wanglab/gogpt-training-data huggingface dataset:
Protein: 23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD (EC 2.1.1.190) (23S rRNA(m5U1939)-methyltransferase) (P55135)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Interaction partners:
- GTP pyrophosphokinase
- Ribosomal RNA small subunit methyltransferase F
- Ribosomal RNA large subunit methyltransferase I
- Ribosomal RNA large subunit methyltransferase K/L
- Protein UmuD
- tRNA pseudouridine synthase B
Sequence:
MAQFYSAKRRTTTRQIITVSVNDLDSFGQGVARHNGKTLFIPGLLPQENAEVTVTEDKKQYARAKVVRRLSDSPERETPRCPHFGVCGGCQQQHASVDLQQRSKSAALARLMKHDVSEVIADVPWGYRRRARLSLNYLPKTQQLQMGFRKAGSSDIVDVKQCPILAPQLEALLPKVRACLGSLQAMRHLGHVELVQATSGTLMILRHTAPLSSADREKLERFSHSEGLDLYLAPDSEILETVSGEMPWYDSNGLRLTFSPRDFIQVNAGVNQKMVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEEDVTKQPWAKNGFDKVLLDPARAGAAGVMQQIIKLEPIRIVYVSCNPATLARDSEALLKAGYTIARLAMLDMFPHTGHLESMVLFSRVK
Protein: DNA 3'-5' helicase (EC 5.6.2.4) (Q8I2W7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- DNA repair protein RAD51 homolog
- Exonuclease 1
- DNA topoisomerase
- DNA mismatch repair protein MLH
- DNA 3'-5' helicase
- Crossover junction endonuclease MUS81
- Double-strand break repair protein MRE11
- DNA repair endonuclease XPF, putative
- Uncharacterized protein
- Replication factor C subunit 1
Sequence:
MNEDAMKILNKCSGEKKKGEDLNSCNLLEYYKTKYSSIDIEKAKLILKEQFLIPDFREKQLECLNSIKRFEHVLNIMPTGGGKSLIYQVLPLIIEGISIVISPLISLIQDQIISLRNKKIVAETINSSLNKKENERILDILKSQDLGNLKVLYITPETATSGYFIDILYELYINKKISLISIDEVHCISTWGSDFRKSYRNLNKILDICPYVRTYCCTATATKFVEKDIIRNLNFYIFNKDCDNNINNNNINNNNNIHNNNKYDDHNNNCKVLNIVRTSFNRPNLKYIIIYSDLIKDEKKNSVCDIINEKRNKGKIGIIYCFKRNTCDEISKYLREKGIQALSYHAGLTNNTRKRIQQKWISGKTNILVATIAFGMGIDRKDVSFIIHYNLPKSIENYYQESGRCGRSGHISFCYLFYSKEDVEKLSYIIKTSFAHLDMHDVNIEKKYEKEIYNLECVHNLCINEKCIRSQILSYFGETYPNKNLQTNNTSDHNKQTYKNQTHVEKYNFDTANMYHPSDQNKDNLTDEHFCCSFCYDTKGSRIKIQKVINLYENKKGSNISQFYSKGETHEYNYLYTNNGKHKLYDDDTYYSPSGEEPREKRSTNYYNKYGDKYGDKYDDKYDDKYDEKYDDKYGDRKLQEGIYKLNNKKIKGYIPFQSASSIIPKQIRDKGIIEVMKELEKREEELNEKTKNDQEKHKVNKMNLFKSNSMNVKRKHVFSSFKIPRKI
Protein: Nucleoporin npp106 (Nuclear pore protein npp106) (O14310)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in promoting mRNA export from the nucleus.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:9372936}.
Interaction partners:
- Nucleoporin nup186
- Probable nucleoporin C890.06
- Nucleoporin nup189
- Nucleoporin nup184
- Nucleoporin nup44
- Nucleoporin nup107
- Nucleoporin nsp1
- Nucleoporin nup85
- Nucleoporin nup45
- Nucleoporin nup146
Sequence:
MESKEAKEKGVNTSDSKGSQIESSISDLREKSQHLFGVLLEPQVPVIQYGLNQLEEKARNLESKVLLTRDGDTKAHYLLAESGMNAEQTRQKIYSIHIHSPWDQLELDKKSLYEQPHTKLYNGQNVVASIENGYQSNVYEFQLRLMKNNGIAWENTKTEFMEDVGKLLHSKDNSGLGTSISMSLRPNLARPLLTASSVKSQSVRSLREVGSNLPIPTGSLTKIDGLNNQLSNDLTRSQTTNIFGFAEKASSFAAAVHKLNEARIRNQACHVWSLFASVSQMVNTEVIQLFDAWSLLAHMIDETRYGMGDFEARHLALDSSSAALAVEKNCIEGSLKYLENQFLSLIDLHLSDAGHITTVNSVEKVIAYSKLRFYKNGSWIKSTVSVVNDVPLWVVLFYLMRSGQLDAALQFVNTYSDDFEKLGRSFPLYFYSYAKNPSLPLPKQLRDRLQAEYGQLMKYAPEDPFKHAIYKLLGNCEPHRVSLPEVCVTSEDYMWIQLMFCRVNQNDVIDSNGGQSTNSLFNLYQLEKKIVAFGPRYFNPKNNTPTNYFLALLMCGEFERAISFLHTNYPVEATHFAVAMAYYGLLRTKNYEKNENILIYEADDVKINFPQLIIAYLKHLEYVDAAVYLDYIACIPLVPAYQACSINLTKILLLQSHEFSKFLGDIKPDTERTTGLLDLYLRLIPFDHDSLQKLYLEGAREADDDGRFGDSIILYHLLGDYDTVIGVAIKNLSQSIVSRGLWSIDSKESKNMHISSNVVASEAPDALAANLLAMYESNPKKSAKVSATNKKALKVLLKVVKVQKLYGQEKWDEVLQLIEHLDLLPINEVQAEFEPNEQIPPISARLRRRAFEFSTFQDEVLSVIPSLMYISMSSIKALYRTISKLPVVNEESKKKLQRLQFKGSMLVMFSTMIESRLSPQILEYLQAEQLTLL
Protein: Elongation factor Tu, mitochondrial (EF-Tu) (EC 3.6.5.3) (P49410)
Organism: Bos taurus (Bovine)
Function: Promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Also plays a role in the regulation of autophagy and innate immunity. Recruits ATG5-ATG12 and NLRX1 at mitochondria and serves as a checkpoint of the RIGI-MAVS pathway. In turn, inhibits RLR-mediated type I interferon while promoting autophagy.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P49411}.
Interaction partners:
- Elongation factor Ts, mitochondrial
- Large ribosomal subunit protein uL5
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Ribosomal protein
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein bL19m
Sequence:
MAAATLLRATPLFSGLGAGPAPLLQGLLRPLKAQALPVLCRGLAVEAKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPIIVGSALCALEQRDPELGLKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLGHSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVMAKPGSIQPHQKVEAQVYILTKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPGKELAMPGEDLKLTLILRQPMILEKGQRFTLRDGNRTIGTGLVTDTPAMTEEDKNIKWS
Protein: Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent) (PPi-dependent phosphofructokinase) (PPi-PFK) (Pyrophosphate-dependent 6-phosphofructose-1-kinase) (Q9EZ02)
Organism: Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01980}.
Interaction partners:
Sequence:
MTRISPLQKARYGYVPKLPPVLQDEIARIQAELGQPTEAVADREDLKRLFANTYGKPIATLTRGSNPEAGRRRTVGVILSGGPAPGGHNVICGLFDALKKANRESTLIGFKGGPSGILDDEWIEFTDSLINQYRNTGGFDIIGSGRTKIETPEQFAKALENAKKHGLDALVIIGGDDSNTNAALLAEYFVQQGAPIQVIGIPKTIDGDLKNEYIEASFGFDTATKVYAELIGNIARDAISSRKYWHFIRLMGRSASHIALECALQTHPNVCIVSEEVREKNMTLSQIVDQIVDAVVKRAAKGENFGVVLVPEGLIEFIPEVGALIDELNTLLAKEAEVFNRIDDPRERISWVKGKLSGNNQHVFSSLPETIQAQLLMDRDPHGNVQVSRIETEKLLIEMVSSRLKALKEEGAYKGKFSALNHFFGYEARCAFPSNFDADYCYALGFTAFVLIANGLTGYIAAIKNLARPAVEWKPMGIPLTMMMNMEKRHGKMKPVIRKALVDLEGAPFKRFATQRDAWATESAYVFPGAIQYYGPDDVCNQPTMTLKLEQGLE
Protein: Fatty acyl-CoA reductase (EC 1.2.1.84) (Q0E8W1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTVDLSPVQEYYKDKTIFITGASGFMGKVLLEKLLYSCHSLKEVIIICRPKRGKAPETRLEEMFKLPIFQRIKDERPEMLKRVTIYQGDVTFDQLGLSGESLKHVTENTNIVFHMAATLKLEGNLRDAIDMNLLGTRRALNVAKEMKQLEAFIHLSTAFCNCDQDVMYEKVYEFPHKPEDLMRLAEWMDVKTLDAITPDLLKPHPNTYTYSKRLAELLVRDHYESMPVIIARPSIVSPSAYEPVPGWVDNLNGPTGLMVGAGKGVIRSMLIDTRHLSEVIPVDYAINGLCVIPYQFAKMTERPKDVPVYNITCADHRKMQWGEVIEMSKEIGYRYPMEAGLWYPDGCITTNKLHHNINVLLFHWLPAYLIDFILLLLGQKRFMIRVQNRISVGLEVLQFFTMRAWFFKSDAYSSLWAMLNESDRKNFNMDMDPEETVPMYIESCVQGGRQYLMKESPDSLPRARLQLKLMYILDRACKTLIVGTLCYWTYGLVARLLGV
Protein: ABC-type transporter cicA (Cichorine biosynthesis cluster protein A) (A0A1U8QTJ9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: ABC-type transporter; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans. CicA is probably involved in the secretion of cichorine (Probable).
Subcellular location: Cell membrane {ECO:0000305|PubMed:24244835}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MRLSSEAKIAESGGQPPTAGSRSETGSESTEAESADPKAQKWYQRSLNPLRWQKIPPVPEERTVSREYGASFFSIASFQWMAPLMKVGYLRPLELQDIWTVNPDREVDVLTKRFEVSLEKRTNAGAKRPLLWALYDTFRFEFLLGGFCHLISSLLIVFAPYLTRYQIAFATEAYVAQRSGQPAPRIGRGMGFVVGITVMQAIQSLCTNQFLYRGQMVGGQIRAVLILQIFNKAMKLSGRAKAGGVQSPEQQEKIKELKAAKDQALKKPGSPPADDKGWGNGRIVALMSIDVDRINLACGMFHISWTAPVSIIVALILLLVNLTYSALAGFGLLVIGMPFLTYAVRFLFKRRRNINKLTDQRVSLTQEILQGVRFVKFFGWESSFLDRLKEIRHHEIRSIQTLLAVRNGILCVSMAIPVFASMLSFITYALSNHVLDPAPIFSSLALFNSLRMPLNLLPLVLGQITDAWTALNRIQEFIVAEEQKEDIERDEHMPEAVRMDRASFTWERKAADKEAEKVEKKANPRRTEPKSEAPTDSAESDEPFQLRDMTLDIRRDELVAVIGTVGSGKSSLLAALAGDMRLTDGSVRLSTSRAFCPQYTWIQNTSLRDNILFGKDYDEKWYDQVIDACALKPDLEILPNGDATEIGERGITISGGQKQRLNIARAIYFNAELVLLDDPLSAVDAHVGRHIMDKAICGLLKGRCRILATHQLHVLSRCDRIVVMDDGRIHAVGTFDELSRDNDLFKQLMSTASQDSKEDEEEATEVVEEEAEKQAQQEPTKPAAALMQQEEKATDSVGWTVWKAYIRASGSYFNALAILFLLAFANVVNVWTNLWLSYWTSNHYPSLSTGQYIGIYAGLGAGSALTMFIFSTYMSTAGTNASRQMLQLAMTRVLRAPMSFFDTTPLGRITNRFSKDIGVMDNELCDAMRMYAITITMIVSIMILIIVFYHYFAIALVPLFLLFLTASNYYRSSAREMKRHESILRSAVYARFSEAITGTASIRAYGVQNQFRSSLRDSVDTMNGAYFLTFSNQRWLSVRLDAVAVLLVFVTGVLVVTSRFDVSPSISGLVLSYILAIAQMLQFTVRQLAEVENNMNATERVHYYGTQLEEEAPAHIPSNPVPESWPPHGEITFDNVAMRYRPGLPLVLKNLSMNISGGERIGIVGRTGAGKSSIMSALFRLTELSSGRITIDGVDISTIGLHDLRSRLAIIPQDPTLFRGSIRSNLDPFNEHSDLELWDALRKAHLIDSDTKDSAVDASNPNGNANAQRLTLDTAVDEEGLTFSLGQRQLMALARALVRNARIIICDEATSSVDFATDQRIQETMAQGFEGKTLLCIAHRLKTIIHYDRICVMDQGSIAEIDTPLNLWEKEDGIFRAMCERSGISREDIVGQVEKE
Protein: Guanine nucleotide-binding protein subunit beta-like protein (Q4GZE2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFAPPECTIEGELPLKCESPFSSVYRDPQGAVWTVDSTSTRVFRFPRVVVCPNSAPGHSSPAPKGSDELDQPYFDCSEENDRVLSVVFTTVRDDERFFVCIATAGGCIAFGVADSFEGDIRRVQLGVEVTALAAAPCTDGASAKDCDDGNEDLLETTSLCSSGYGGGVLVSSFDGTFSEVMLLCWVSGSCAADLPQRDSDVDVVGLFRVQGRVCGLMVDEVGDRVVTVTQRGDVDVWNLRANVDETHTFGMPAYLASEYGEPCCSILLGGYQLWIGTSKGFVIVFFLQPLGNVVSNDNSPCISHTKCNVDESKGSRGAPHRVWHAHGATAVRSLLVMSLGRLVWSYGADQQANVWDTTELLLRGSLQFPCGDLSELCCGGQYLDTSVWGVCSESGKLTQFRVKELLFGGSRGLAAALCGPTSNEQMERCNVLSSFVSYLCSLLNPTSEQPHASSTMITAATDESNCSYGLSLNGDGDTDTDKYETDTLCLPPHMEVVVKQMEQCYPASHLLPHAVTSLVKGQRIVSQLTANERRGSATFLDGLRHLQRQHQQDSYDLKALRLQVGEERKKRQDAEARLAERENETHEYQQRLERLTVLQEECEKRTATLERQLKSAKKAAAVTSAEATRLCEMEANLHEAHCTVQGLQERMESLVRERQEYLRVSQENKSLRAQVRRFELKQQAAKRALANFIATQDHIVDSLGNILLVDEGGDHRRAHADIDNLYEWLCRNIENQQEFLAGLKRSYETQAGGVAEDRIGQ
Protein: Protocadherin 11 X-linked (Protocadherin 11 isoform 9) (Q2TJH9)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
RCRQPPHLKASQKNKQNSEWVTPNPENRQMIMMKKKKKKKKKHPPKNLLLNFVTIEEAKPDDGENERNSVTLDLPIELEEQTMGKYNWGTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKHHIIQELPLDNTFVGCDSISKCSSSSSDPYSVSECSYPVTTFKAPVSVHIRPTMKEVVRSHTPMKEATTVEIWTHPHPQRRSDGKKAGKSQRRVTFHLPEGSQESISDGGLGDHDAGSLPSTSHALPLGYPQEEYFDHAAPNNRTEGDGNSDPESIPLHPSKTTASRSFHIHHTLLSN
Protein: Microtubule-associated protein 6 (MAP-6) (145-kDa STOP) (STOP145) (Stable tubule-only polypeptide) (STOP) (Q63560)
Organism: Rattus norvegicus (Rat)
Function: Involved in microtubule stabilization in many cell types, including neuronal cells. Specifically has microtubule cold stabilizing activity. Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with TMEM106B (By similarity). Regulates KIF5A-mediated axonal cargo transport. Regulates axonal growth during neuron polarization.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14724383, ECO:0000269|PubMed:28521134, ECO:0000269|PubMed:3456161, ECO:0000269|PubMed:8700896, ECO:0000269|PubMed:9660871}. Golgi apparatus {ECO:0000269|PubMed:28521134}. Cell projection, axon {ECO:0000269|PubMed:28521134, ECO:0000269|PubMed:9660871}. Cell projection, dendrite {ECO:0000269|PubMed:28521134}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:28521134}; Lipid-anchor {ECO:0000269|PubMed:28521134}; Cytoplasmic side {ECO:0000269|PubMed:28521134}. Note=Isoform 1 and isoform 2 associate with axonal microtubules in neuronal cells (PubMed:8700896, PubMed:9660871). Localizes predominantly in the proximal part of the axon (PubMed:28521134). Preferentially concentrated on a portion of the microtubule polymer in which tubulin is modified by detyrosination and acetylation and is also resistant to depolymerization induced by both nocodazole and cold (PubMed:14724383, PubMed:28521134, PubMed:9660871). In unpolarized neurons, localizes to the Golgi and to secretory vesicles accumulating transiently at the tips of a subset of neurites (PubMed:28521134). Following neuronal polarization and during axon outgrowth, accumulates in the axonal growth cone and subsequently localizes throughout the axon (PubMed:28521134). Partially localizes to dendrites in mature neurons (PubMed:28521134). {ECO:0000269|PubMed:14724383, ECO:0000269|PubMed:28521134, ECO:0000269|PubMed:8700896, ECO:0000269|PubMed:9660871}.
Interaction partners:
- Transmembrane protein 106B
Sequence:
MAWPCITRACCIARFWNQLDKADIAVPLVFTKYSEATEHPGAPPQPPAPPQPGLAPPSRAVAIETQPAQGESDAVARATGPAPGPSGDRETAAAPGRSGLGLGAASGSTSGSGPADSVMRQDYRAWKVQRPEPSCRPRSEYQPSDAPFERETQYQKDFRAWPLPRRGDHPWIPKPVQIPATSQPSPPVLGMPKRRPQSQERGPIQLSADARDPEGAGGAGVPAAGKASGADQRDTRRKAGPAWMVTRTEGHEEKPLPPAQSQTQEGGPAAGKASGADQRDTRRKAGPAWMVTRTEGHEEKPLPPAQSQTQEGGPAAGKASGADQRDTRRKAGPAWMVTRTEGHEETPLPPAQSQTQEGGPAAGKASGADQRDTRRKAGPAWMVTRTEGHEETPLPPAQSQTQEGGPAAGKASGADERDTRRKAGPAWMVRRSEGHEQTTAAHAQGTGPEGGKGRAVADALNRQIREEVTSTVSSSYRNEFRAWTDIKPVKPIKAKPQYKPPDDKMVHETSYSAQFKGEASKPTTADNKVVDRRRIRSLYSEPFKESPKVEKPSVQSSKPKKTSTSQKPLRKAKDKQVASGQAAKKKTTESPSATKPDDKEQSKEMNNKLAEAKESRVKPTSDKNQGPVAKEPHKDQGPVAPGLPKGQGPAVQEPLKDQGPMVPGLPKDQAPVVPGSLKGQSPTAPGPPKDQGAVLLGPMKDLGPVAPASVKDQDHMASELLKNKDSVPLAPAKAQSPLLPEPLKNQSPVVPARAKDQSFPAPAPTPLKDPGPVIPEPEKDGAPMVPERRKDQNASIMASLKNEAPVASESVKNQGLGGPEPAKDTGTDLKGHGSVFVAPVKSQGPVVPEPTKGQDPIIPALAKDQGPILPEPPKNQGPPVVLGPIKNQDPVIPVPLKGQDPVVPAPTKDPGPTAPDPLKSQGPRGPQLPTVSPSPPVMIPTVPHAEYIEGSP
Protein: Nuclear fallout, isoform M (M9NFB1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004654}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004654}.
Interaction partners:
Sequence:
MYSDISLENRHDYDYRLELLQRKVDDLSDTQNIAEDRTTRTKTEYAVLQARYHMLEEQYRESELRAEERLAEEQKRHREILARVEREASLQNENCQMKIRATEIEATALREEAARLRVLCDKQANDLHRTEEQLELARDQIGVLQQEHEEQAQALRRHEQEKKSTEELMLELGRELQRAREESGARAMPTTSPESIRLEELHQELEEMRQKNRTLEEQNEELQATMLTNQATMLTNGVEQGRHLLNGTLNSLAQELEEMSQAQDSVDSATLASLSQLQQAFQEKEDENVRLKHYIDTILLNIVENYPQLLEVKPMERK
Protein: UPF0337 protein YjbJ (P68206)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Osmotically-inducible protein Y
- UPF0391 membrane protein YtjA
- Uncharacterized lipoprotein YgdR
- Uncharacterized protein YgaM
- Uncharacterized protein YbgS
- Uncharacterized lipoprotein YgdI
- Potassium binding protein Kbp
- Uncharacterized protein YahO
- Peroxiredoxin OsmC
Sequence:
MNKDEAGGNWKQFKGKVKEQWGKLTDDDMTIIEGKRDQLVGKIQERYGYQKDQAEKEVVDWETRNEYRW
Protein: Polyketide synthase RzxF (Q4KCD3)
Organism: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- AMP-binding enzyme
- L-cysteine--[L-cysteinyl-carrier protein] ligase
- Non-ribosomal peptide synthetase OfaB
- Non-ribosomal peptide synthetase PvdJ
- Non-ribosomal peptide synthetase OfaA
- L-cysteine--[L-cysteinyl-carrier protein] ligase
- Non-ribosomal peptide synthetase PvdL
- NADH-quinone oxidoreductase subunit C/D
- [acyl-carrier-protein] S-malonyltransferase
- Non-ribosomal peptide synthetase PvdD
Sequence:
MDNTTLNDTQDIRLPNQRPTQQPPHTQAPRLRRQIGAGPQGAVAAPVQPPRVAIVGFSGRFPGADTAEQFWQLLLEERASISELPYWHLPGIAERVQLRETFTCPGGFINDPSAFDADFFKISAREAEAMDPQHRLVLEQTWAAFEDAAICPHDLRGSNTGVFIGISSADYNGLLARSEAGAHDATGNAHSIIANRISFVFDFHGPSAPIDTACSSSLVAVHRAAQSILNGDCTVAVAGGVNLCFEPMVFIGALKAGMLSPTGRCKAFAADADGYVRGEGVGVLILKDYQQALADGDNIVAAIIGSAENHGGHANSLTAPNPRAQADLIKQACRGIDINSIGYIEVHGTGTRLGDPIEISGLKQAFAELGANPEQRCYLGSVKTNIGHLESAAGIAGVIKTLLVLKQGYLPKSLHSEQLNPYIDLAGSPFAVLQTGREWPQVSDRQGQALPRRAGVSSFGFGGANAHVVLEAVEPVIPGNEPQGAASVFVLSAKTPEALQSRIEQLIDFVQRQPQLQLAELAVSLQLGREAMEYRCGFVAHSRDSLLSQLRDSGAGEGGPPAGKIAPEPLHRALQQRDLGTLLSLWQQGATLDWRQLYEQPRPRRISLPTYPFNRERYWISEAPAASPTGAASLHPLVQRNTSDLAGQRFSSRFDGNEWFFSGHRVNGRKVLPGVAYLEMARAAVERSMVDADAVVALKHVAWRQPMVHDGGDLDIDIELVEQGEGQIRFEIRGSAADGPSYCTGVALVGSAERLVPLDLGTIAGVTNQQRLTPEQCYQVFGEMGLAYGESFRRINTLQAGNGQVLASLLRGEQAPGCELPPGLLDSALQAALGLALLEPLQAQREHQPLVPFALDRVVLGELDLLKQPCQAWVRYSADHQPGRINKLDLDICDEQGRIALRLQGFSSRKLAAAPPSMLAMTPVWRDKALIDPPQRSLARQLIVLAGAQSQDLDLLTQRCQALVGNRRQIHIVPLPVVTQDPAIALPALAGFVIELVQKSPANSLVQLVLADLEHAGPVFASLLALLKTAKNEGLIDAAQCIELQGSLQPQWLVDNALQDDERVRYRDGQRQVASWQETQLAQGTAPQWREGGVYLLSGGTGGLGLLLAEQLARQGLGVRLILASRSAGQLSPEASQRVAAIRALGAQVQLHALDIADRGAVEALIAQCEQEWGTLNGIFHCAGITRDSLLQHKNATDLAAVLAPKVAGVLNLDRASAHLPLDCFVLYSSVSAVIGNPGQGDYALANAYLDEWAGWRGAQVRAGRRQGRTLAINWPLWRNGGLQIDGQREQQMIELTGIEPLSDSGGLGFLQQALAQASDAERWMVLEGDIAKIKRFIAGQWQQDRFEEPPAPQEMPAAIALAPSTPLAASVEGDLQALAIRYFKQLLSTTLKRPLEKIDSDASFERYGADSIMLTELTRQLERLFGSLPNTLLYEYQTVRELSAYFIGQHAQRLDQWLRPEGAKASAPGEETSLIAQAPVRQRARNRQQCETPAVAGNSRDLAIIGISGRYPGAADLETFWHKLAGGEDLISEVPSARWDHQAYFDPARDRFDKTYCKWGGFLEGVEDFDPLFFNLSPREAHIINPNDRLFLETCWNLLESAGLTRQQIQQRYQQQVGVFVGVMYQQYQAFESDLVRESLVSVTSYSAIANRVSYFFDFQGPSLAIDTMCSSSISAIHAAGEALRNGDCRLAIAGGVNLTLHPKKYIGLSVGQVLGSHAGSRSFADGDGYLPAEGVGAVLLKTLADAERDGDPILAVIKSTAVNHGGHTHGFSVPSAKLQAALIDSNFKRAGIDPCTLSYVESAANGSEMGDAIELSALSRVFSAAGVAPQSCAIGSVKSNIGHAEAASGMSALSKLVLQLQHRQLAPSLLLGELNPKLDFAHSPFVLQRTLTEWPQPVLEIDGVEQPVPRRACLSAFGAGGSNAHLIIEEYSSAPIPDLAASEPGLLQIVPLSAHSSAALQQGLERLARHLDRHPQVRLQDLAHTLQNGREAMPLRLALRVSSTAQLRGLLAEILQRLQQGQALASLDSTDLPLALGNVDEVPAALASLLSGPGAAALSAGLIAAADLQQLALLWTQGGEIPWHALGHNTGAALIPLPTYAFDKQRYWLEQPSAVKALHEPLTAAGSTRHVVGQKPPTAAEQGRQLLADLLGMQPQDLSPSKPLSAYGADSIVMLQWAMQVQAQIDPGLALADIQQCQTLGDVLQRLSRDATPTGVAESVLPAQILGLLSGSTTRFPELQRLNPVQQGRPVFWFHGALGGSEIYQGLAQHIQRPFFGLQARGWMTDRAPLQGIQAMAAYYVQVIQSVQPQGPYDLGGYSLGGMLAYEVTRQLQELGETVISLVMLDSPDVTGERSARLADKTRLLQTVNMSLQMTLGQTPERFAEVLIHRDEIDLALSPADYLQQLTDLARQRGLKTSDQRLQQLMAQVTQIQQAYQVEHYRIQPLPRAAEVACYYFRNASGLWMGDLEPFFSTDSQEFAAFNHADYWQEWQRQLPNFEMIEVASANHMTLLTQPEVFRVIAQFCATLYGQRSVENAVG
Protein: DNA-directed RNA polymerase, mitochondrial (EC 2.7.7.6) (P13433)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Mitochondrion.
Interaction partners:
- Mitochondrial transcription factor 1
- Mitochondrial translation factor 2
- Dimethyladenosine transferase
- ARS-binding factor 2
- ATP-dependent RNA helicase MSS116, mitochondrial
- Putative uncharacterized protein Q0092
- Mitochondrial COX1 translation regulator PET309
- Non-histone chromosomal protein 6A
- Mitochondrial genome maintenance protein MGM101
- DNA-directed RNA polymerase I subunit RPA135
Sequence:
MLRPAYKSLVKTSLLQRRLISSKGSKLFKPSPDSTSTILISEDPLVTGSSPTSSTTSGIISSNDFPLFNKNRKDAKSSISYQWKNPSELEFDPFNKSHASAVTSMTRTRDVMQLWSLLEACLQSNLMKRAFSILESLYLVPEHKQRFIEDYNMYLNSFSKNDPNFPILKMNEKLTNDLETSFKDVNYNDKTLAIMIHHALNFHSTTSSMLLKPIISAYLKMSVNGIREIFSCLDILTISDLNILMNDLKVITPSQLPNSVRPILESLTLSPTPVNNIENEEGLNKVEAENDSKLHKASNASSDSIKKPSLDPLREVSFHGSTEVLSKDAEKLIAVDTIGMRVIRHTLLGLSLTPEQKEQISKFKFDANDNVLKMKPTKNDDNNNSINFFEIYNSLPTLEEKKAFESALNIFNQDRQKVLENRATEAARERWKHDFEEAKARGDISIEKNLNVKLWKWYNEMLPLVKEEINHCRSLLSEKLSDKKGLNKVDTNRLGYGPYLTLIDPGKMCVITILELLKLNSTGGVIEGMRTARAVISVGKAIEMEFRSEQVLKSESQAFRDVNKKSPEFKKLVQNAKSVFRSSQIEQSKILWPQSIRARIGSVLISMLIQVAKVSVQGVDPVTKAKVHGEAPAFAHGYQYHNGSKLGVLKIHKTLIRQLNGERLIASVQPQLLPMLVEPKPWVNWRSGGYHYTQSTLLRTKDSPEQVAYLKAASDNGDIDRVYDGLNVLGRTPWTVNRKVFDVVSQVWNKGEGFLDIPGAQDEMVLPPAPPKNSDPSILRAWKLQVKTIANKFSSDRSNRCDTNYKLEIARAFLGEKLYFPHNLDFRGRAYPLSPHFNHLGNDMSRGLLIFWHGKKLGPSGLKWLKIHLSNLFGFDKLPLKDRVAFTESHLQDIKDSAENPLTGDRWWTTADKPWQALATCFELNEVMKMDNPEEFISHQPVHQDGTCNGLQHYAALGGDVEGATQVNLVPSDKPQDVYAHVARLVQKRLEIAAEKGDENAKILKDKITRKVVKQTVMTNVYGVTYVGATFQIAKQLSPIFDDRKESLDFSKYLTKHVFSAIRELFHSAHLIQDWLGESAKRISKSIRLDVDEKSFKNGNKPDFMSSVIWTTPLGLPIVQPYREESKKQVETNLQTVFISDPFAVNPVNARRQKAGLPPNFIHSLDASHMLLSAAECGKQGLDFASVHDSYWTHASDIDTMNVVLREQFIKLHEVDLVLRLKEEFDQRYKNYVKIGKLKRSTDLAQKIIRIRKDLSRKLGRSTTLADEIYFEKKRQELLNSPLIEDRNVGEKMVTTVSLFEDITDLDALELENGGDENSGMSVLLPLRLPEIPPKGDFDVTVLRNSQYFFS
Protein: Large ribosomal subunit protein uL2y (60S ribosomal protein L8-2) (Q4PSL7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS1z
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL22y
- Large ribosomal subunit protein eL32z
- Large ribosomal subunit protein uL24y
- Large ribosomal subunit protein uL24z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein eL8y
- Large ribosomal subunit protein uL4y
- Large ribosomal subunit protein uL6x
Sequence:
MGRVIRAQRKGAAGSVFKSHTHHRKGPAKFRSLDYGERNGYLKGLVTEIIHDPGRGAPLARVAFRHPFRYMKQKELFVAAEGMYTGQYLYCGKKANLMVGNVLPLGSIPEGAVICNVELHVGDRGALARASGDYAIVIAHNPESNTTRVKLPSGSKKILPSACRAMIGQVAGGGRTEKPLLKAGNAYHKYKAKRNCWPVVRGVAMNPVEHPHGGGNHQHIGHASTVRRDKSAGAKVGQIAARRTGRRRGAAATLAAKADY
Protein: RAD54 like (A0A590UJ71)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRRSLAPSQLAKRKPEGRSCDDEDWQPGLVTPRKRKSSSETQIQECFLSPFRKPLSQLTNQPPCLDSSQHEAFIRSILSKPFKVPIPNYQGPLGSRALGLKRAGVRRALHDPLEKDALVLYEPPPLSAHDQLKLDKEKLPVHVVVDPILSKVLRPHQREGVKFLWECVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECKPEIDKAVVVSPSSLVKNW
Protein: Steroid 3-ketoacyl-CoA thiolase (EC 2.3.1.16) (Acetyl-CoA acetyltransferase FadA5) (Beta-ketoacyl-CoA thiolase) (I6XHI4)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the beta-oxidation of the cholesterol side chain. It is important for utilization of cholesterol as a sole carbon source in vitro and for full virulence in the chronic stage of mouse lung infection. Catalyzes the thiolysis of 3,22-dioxochol-4-en-24-oyl-CoA to yield 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) and acetyl-CoA. Also able to use acetoacetyl-CoA (AcAcCoA) as substrate.
Interaction partners:
- Probable fatty oxidation protein FadB
- Acyl-CoA dehydrogenase FadE29
- Acyl-CoA dehydrogenase FadE28
- Probable 3-hydroxybutyryl-CoA dehydrogenase FadB3
- 3-hydroxybutyryl-CoA dehydrogenase
- Probable lipid carrier protein or keto acyl-CoA thiolase Ltp3
- Enoyl-CoA hydratase EchA19
- 3-oxo-4,17-pregnadiene-20-carboxyl-CoA hydratase alpha subunit
- 17-hydroxy-3-oxo-4-pregnene-20-carboxyl-CoA lyase
- Acyl-CoA dehydrogenase FadE34
Sequence:
MGYPVIVEATRSPIGKRNGWLSGLHATELLGAVQKAVVDKAGIQSGLHAGDVEQVIGGCVTQFGEQSNNISRVAWLTAGLPEHVGATTVDCQCGSGQQANHLIAGLIAAGAIDVGIACGIEAMSRVGLGANAGPDRSLIRAQSWDIDLPNQFEAAERIAKRRGITREDVDVFGLESQRRAQRAWAEGRFDREISPIQAPVLDEQNQPTGERRLVFRDQGLRETTMAGLGELKPVLEGGIHTAGTSSQISDGAAAVLWMDEAVARAHGLTPRARIVAQALVGAEPYYHLDGPVQSTAKVLEKAGMKIGDIDIVEINEAFASVVLSWARVHEPDMDRVNVNGGAIALGHPVGCTGSRLITTALHELERTDQSLALITMCAGGALSTGTIIERI
Protein: Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.8.7) (Q5T4U5)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCDYSVCPLLEACTLYLDAFFLLLTGSNLNLHLNLGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYKN
Protein: Uncharacterized protein At5g65207 (Q8RXW8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F18C1.18 protein
- Hypoxia-responsive family protein
- F3I6.9 protein
Sequence:
MADIAILVAEEYERRMKHTTVGSRSSPVEFDWWKIIPAKMTIAFDKMKIESLKKNFEAKSEFALAISHGFFSA