYRQAKEFMEAEIQGIRERTEATDEDIFRNRCSNLISIAKRHAGYKIMWKICYDLNDTGLLRNLMHEGVGPQGGFSYFVFQQLYDMKQFSKLLRLGEEFQDELLIFLKRHSDLVWLHQVFLHQFSSASDTLHTLALSQDEESMTTVEERTGPEPEDVQPTFADRKRFLNLSKIAYVADKDADSESKVKRIEADLNLLKLQEEITKALPNGEARNRLFRPEELIETCLNIQGRWTAIKAFEVFAWTSSSFRENHRSLLEECWRNAADQDDWDRHHQASTNEGWSEEETLQNLRNTALFQASKRCYGPTRVNTFDGDFAQVLPLRRENPEDSTSSVEDVLMSHKDFAEAGKLMLTAIMLGCVEEEGIVAEEFSSPME
Protein: SCAN domain-containing protein 1 (Q8C2P0)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187}.
Interaction partners:
Sequence:
MAAPQPSQDPQSPAAPPEQQEGAGDCAAPSPDSGSSPAPELPGAPAALNTAPYADAVLRPGASRPGPETFRQRFRQFRYQDAAGPREAFRQLRELSRQWLRPDIRTKEQIVEMLVQEQLQAILAGGGPGSAAAAPRGRAHHRLSGGAWGSLD
Protein: Serine/threonine-protein kinase 40 (EC 2.7.11.1) (SINK-homologous serine/threonine-protein kinase) (Sugen kinase 495) (SgK495) (Q8N2I9)
Organism: Homo sapiens (Human)
Function: May be a negative regulator of NF-kappa-B and p53-mediated gene transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:13679039}. Cytoplasm {ECO:0000269|PubMed:13679039}.
Interaction partners:
- E3 ubiquitin-protein ligase COP1
- Tribbles homolog 3
- Tribbles homolog 1
- ETS translocation variant 1
- ETS translocation variant 5
- Protein c-Fos
- DET1 homolog
- Fos-related antigen 2
- Tribbles homolog 2
- Nuclear factor interleukin-3-regulated protein
Sequence:
MKRRASDRGAGETSARAKALGSGISGNNAKRAGPFILGPRLGNSPVPSIVQCLARKDGTDDFYQLKILTLEERGDQGIESQEERQGKMLLHTEYSLLSLLHTQDGVVHHHGLFQDRTCEIVEDTESSRMVKKMKKRICLVLDCLCAHDFSDKTADLINLQHYVIKEKRLSERETVVIFYDVVRVVEALHQKNIVHRDLKLGNMVLNKRTHRITITNFCLGKHLVSEGDLLKDQRGSPAYISPDVLSGRPYRGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEDGRVSENTVCLIRKLLVLDPQQRLAAADVLEALSAIIASWQSLSSLSGPLQVVPDIDDQMSNADSSQEAKVTEECSQYEFENYMRQQLLLAEEKSSIHDARSWVPKRQFGSAPPVRRLGHDAQPMTSLDTAILAQRYLRK
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q400N4)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- E3 ubiquitin-protein ligase hrd-like protein 1
- E3 ubiquitin-protein ligase hrd-1
- NOT2/NOT3/NOT5 C-terminal domain-containing protein
- E3 ubiquitin ligase rnf-121
- Ubiquitin-conjugating enzyme E2 G2
- Transitional endoplasmic reticulum ATPase homolog 2
- Transitional endoplasmic reticulum ATPase homolog 1
- Derlin-1
- E3 ubiquitin-protein ligase ubr-1
- Probable ergosterol biosynthetic protein 28 homolog
Sequence:
MEVEHEQPPEHEAGSVDASNRPSTSSENPNPEEPCPQPPSDPIIDDNDDHLMCRVCRGNEGSLYYPCLCTGSIKYVHQECLVEWLKYSKKEVCELCNHKYSFQPIYRQDMPKALPILEILRGVLISGAIMVRTWIIYTIVMTTWLGIVPLTAARIYNCIFYLSFHDIVNAPFQLFKAEHFFNDILKGSLLLLVFVCTFISLVWLREQIIIGGPQHFLNIEAEENEGEDDVVNENNESSDESEDDEEDEDDEEDDDEDDEEEEEDSESGYEEDPVPEFREEGEAYVARRRVPFEERRRDILEARHGFRPQMPNLGIYDDMRDDENEVLENDHVLQNVQEDRIPPPMEPEPIVPRAAARANRRIRRQRENEEAAAAAAAAQEQGGAGDQEDNWREWDRFGDELTWQRLLGLDGSLIFLEHVFWVISLNTLFTATFAYFPFRIGNWFLSVIGLHGKISYFPSIVAMLLGYIQIAIITYVIHQIMLQFKMKMMYRFLGIMFLIIKVFLLVFLEIGFFPVMCGCWMDVCTLPLFNITLSQRIATFATAPFMSIFLHWMVGMVYVFYSASFVILLREILRPGVLWFMRNLNDPDFNPIQEMIDLPFTRHFRRLVVSTTLFFSTILLIFYIPLNIISSLIPSLLPYNVSMSAETPLSEISLELLILQVVMPAILEHANGRGFIKYGVRFWCKVVGAALDLDQYLLSDNNNNNQNNNNNNNDPLRAGNNQAGGGLAAEHQALLLLREPRAYEPYNRPSLFGVRVSILLVLMSLTTTLSSVVVFIVPASIGRFIILMVSGQTNVHEMYTVSLGLYVCWTIGKFGAVVTKFVRGGPHLFKRAVVHYSYLGMRLFLVAIPIIIVLPLLMGTYFQLVFFTPMRLGYQQTALMFPYQDWAMGVVQIKIFGVIAVMGPDWWLKTELDLLVQRGIENFAALHVFVRIVVPCILYLSTFIAFPVVVIKFYAFISGADPEFTMLLLRFSYPAFLFITSAVVFIRWQVVKFRELAEKIKNDRYLVGTQLVNYERNGVRATAAQ
Protein: Nucleoporin (F4JSP7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Nuclear pore complex protein NUP1
- Nuclear pore complex protein NUP96
- Nuclear pore complex protein NUP88
- Nuclear pore complex protein NUP160
- Nuclear pore complex protein NUP85
- Protein SEH1
- Nuclear pore complex protein NUP107
- Nuclear pore complex protein NUP205
- Protein transport protein SEC13 homolog B
- Protein RAE1
Sequence:
MDKKKNRADPLAAGRQKLQQFRQKKADKGTDQKKDSKGSTSQGKSSKKSNKSEKHERKPDTSAVSDEAQAPSPVTVGGATSHVNVAEEVVDSPQTSSDTKAHEYVSVHGSSSEPDALQPGHTTSNDGSEARKEVVNSENDISKSLSTEEENVKSINSGVAGTVDSLISDPADSEKGVTHDDASNVDGIFAASGNIAEGEGVEVEGGSGNVEKPHQPSSLQEYIPDVSLIRARGDQVTDVGEMQEEDMEQFSELSAKAGVDKIATEERQTSYPAVVDSSASPSHFSEGSSVAFDTVELEGINGNFRSQQIREAAELNEEKPETSIDFPNNRDHVLSAEPEESSVAEMASQLQLPESVSISGVLSHEETRKIDTLNLSAELTSAHVHEGRSVSFLQLMDIVKGLGQDEYQILCNAREAASSTEPGTSSLERLREELFVSSTMEDILHVQLTEQSHLQIEFDHQHNQFVAEISQLRASYSAVTERNDSLAEELSECQSKLYAATSSNTNLENQLLATEAQVEDFTAKMNELQLSLEKSLLDLSETKEKFINLQVENDTLVAVISSMNDEKKELIEEKESKNYEIKHLSSELCNCKNLAAILKAEVEQFENTIGPLTDEKIHLVEEKYSLLGEAEKLQEELANCKTVVTLQEVENSNMKETLSLLTRQQTMFEENNIHLREENEKAHLELSAHLISETYLLSEYSNLKEGYTLLNNKLLKFQGEKEHLVEENDKLTQELLTLQEHMSTVEEERTHLEVELREAIARLDKLAEENTSLTSSIMVEKARMVDNGSADVSGLINQEISEKLGRSSEIGVSKQSASFLENTQYTNLEEVREYTSEFSALMKNLEKGEKMVQNLEEAIKQILTDSSVSKSSDKGATPAVSKLIQAFESKRKPEEPESENAQLTDDLSEADQFVSVNVQIRNLRGLLDQLLLNARKAGIQFNQLNDDRTSTNQRLEELNVEFASHQDHINVLEADTIESKVSFEALKHYSYELQHKNHDLELLCDSLKLRNDNISVENTELNKKLNYCSLRIDELEIQLENLQQNLTSFLSTMEEQLVALQDESERAMMVEHELTSLMSEFGEAVVRLDDCLLRSGTSGAHTGLDMTKRISGSVDVAVNVIEDLKEKLEAAYVKHESTSNKYEELKQSFNTLFEKNEFTASSMQKVYADLTKLITESCGSAEMTSLEVENVAVFDPFRDGSFENLLEAVRKILSERLELQSVIDKLQSDLSSKSNDMEEMTQRSLDSTSLRELVEKVEGLLELESGVIFESPSSQVEFLVSQLVQKFIEIEELANLLRKQLEAKGNELMEIEESLLHHKTKIAGLRESLTQAEESLVAVRSELQDKSNELEQSEQRLLSTREKLSIAVTKGKGLIVQRDNVKQSLAEASAKLQKCSEELNSKDARLVEVEKKLKTYIEAGERVEALESELSYIRNSATALRESFLLKDSLLHRIEEILEDLDLPEHFHARDILEKVEWLARSANGNSSRPSGWDQKSSDGGAGFVLSEPWREDVQTGTSSEDDLRIKFEELKGKFYGLAEQNEMLEQSLMERNTLVQRWEKLLENIDIPPQLHSMEVENKIEWLASTITEATHDRDNLQQKIDNLEVYCQSVTTDLEVSQKQVGDVEGNLQSCVSERVNLSERLESLIGDHESLSARGIHLEVENEKLQNQVKDLHEKLVEKLGNEEHFQTIEGDLLSLRYMIDDVIQEDGLQDLALASNSENLDGVLRKLIDYYKNLVKSSLPGETDDNVCETRPSDADVRSGESLGAHGATSHGQHFELSDSNVVEATSRDIAVVETPDVASLTKDLDQALHVQKLTREERDLYMAKQQSLVAENEALDKKIIELQEFLKQEEQKSASVREKLNVAVRKGKALVQQRDSLKQTIEEVNAELGRLKSEIIKRDEKLLENEKKFRELESYSVRVESLESECQLLKIHSQETEYLLQERSGNLSMTLNALNSIDIGDEGDINDPVMKLQRISQLFQTMSTTVTSAEQESRKSRRAAELLLAELNEVQETNDSLQEDLSKFTYEIQQLSREKDAAEAAKVEAISRFENLSAVSNEEKNKLYAQLLSCGTSVNSLRKILAGTNSCLADIFIMDMEFLHHLKANMELCAKKTGTDLSGLPQLSTENLVDKEIFARLSAAWSNINLHETSSGGNIAEICGSLSQNLDQFVVGVSHLEEKVSKHLATWHDQINIVSNSIDTFFKSIGTGTDSEVAALGERIALLHGACSSVLVEIERRKAELVGNDDFNMSLHQVDEDFSSMESVRSMVNRLSSAVKELVVANAETLERNEKEMKVIIANLQRELHEKDIQNNRTCNELVGQVKEAQAGAKIFAEDLQSASARMRDMQDQLGILVRERDSMKERVKELLAGQASHSELQEKVTSLSDLLAAKDLEIEALMQALDEEESQMEDLKLRVTELEQEVQQKNLDLQKAEASRGKISKKLSITVDKFDELHHLSENLLAEIEKLQQQVQDRDTEVSFLRQEVTRCTNEALAASQMGTKRDSEEIQTVLSWFDTIASLLGIEDSLSTDADSHINHYMETFEKRIASMLSEIDELRLVGQSKDVLLEGERSRVAELRQKEATLEKFLLEKESQQDISTSSTSEIVEVEPLINKWTKTSIPSQVRSLRKGNMDQVAISIDADQTDQSGSLEEDDDKDHSLRQESFLDSQDPSLTWSMVYGQTLFIHGSRSVVSCDRTLMRQPALRLGIMLYWAILHALLAAFVV
Protein: Ech hydrogenase, subunit EchD, putative (Q72EY7)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Ech hydrogenase, subunit EchF, putative
- Ech hydrogenase, subunit EchA, putative
- Ech hydrogenase, subunit EchB, putative
- Pyridine nucleotide-disulfide oxidoreductase
- NAD
- Ech hydrogenase, subunit EchE, putative
- Succinate--CoA ligase subunit alpha
- Pyruvate:ferredoxin oxidoreductase
- Acyl carrier protein
- Acyl carrier protein, putative
Sequence:
MPNHTEILNAKPIAIDAIVGEAKALFEQDYRLVTYSVVDLGDGNVDIIYHFDKDLEFVHYRLTTPKDQPIPSLTPVYFAALLIENEARDQFGLTFDGLVLDFNRTLYLDDEITGSMSAPFCKISTIQKKA
Protein: fumarate hydratase (EC 4.2.1.2) (Q9W3X6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Malate dehydrogenase
- Malate dehydrogenase, mitochondrial
- Malate dehydrogenase
- Malate dehydrogenase
- Probable citrate synthase, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Aspartate aminotransferase
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
Sequence:
MVLPLLQRSTLRGVQQMTKPWAAIGSLRLASQEFRVESDTFGELKVPADKYYGAQTMRSQINFPIGGATERMPKPVVQAMGILKKAAAEVNKEFGLDSKVSEAISKAADDVISGKLYDDHFPLVIWQTGSGTQSNMNVNEVISNRAIELLGGKLGSKTPVHPNDHVNKSQSSNDTFPTAIHISVALELNNNLKPAIKTLHDALRAKSEEFKDIIKIGRTHTMDAVPLTLGQEFSGYAQQLAYAQERIDACLPRVYELALGGTAVGTGLNTRKGFAEKCAAKIAELTSLPFVTAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRFLGSGPRCGLGELSLPENEPGSSIMPGKVNPTQCESLTMLSAQVMGNQVAVTIGGSNGHFELNVFKPLIVSNVLRSIRLLSDGSRTFTANCVNGIQANRENIAKIMNESLMLVTALNPHIGYDKAAKIAKTAHKNGTTLKEEAINLGYLTEQQFNDWVRPEQMLGPK
Protein: Fanconi anemia complementation group G isoform 5 (A0A0S2Z3S1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRQTTSVGSSCLDLWREKNDRLVRQAKSGASKDLLLLLKTWSPPAEELDAPLTLQDAQGLKDVLLTAFAYRQGLQELITGNPDKALSSLHEAASGLCPRPVLVQVYTALGSCHRKMGNPQRALLYLVAALKEGSAWGPPLLEASRLYQQLGDTTAELESLELLVEALNVPCSSKAPQFLIEVELLLPPPDLASPLHCGTQSQTKHILASRCLQTGRAGDAAEHYLDLLALLLDSSEPRFSPPPSPPGPCMPEVFLEAAVALIQAGRAQDALTLCEELLSRTSSLLPKMSRLWEDARKGTKELPYCPLWVSATHLLQGQAWVQLGAQKVAISEFSRCLELLFRATPEEKEQGAAFNCEQGCKSDAALQQLRAAALISRGLEWVASGQDTKALQDFLLSVQMCPGLSPCT
Protein: Cobalamin biosynthesis protein CobIJ [Includes: Precorrin-2 C(20)-methyltransferase (EC 2.1.1.130) (S-adenosyl-L-methionine--precorrin-2 methyltransferase) (SP2MT); Precorrin-3B C17-methyltransferase (EC 2.1.1.131) (S-adenosyl-L-methionine--precorrin-3B methyltransferase)] (P9WGB3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Methylates precorrin-2 at the C-20 position to produce precorrin-3A.
Interaction partners:
- Precorrin-4 C
- Precorrin-8X methylmutase
- Precorrin-6A reductase
- Precorrin-6Y C
- Cobyric acid synthase
- Precorrin-3B synthase CobG
- Adenosylcobinamide-GDP ribazoletransferase
- uroporphyrinogen-III C-methyltransferase
- Probable uroporphyrin-III C-methyltransferase HemD
- Cobalamin biosynthesis protein CobN
Sequence:
MSARGTLWGVGLGPGDPELVTVKAARVIGEADVVAYHSAPHGHSIARGIAEPYLRPGQLEEHLVYPVTTEATNHPGGYAGALEDFYADATERIATHLDAGRNVALLAEGDPLFYSSYMHLHTRLTRRFNAVIVPGVTSVSAASAAVATPLVAGDQVLSVLPGTLPVGELTRRLADADAAVVVKLGRSYHNVREALSASGLLGDAFYVERASTAGQRVLPAADVDETSVPYFSLAMLPGGRRRALLTGTVAVVGLGPGDSDWMTPQSRRELAAATDLIGYRGYLDRVEVRDGQRRHPSDNTDEPARARLACSLADQGRAVAVVSSGDPGVFAMATAVLEEAEQWPGVRVRVIPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWDVIAARLTAAAAADLVLAIYNPASVTRTWQVGAMRELLLAHRDPGIPVVIGRNVSGPVSGPNEDVRVVKLADLNPAEIDMRCLLIVGSSQTRWYSVDSQDRVFTPRRYPEAGRATATKSSRHSD
Protein: Probable NADPH dehydrogenase (EC 1.6.99.1) (Estrogen-binding protein) (EBP) (P43084)
Organism: Candida albicans (Yeast)
Function: Oxidoreductase that binds mammalian estrogens with high affinity.
Interaction partners:
Sequence:
MTIESTNSFVVPSDTKLIDVTPLGSTKLFQPIKVGNNVLPQRIAYVPTTRFRASKDHIPSDLQLNYYNARSQYPGTLIITEATFASERGGIDLHVPGIYNDAQAKSWKKINEAIHGNGSFSSVQLWYLGRVANAKDLKDSGLPLIAPSAVYWDENSEKLAKEAGNELRALTEEEIDHIVEVEYPNAAKHALEAGFDYVEIHGAHGYLLDQFLNLASNKRTDKYGCGSIENRARLLLRVVDKLIEVVGANRLALRLSPWASFQGMEIEGEEIHSYILQQLQQRADNGQQLAYISLVEPRVTGIYDVSLKDQQGRSNEFAYKIWKGNFIRAGNYTYDAPEFKTLINDLKNDRSIIGFSRFFTSNPDLVEKLKLGKPLNYYNREEFYKYYNYGYNSYDESEKQVIGKPLA
Protein: Uncharacterized protein (Q387L7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTMWFPAETVPSSARKEGVTPRDNGGLLSIGCDCACHSPPRDFSHILESSHVTFANSSRGVSYKGIDPPVRMRSSIGSGARTQDLQVSSTSRRKRAKTSNNRGALHGVEESYLQEIDHLQQLAKQFDEERSEAVDRAEEMRAAYERSRQQSILKEREIQSLGDQMHRLQDKLHRAEYQLTSVQSICRRDAEFHREQQLLLFEENERNTREALVFAEASWRTVIQERCSNTMSALAHKQYSSVERHSEELGVARHGCRSEKTWNQAYTDRPVSCPAQRCTSTSRQYSGQQEEDCWATPATGMKSTLLAELHQSKKRADETIEQLKRELEEKEEVIASLRNQLNLQEEGLQKVPRAGGSDESLMMEMQAEIDDLLLNELLLTHSCERYALETEAMEELTYALRWLLQQHAFALQEAPFITPQRTPAGSKQPVLPRTPGTSPHLVEVHSAASPGCNDVTTSVAEMRAIVGDTVLEVIKKELQGCLLPIRLSVESMRASSEELIGDLRKAVRDAGYNAPQLTPSITMGEIKSEHAALLRNIQRSLDDMNTTVAPPLCTELKQLRETVVKVGRLTAHNNKVMDDKLSDILHCQSAVSRQMILSALPCDEKLDFCRTPVAECSTTVPPAKVSLSREGANAISSVGGGLNYNAENVLSDGGNESGVSIKKTQSHESSGAYVDSTGPAFHDWDVESSDSKFMVPSMDVSIIRKTPYDIEDA
Protein: Peroxiredoxin-2E, chloroplastic (EC 1.11.1.25) (Glutaredoxin-dependent peroxiredoxin) (Peroxiredoxin IIE) (Thioredoxin peroxidase 2E) (Q949U7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides (By similarity). May be involved in chloroplast redox homeostasis (Probable).
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:12913160}.
Interaction partners:
- 2-Cys peroxiredoxin BAS1-like, chloroplastic
- 2-Cys peroxiredoxin BAS1, chloroplastic
- Peroxiredoxin Q, chloroplastic
- NADPH-dependent thioredoxin reductase 3
- Thioredoxin-like protein CDSP32, chloroplastic
- Monothiol glutaredoxin-S12, chloroplastic
- Sulfiredoxin, chloroplastic/mitochondrial
- Thioredoxin M4, chloroplastic
- Glutaredoxin-C5, chloroplastic
- L-ascorbate peroxidase T, chloroplastic
Sequence:
MATSLSVSRFMSSSATVISVAKPLLSPTVSFTAPLSFTRSLAPNLSLKFRNRRTNSASATTRSFATTPVTASISVGDKLPDSTLSYLDPSTGDVKTVTVSSLTAGKKTILFAVPGAFTPTCSQKHVPGFVSKAGELRSKGIDVIACISVNDAFVMEAWRKDLGINDEVMLLSDGNGEFTGKLGVELDLRDKPVGLGVRSRRYAILADDGVVKVLNLEEGGAFTNSSAEDMLKAL
Protein: Germ cell-expressed bHLH-PAS, isoform C (Germ cell-expressed bHLH-PAS, isoform D) (Germ cell-expressed bHLH-PAS, isoform E) (Germ cell-expressed bHLH-PAS, isoform G) (LP18592p1) (Q9VXW7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein cycle
- FI10506p
- Spineless, isoform C
- Dysfusion, isoform D
Sequence:
MEGASRSRNSSTSHSQGRGQDIEDLKQDIPYFDEPPALDADLLVLGKSECQLDELAWDRDADGDADAPLETAPAVDLEEDNYPDENESSVLGSDYAPSGSGSGANSFYQSPTPSATGSGCDLMLRPPSNSMYHFNYRSPGSPMPVAPGVTNSRGLHPYAHSPAHGNPPGFYPNMWYPNAPYGSAGAAGSAGGAVSGGRYMGYGPGGVPGGTNSGPGAGPGAMQAAYPGHSAHMHALHHQYPQPHPHAHHPQHPHHSPHPHHPHPHETMMEMFQLSNSGREARNRAEKNRRDKLNGSIQELSTMVPHVAESPRRVDKTAVLRFAAHALRLKHAFGNSLMQQRPQITDTLMDMLDSFFLTLTCHGHILLISASIEQHLGHCQSDLYGQSIMQITHPEDQNMLKQQLIPTELENLFDAHGDSDAEGEPRQRSKAEEDAIDRKLREDRRSFRVRLARAGPRSEPTAYEVVKIDGCFRRSDEAPRGVRSNHFSSNLQLIRRTRGRDDVIPLHTISGNDIILTGCARIIRPPKIASRLIDANTLEYKTRHLIDGRIIDCDQRIGIVAGYMTDEVRNLSPFTFMHNDDVRWVIVALRQMYDCNSSYGESTYRLFTRNGNIIYLQSKGYLEIDKETNKVHSFVCVNTLLGEEEGKRRVQEMKKKFSVIINTQIPQSTIDVPASEHPALLEKAVLRLIQNLQKSGENGGHDDGDEDDDAQDGDDDEEDDDDDQDDGARSMSEFGDPYGSHHGRSHHGSSALSSHGHGNAKTPPLALVPPEASSVKSAITKSISVVNVTAAKHLRGIHASTAVKSPSSLGSCTCSDSHSPCDFCQGAPTTDLQAVGSNLKRGSTAHVETEEKLSKRRFIPSTEIEHVLHTSLDQIGRNLTQQLNVARNLREQSQRYELPHANQRFDEIMQEHQKQSELYVNIKSEYEVQLQHKASTRKSSDSDRNQEQPPPPLQEDDQD