wanglab/gogpt-training-data huggingface dataset:
Protein: HTH-type transcriptional regulator EcpR (B7UJE2)
Organism: Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Function: Part of the ecpRABCDE operon, which encodes the E.coli common pilus (ECP). ECP is found in both commensal and pathogenic strains and plays a dual role in early-stage biofilm development and host cell recognition (By similarity). Positively regulates the expression of the ecp operon by binding to two TTCCT boxes.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MTWQNDYSRDYEVKNHMECQNRSDKYIWSPHDAYFYKGLSELIVDIDRLIYLSLEKIRKDFVFINLNTDSLTEFINRDNEWLSAVKGKQVVLIAARKSEALANYWYYNSNIRGVVYAGLSRDIRKELAYVINGRFLRKDIKKDKITDREMEIIRMTAQGMLPKSIARIENCSVKTVYTHRRNAEAKLYSKLYKLVQ
Protein: Cytochrome b559 subunit alpha (PSII reaction center subunit V) (P0C368)
Organism: Oryza sativa (Rice)
Function: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00642}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00642}.
Interaction partners:
Sequence:
MSGSTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESRQGIPLITDRFDSLEQLDEFSRSF
Protein: Acetolactate synthase small subunit (AHAS) (ALS) (EC 2.2.1.6) (Acetohydroxy-acid synthase small subunit) (A0A0H2UNL0)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MRRMLTAKLQNRSGVLNRFTGVLSRRQVNIESISVGATEDPNVSRITIIIDVASHDEVEQIIKQLNRQIDVIRIRDITDKPHLEREVILVKMSAPAEKRAEILAIIQPFRATVVDVAPSSITIQMTGNAEKSEALLRVIRPYGIRNIARTGATGFTRD
Protein: GH26506p (Q95TE3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKVNFTEKNKIKESNSKQQVSSSISVMRSSKSKRIISLSRKDNIDSRDDILSKSGLQFCRKGAQLFSAIWSCACGEFAALSDGLLLKICWQSWSLQTVVPPLVNFYGAGRMVPHFGSMKMR
Protein: RNA-directed RNA polymerase (EC 2.7.7.48) (G5EE53)
Organism: Caenorhabditis elegans
Interaction partners:
- 3'-5' exonuclease eri-1
- Tudor domain-containing protein
- DRBM domain-containing protein
- Endoribonuclease dcr-1
- Piwi-like protein ergo-1
- Piwi domain-containing protein
- Helicase ATP-binding domain-containing protein
- Reverse transcriptase domain-containing protein
- Nuclear RNAi defective-3 protein
- RNA-directed RNA polymerase
Sequence:
MLPFDNDDSSDDATTSVRPKHPRGVPQSQSTFPRGRSNFSSGTLPNRKTECTPVNTLTIGHSNKMLLTTFRMDRNSKSKSEVDVQEQPVHSSSSAFPGNHLNNFSYPVNRGYLRDYLLQSQRPSTSKPVDCSVLKRHSLPSTHILYEKTKHRGGVNIEEQEKLVRMLWAAAEESETVAKTRQFSKKQAIELNFDAKLIGSMNNDCFGYCRAHMENIKDVLKTHLKLSKVDEVNWIKVGMVPRAAYEDKSYVIDAHLVLTPNGEVEDENELFSEFASSFTSRITGMLHDQVFLEVPKMHTLFTKITPQHMDINISAIAIGNCPNSGLFLVRGDFISQENTVCSVKLQSHHNADASRENSSFKVAGSNKYLSYARFEHDKRLAVVYFGVRLAEFADDGLDHAGFRLNLYYNLFVRIVVDMSHETTNSIYIQMKNPPHLWEGIPKNTIFHPSKSKVLNMETCTEWTRVLSWPGDAEGRGVGCTSEAFSQSSWIRLTMRKDDDNDSVSSTQLMDIVTRLSARSKAKVMFGSIFSIRRKLAPSPAFHSLGSFRANYALQALITRGSVFTDQLFDATDENIPSSDNDNDEDDDDDVDDTKKPMELVHEPLFLKLVRRGMKECSQATEETLEQLLNAFDERRQIDVVTAFTTMYQSRKIQYERLLKGESLQDVGLAKPLPKNCVSVAKVIVTPSRILLMAPEVMMVNRVVRRFGPDYALRCVFRDDNLGRLAIRDFSINNIDHMSNIVTEGIYLTLKNGIQVADRVYSFLGWSNSQMRDQGCYLYAPRVNALTGEVTGTVEDIRVWMGDFRDAISVPKMMSRMGQCFTQAQPTVRLERHHWIVEPDIEGGVENKYCFSDGCGRISIKLATHISKILQLKEVPACFQVRFKGFKGILVIDPTIDDIINMPKVIFRKSQQKFGEGGGELQDEYLEVVKYAMPSPVCLNRPFITILDQVSEKQSASSHRRITNRVHYYLERELCSLSNMLINENQAAEELVNRTNLAIDWNAASKRAGFELSVDPLIRDMLFSIYRYNIIHHISKAKIFLPPSLGRSMYGVVDETGLLQYGQVFIQYSPSIRQTSNRPILKTGKVLITKNPCHVPGDVRVFDAVWQPALAHLVDVVVFPQHGPRPHPDEMAGSDLDGDEYSIIWDQEMLLDYNEEAMVFPSSSAAEEDKEPTTDDMVEFFLRYLQQDSIGRMSHAHLAYADLHGLFHENCHAIALKCAVAVDFPKSGVPAEPLSSFEQCEMTPDYMMSGGKPMYYSTRLNGQLHRKARKVEEVLEEFETRGSVFEREYDKLICPEDVDVFFGNEIKLVQTLTLRDEYVDRMQQLLDEYGIEDEASVVSGHAASIKRLAGMERDDYSFYHTDKVVELRYEKLYAVFRAKFFEEFGGEEINIENDGKNTRLKCTKAMHEKIRQWYFVAYVQPKINKAGRCIGQSLPWVAWDALCDLRRQLMLDKNDAVLRGKYPIAARLEEEIENSIERQFDKFLKLKDLIESHKDALFLRRYVYFYGDQIIKMLFILKVWLERENVLPSSVLSIWQLGRLLIRLGLGDLLGNPTIDYEKSLLMPTTMFQQWISKKEDADEAPILRNFDMGTMMLEFLRYLASQSFASAESISLRVFYEKDIVEPILTKSAQWMPLHLIAYRTFHSIAVSGRFDALHLDDEDAVDQITESKDPILVNESLFSSRNYNDDYPISRSRILQSLKDWSGVKEIIPREITGTRKSDMIYVTSVGTVLARQRLARLLLLSGETIRDAIANNVVPNEVRDEFL
Protein: tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit wuho (Q9W415)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. Required during gametogenesis.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03056, ECO:0000269|PubMed:16762337}. Note=Localized to the nuclei of nurse cells, follicle cells and oocytes at early stages, from germarium to stage 4 egg chambers. Also present in the nuclei of spermatocytes and in the apical cells of the testes.
Interaction partners:
- tRNA
- SAGA complex subunit Spt7
- tRNA
- Pseudouridylate synthase 1 homolog
- tRNA
- LD10780p
- Ribosome assembly factor mrt4
- Ribosome biogenesis protein BOP1 homolog
- Protein HGH1 homolog
- Pescadillo homolog
Sequence:
MCTTISFAEPEIVLGHGRRVLFVNPDDLQIFKEIELPPDLGLKGHTSQSQESCTAAAAASTATAASGQAPGGKEQQLANQPEEGGTSASASGLGCATSTSVQNVAYSPDGQLLAVTTSGKQKALLLYRSRPENARLLSARPLARASSALRFCSDSSSILVTDKTGDCYQYDCVEVEAPPRLLLGHLSVVYDILWSEDQQHIITCDRDDKIRVTNYPATFDIHSYCLGHREFVSGLALLTEQHIASASGDKTLRVWNYIQGKELLQHELPAPAVRLLVRQLEPEKVFQAAVLFYEHVDALGLYRLERSSDDTWSVTATQLVCAEAGSWSISNFTLTSDRIYITGAENERLSLRVYDIATGQPASSGVPEGWLKMVLDGLGANEEGAPPFIPEDLSVWFKKRFDNVSDYLERKKRRIEEQQQQKCG
Protein: Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase (EC 3.2.1.113) (ER alpha-1,2-mannosidase) (Man(9)-alpha-mannosidase) (P32906)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in glycoprotein quality control as it is important for the targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations it further trims the carbohydrates to Man(5)GlcNAc(2).
Subcellular location: Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Interaction partners:
- Putative endoplasmic reticulum mannosidase MNL2
- Glucosidase 2 subunit alpha
- Protein RER1
- Alpha-1,2-mannosyltransferase ALG9
- Mannosyl-oligosaccharide glucosidase
- Alpha-mannosidase
- Protein OS-9 homolog
- Initiation-specific alpha-1,6-mannosyltransferase
- Calnexin homolog
Sequence:
MKNSVGISIATIVAIIAAIYYVPWYEHFERKSPGAGEMRDRIESMFLESWRDYSKHGWGYDVYGPIEHTSHNMPRGNQPLGWIIVDSVDTLMLMYNSSTLYKSEFEAEIQRSEHWINDVLDFDIDAEVNVFETTIRMLGGLLSAYHLSDVLEVGNKTVYLNKAIDLGDRLALAFLSTQTGIPYSSINLHSGQAVKNHADGGASSTAEFTTLQMEFKYLAYLTGNRTYWELVERVYEPLYKNNDLLNTYDGLVPIYTFPDTGKFGASTIRFGSRGDSFYEYLLKQYLLTHETLYYDLYRKSMEGMKKHLLAQSKPSSLWYIGEREQGLHGQLSPKMDHLVCFMGGLLASGSTEGLSIHEARRRPFFSLSLERKSDWDLAKGITDTCYQMYKQSSSGLAPEIVVFNDGNIKQDGWWRSSVGDFFVKPLDRHNLQRPETVESIMFMYHLSHDHKYREWGAEIATSFFENTCVDCNDPKLRRFTSLSDCITLPTKKSNNMESFWLAETLKYLYILFLDEFDLTKVVFNTEAHPFPVLDEEILKSQSLTTGWSL
Protein: Pumilio homolog 1 (S6B5C2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, P-body {ECO:0000256|ARBA:ARBA00004201}. Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}.
Interaction partners:
Sequence:
MSVACVLRRKAVLWQDSFSPHLRLPPPDRPLPSMPVVLSAAGHTPQPGPSPQAPAPTQGAGRSQDDAMVDYFFQRQHGDQPGYNNCKHRWPTGDNIHADNQVRSMDELNHDFQALALEGRAMGEQLLTGKKFWETDDSGKDGPKGIFLDQWRDSAWGASDHSVSQPIMVQRRPGQGFHGVGEAGSVLSPRSESGGLGVSMVEYVLSSSPAEKMDSCLRKGAYGPRDSEADDPEKRVEQKPKTTFDPERKELKETEPDVLDNPNGLPNQNGLDVDVKDFSRTPGNCPPTGQEVELGGPEMVGGAGPKPAEEFSNVETQNVTLDPMESVSMETLQFEYPGGQLPLDSTAATVGLFDYNSPQQLFQRPNALAVQQLTAAQQQQYALAAAQQPHIGLAPAAFVPNPYIISAAPPGTDPYAAGLAAAATLGPAVMPPQYYGVTPWGVYPANLFQQQAATPSNSANQQSAAQNQQNQQQVMRAGGNQRPLTPSQGQQGQQTEQLVAAAAVNSALAFGQGLAAGVPGYPVLAPAAYYDQTGALVVNTGARGGPVRLMAPASVIISPSAAVAAAAASAGGANAGLGGGASGAFRALSSQQAPGQQGSGALGGSSFYGSGSPSSSSQSSSLFSQGSAQPGNTSLGFNANPTSSLGATLGAALGGFGTAVANSSSSGSRRDSLTGSSDLYKRTASSLTPIGHGAFYNGLSFSSSPGPVGMPLPNQGPSHSLTPPPSLSTHGSSSSLNLGGLTNGSGRFISAAPGAEAKYRSATTGSSLFSPSSQLFPSSRLRYGMSDVMPSGRSRLLEDFRNNRYPNLQLREIAGHVMEFSQDQHGSRFIQLKLERASPAERQLVFNEILQAAYQLMVDVFGNYVIQKFFEFGSLDQKLALAERIRGHVLSLALQMYGCRVIQKALEFIPSDQQVINEMVRELDGHVLKCVKDQNGNHVVQKCIECVQPHALQFIIDAFKGQVFALSTHPYGCRVIQRILEHCLPEQTLSILEEIHQHTEQLVQDQYGNYVIQHVLEHGRAEDKSKIVSEIRGNVLGLSQHKFASNVVEKCVTHSLRAERAMLIDEVCSMADGPHSALYTMMKDQYANYVVQKMIDVAEPTQRKIVMHKIRPHIATLRKYTYGKHILAKLEKYYMKNGVDLGPLCAPPNGIM
Protein: Baculoviral IAP repeat-containing protein 1f (Neuronal apoptosis inhibitory protein 6) (Q9JIB6)
Organism: Mus musculus (Mouse)
Function: Sensor component of the NLRC4 inflammasome that specifically recognizes and binds flagellin from pathogenic bacteria. Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria. The NLRC4 inflammasome senses Gram-negative bacteria such as L.pneumophila and P.aeruginosa, enteric pathogens S.typhimurium (Salmonella) and S.flexneri. May contribute to prevent motor-neuron apoptosis induced by a variety of signals (By similarity).
Interaction partners:
- NLR family CARD domain-containing protein 4
- Baculoviral IAP repeat-containing protein 1e
- Caspase-1
- Baculoviral IAP repeat-containing protein 1b
- NACHT, LRR and PYD domains-containing protein 3
- Gasdermin-D
- NACHT, LRR and PYD domains-containing protein 6
- Interferon-inducible protein AIM2
- Apoptosis-associated speck-like protein containing a CARD
- ATP-dependent RNA helicase DDX3X
Sequence:
MAEHGESSEDRISEIDYEFLAELSARFGMNLVQLAKSQEEEDHKERMKMKKGFNSQMRSEAKRLKTFESYDTFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQGKDVGNIGKYDIRVKSPEKMLRGGKARYHEEEARLESFEDWPFYAHGTSPRALSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFLQSKKSSEEIAQYIQDYEGFVHVTGEHFVKSWVRRELPMVSAYCNDSVFTNEELRMDMFKDWPQESPVGFEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQTLKSSAEVIPTLQSQYALPEATETTRESNHDDAAAVHSTVVDLGRSEAQWFQEARSLSEQLRDTYTKTSFCHMNLPEVCSSLGTDHLLGCDVSIISKHVSQPVQGALTIPEVFSNLSSVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLYRFQLVFYLSLSSITPDQGLANIICTQLLGAGGCISEVCLSSSIQQLQHQVLFLLDDYSGLASLPQALHTLITKNYLFRTCLLIAVHTNRVRDIRPYLGTSLEIQEFPFYNTVFVLRKFFSHDIICVEKLIIYFSENKDLQGVYKTPLFVAAVCNDWNQNASAQDDFQDVTLFHSYMQYLSLKYKATAESLQATVSSCGQLALTGLFSSCFEFNSDDLAEAGVDEDVKLTTFLMSKFTAQRLRPVYRFLGPLFQEFLAAVRLTELLSSDRQEDQDLGLYYLRQIDSPLKAINSFNIFLYYVSSHSSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPQTFLWFQFVRGLWLVSPESFSSFVSEHLLRLALIFAYESNTVAECSPFILQFLRGRTLALRVLNLEYFWDHPESLLLLRSLKVSINGNKMSSYVDYSFKTYFENLQPPAINEEYTSAFEHVSEWRRNFAQDEEIIKNYENIWPRALPDISEGYWNLSPKPCKIPKLEVQVNNMGPADQALLQVLMEVFSASQSIEFHLFNSSGFLESIRPALELSKASVTKCSMSRLELSRAEQELLLTLPALQSLEVSETNQLPDQLFHNLHKFLGLKELCVRLDGKPDVLSVLPEEFLNLHHMEKLSIRTSTESDLSKLVKFIQNFPNLHVFHLKCDFLSNCESLMTALASCKKLREIEFSGQCFEAMTFVNILPNFVSLKILSLKGQQFADKETSEKFAQALGSLRNLEELLVPTGDGIHQVAKLIVRQCLQLPCLRVLAFHDILDDESVIEIARAATSGSFQKLENLDISMNHKITEEGYRNFFQALDNLPNLQMLNICRNIPGRIQVQATTVKALGHCVSRLPSLTRLGMLSWLLDEEDMKVINDVKERHPQSKRLTIFWKWIVPFSPVVLE
Protein: Hemoglobin subunit alpha-1/2 (Alpha-1/2-globin) (Hemoglobin alpha-1/2 chain) (P68240)
Organism: Ovis aries (Sheep)
Function: Involved in oxygen transport from the lung to the various peripheral tissues.
Interaction partners:
- Hemoglobin subunit beta
- Hemoglobin fetal subunit beta
- Globin domain-containing protein
- Haptoglobin
- Alpha hemoglobin stabilizing protein.
- Hemopexin
Sequence:
MVLSAADKSNVKAAWGKVGGNAGAYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGEKVAAALTKAVGHLDDLPGTLSDLSDLHAHKLRVDPVNFKLLSHSLLVTLACHLPNDFTPAVHASLDKFLANVSTVLTSKYR
Protein: Pantoate--beta-alanine ligase (EC 6.3.2.1) (Pantoate-activating enzyme) (Pantothenate synthetase) (P40459)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for pantothenic acid biosynthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- Pantothenate kinase CAB1
- 2-dehydropantoate 2-reductase
- Glutamate decarboxylase
- Aldehyde dehydrogenase [NAD
- Aldehyde dehydrogenase 5, mitochondrial
- Phosphopantothenate--cysteine ligase CAB2
- 4-aminobutyrate aminotransferase
- Aldehyde dehydrogenase [NAD
- Magnesium-activated aldehyde dehydrogenase, cytosolic
Sequence:
MKIFHTVEEVVQWRTQELRETRFRETIGFVPTMGCLHSGHASLISQSVKENTYTVVSIFVNPSQFAPTEDLDNYPRTLPDDIKLLESLKVDVLFAPNAHVMYPQGIPLDIEEQKGPFVSVLGLSEKLEGKTRPNFFRGVATVVTKLFNIVMADVAYFGQKDIQQFIVLQCMVDELFVNTRLQMMPIVRNNNGLALSSRNKYLCPESLKISENLYRGLKAAENAIRRLAPGGRLSRSEIIDTVTQIWAPYVDSHDFKIDYVSLADFKTLDELSDVENTSEQQPIVISCAVYVTDREKPDTVVRLIDNIVI
Protein: Limpet, isoform P (M9PFX9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLLKVCPCDDFQVQPKVVKKQPKFPTRERHMAIRRKKSTAMVTTTSENTAKCPEQRKTCQSCKCPREAHAIYQQQTTNVHERLGFKLVSPADSGVEARDLGFTWVPPGVRASSRINRYFEQLPDEMVPRLGSEGACSRERQISYQLPKQDLSLEHCKHLEVQHEASFEDFVTARNEIALDIAYIKDAPYDEHCAHCDNEIAAGELVVAAPKFVESVMWHPKCFTCSTCNSLLVDLTYCVHDDKVYCERHYAEMLKPRCAGCDELIFSGEYTKAMDKDWHSGHFCCWQCDESLTGQRYVIRDDHPYCIKCYENVFANTCEECNKIIGIDSKDLSYKDKHWHEACFLCFKCHLSLVDKQFGAKADKIYCGNCYDAQFASRCDGCGEVFRAGTKKMEYKTRQWHENCFCCCVCKTAIGTKSFIPREQEIYCAGCYEEKFATRCIKCNKVITSGGVTYKNEPWHRECFTCTHCNITLAGQRFTSRDEKPYCAECFGELFAKRCTACVKPITGIGGTRFISFEDRHWHHDCFVCASCKASLVGRGFITDGPDILCPDCAKQKLM
Protein: Erythrocyte membrane protein band 4.1-like 3 (A0A8I6AUN0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTTESGSDSESKPDQEAEPQEAAGPQEQAGAQAAPEPAGGNVEEQPGLEQFPEAAAHSTPVKREVSDKDRDFAAAAAKQLEYQQFEDDKLSQKSSSSKLSRSPLKIVKRPKSMQCKVTLLDGSEYGCDVDKRSRGQVLFDKVCEHLNLLEKDYFGLTYRDAENQKNWLDPAKEIKKQIRSGAWHFSFNVKFYPPDPAQLSEDITRYYLCLQLRDDIVSGRLPCSFVTLALLGSYTVQSELGDYDPDECGNDYISEFRFAPNHTKELEDKVIELHKSHRGMTPAEAEMHFLENAKKLSMYGVDLHHAKDSEGVEIMLGVCASGLLIYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQFESTIGFKLPNHRAAKRLWKVCVEHHTFFRLLLPEAPPKKFLTLGSKFRYSGRTQAQTRRASALIDRPAPYFERSSSKRYTMSRSLDGASVNENHEIYMKDSMSAAEVGTGQYATTKVISQTNLITTVTPEKKAEEEHVEEEDRRKKAEEATPVAALRHEGKVQSRKSLWKSDHKTQDELVKHQTNISELKRTFLETSTETALTNEWEKRLSTSPVRLAARQEDAPMIEPLVPEETKQSSGEKLMDGSEILSLLESARKPTEFIGGVSSTTQSWVQKLETKTETIETEVEPTPHPQPLSTEKVLQETVLVEERHVMNVHASGDASHTARDDVDATESAPADRHSGNGKEGSSVTEAAKEQRGEEADKSAPEQEQPATVSQEEDQVSAIHSSEGLEQKSHFESSTVKVESISVGSVSPGGVKLETSTKEVPVVHTETKTITYESSQVDPGADLEPGVLMSAQTITSETTSTTTTTHITKTVKGGISETRIEKRIVITGDADIDHDQALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED
Protein: FAD-dependent monooxygenase dbaB (EC 1.-.-.-) (Derivative of benzaldehyde biosynthesis cluster protein B) (Q5AUY3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives. The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produced by condensation of one acetyl-CoA starter unit with 4 malonyl-CoA units and one methylation step. The FAD-dependent monooxygenase dbaH is responsible for the synthesis of yellow pigments derived from the oxidation of DHMBA. The roles of dbaB, C, E and F have still to be determined (Probable).
Interaction partners:
Sequence:
MTRTSPTLPVIILGAGMVGLTLAQALKKAGIPYEVYERDSAADTEKGRGWALTVHWALNALEECLPAELFNRLEEIQVDPTLDDSRRFCFLDLSTAIPKYVIPPSKRLRVNRRLLGNLLGEGLDINYNKTLSSFHVSPETPDSVTVTFTDGTSTTGCLLVGTDGRNSKTRRLLLGEEAGALNPLPVRSIGTTITMTPEQFAPIREIDPLLFQGSHPETGVYMWFSLVSSPTINGSKDTPNPFYEGQLIQSWLYKSEKDAVPETDADRLALFKNNAQHFQRRLREAIETLPEDSKVLHIKLVDWVPVDWDNRGGRVTLAGDAAHAMTSYRGEAFNHGVADAAMLSRNIIAAWTNPGMTGGIADAPDSPIVSKRAKIAREARDARARAKLSEIAV
Protein: Uncharacterized protein C13E7.07 (Q9P6R3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGYEEAFFRWAFLIATVYVAYYFLVSSDKKLATKPQKSKLTKLGKQKQRQKQKNTKKDTLVNRETPSKKSQKLETSDALKSKSKDSSKKEPVVVPKKGTPKIFQENHKVKKVKSPKKEKLVGKNPAEKEDTTDVEDTQKLEQKHSTTPSSLKMKSSISLAAITADDSLHNSFSSNDIDDGFQTVTSSRSYGKKKSTEPLTKRQRQNQQKKLRAKEMQELADEEQRRRLAAHRKELHEANRPRGGLNNSSRSAYSYINNGQAGSSKGNRYDSLW
Protein: DNA-directed RNA polymerase subunit Rpo1C (EC 2.7.7.6) (DNA-directed RNA polymerase subunit A'') (DNA-directed RNA polymerase subunit C) (Rpo1'') (P11514)
Organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00411}.
Interaction partners:
- DNA-directed RNA polymerase subunit Rpo3
- DNA-directed RNA polymerase subunit Rpo5
- DNA-directed RNA polymerase subunit Rpo1N
- DNA-directed RNA polymerase subunit Rpo2
- DNA-directed RNA polymerase subunit Rpo7
- DNA-directed RNA polymerase subunit Rpo6
- DNA-directed RNA polymerase subunit Rpo11
- DNA-directed RNA polymerase subunit Rpo10
- DNA-directed RNA polymerase subunit Rpo12
- Probable translation initiation factor IF-2
Sequence:
MIDEKLKGYIDKRLNEIKDKIPDKLHEDLRAAIMDINGVELTEEDIDRIIDLTIREYQQSLIEPGEAIGVVTAQSVGEPGTQMTLRTFHFAGIRELNVTLGLPRLIEIVDARKVPSTPMMTIYLTDEYKTDKDKALDIARRIEYTRVENVVSSVSVDISNMSITLQFDQEMLKDKGVSIEEIKKIITKLKLGEIRIEDNDEYSFTIYFEKIDSIMALFKMREKILNTKIKGVKGIKRAIVQKKGDEYVIITDGSNLEGIMNVTGVDINKIQTNNIHEVEEVLGIEAARELISREIKKVLEEQGLDVDMRHIVLVSDIMTRTGDIRQIGRHGVTGEKSSVLARAAFEVTVKHLLDAAARGEREEFKGVIENIIIGQPIRLGTGIVELTMKPNMR
Protein: Centromere protein T (H3BTR4)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADHNPDSDSTPRTLLRRVLDTADPRTPRRPRSARAGARRALLETASPRKLSGQTRTIARGRSHGARSVGRSAHIQASGHLEEQTPRTLLKNILLTAPESSILMPESVVKPVPAPQAVQPSRQESSCGSLELQLPELEPPTTLAPGLLAPGRRKQRLRLSVFQQGVDQGLSLSQEPQGNADASSLTRSLNLTFATPLQPQSVQRPGLARRPPARRAVDVGAFLRDLRDTSLAPPNIVLEDTQPFSQPMVGSPNVYHSLPCTPHTGAEDAEQAAGRKTQSSGPGLQKNSPGKPAQFLAGEAEEVNAFALGFLSTSSGVSGEDEVEPLHDGVEEAEKKMEEEASPESASSTPESLQARRHHQFLEPAPAPGAAVLSSEPAEPLLVRHPPRPRTTGPRPRQDPHKAGLSHYVKLFSFYAKMPMERKALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVKPEDLELLMRRQGLVTDQVSLHVLVERHLPLEYRQLLIPCAYSGNSVFPAQ
Protein: Stevor (Q8IHM4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MNMYYLKMLLFNILINTLVLPHYENYLNNHYNVGLIQNKTKRATIKSRLLAQTQIHNPHYHNDPELKEIIDKMNEEAIKKYQKTHNPYKQLKEVVEKNGKKYTSGNDTEPMSTLEKELLETYEEVFGDEKDITLKSGINSNDDNRSDNSSTCECTDINNAKLAKTKGRDKYLKHLKWRCTRAICFCSVGSLFLTFIGLAAARATDVAALNITFNGINYSIYATYVTILNMFNEASMIAAIQAGVGATVDGLADMLTPAAASASAIFGGFGIAALVLLILAVALIILYIWLYKRRKRSWKHECKKHLCK
Protein: Dishevelled segment polarity protein 2 (I3L2N2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAGSSTGGGGVGETKVIYHLDEEETPYLVKIPVPAERITLGDFKSVLQRPAGAKYFFKSMDQDFGVVKEEISDDNARLPCFNGRVVSWLVSSDNPQPEMAPPVHEPRAELAPPAPPLPPLPPERTSGIGDSRPPSFHHENLEPETETESVVSLRRERPRRRDSSEHGAGGHRTGGPSRLERHLAGYESSSTLMTSELESTSLGDSDEEDTMSRFSSSTEQSSASRLLKRHRRRRKQRPPRLERTSSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDMNFENMSNDDAVRVLRDIVHKPGPIVLTVAKCWDPSPQAYFTLPRNEPIQPIDPAAWVSHSAALTGTFPAYPGSSSMSTITSGSSLPDGCEGRGLSVHTDMASVTKAMAAPESGLEVRDRMWLKITIPNAFLGSDVVDWLYHHVEGFPERREARKYASGLLKAGLIRHTVNKITFSEQCYYVFGDLSGGCESYLVNLSLNDNDGSSGASDQDTLAPLPGATPWPLLPTFSYQYPAPHPYSPQPPPYHELSSYTYGGGSASSQHSEGSRSSGSTRSDGGAGRTGRPEERAPESKSGSGSESEPSSRGGSLRRGGEASGTSDGGPPPSRGSTGGAPNLRAHPGLHPYGPPPGMALPYNPMMVVMMPPPPPPVPPAVQPPGAPPVRDLGSVPPELTASRQSFHMAMGNPSEFFVDVM
Protein: CAP-Gly domain-containing linker protein 1 homolog (P34531)
Organism: Caenorhabditis elegans
Interaction partners:
- Kinesin-like protein
- Calponin homology domain-containing protein
- EB1 C-terminal domain-containing protein
- Microtubule End Binding Protein
- Dynactin subunit 1
- Transmembrane protein
- Uncharacterized protein F10E9.1
- TOM1-like protein 2
- RING-type domain-containing protein
- Acyl_transf_3 domain-containing protein
Sequence:
MNKSHLGTADNPQEVVTAHDIGRLVDVVNVGKGFLRYVGPIHGKDGMFCGIELLEPNGKHDGTFQGVSYFIATPYHGIFAPIFRVTLDAEELPKPPPPNPSNRLSRSALPALQLRNPLTQERKPEEDVMSTSVYVSSSTKPIAIPTKQCRPPETDPMQMSMFSDMMDGSMFSNGSWSDIADSMITSNCTFTVRKGLPIDDDGDLMSVPMVQSVFNIDREALRREEQLQSSIVLGESRIGVEHLPIIEDENELETPLVETRTMPLPNDLNANFSNKNSTTTFVEPETPKVEIRENGNLDNSIETPPQQSPSGSSMVSHESDSSSKKDDTKSDKSPTKKSQKMEEKPVVKKKEEPAAPPPPPKFPVKQKAPSKHQLMMEQLKASIEAEKTKPKKEIKSRVSLLPPPAPKAPQKENKEGGEMTETPRRTITKTPLKTVNAKAKTSPTPPVERQKKERKPLYVAPPAKERVEKEKKIPSKPVVSPPTTAEKKPVVSSIPSTSSASKGPFPTSSFAGGKLQGPRKTSSSSTTTSAKKQKNPPIDEKEKLSRLQHSTHAFEATLIVMNRINEDNERKLGNISEQYEKKVSELGDLKKMLDEARKKFEEDVEQMKNSNQQVIRNHANAVESLQKTHETQIAEKNKEFERNFEEERARREAEVCAMNNRHQKVVACLDEKISEAEKQCEQLNVDKKVLQAALANDCDHRNQMLTKEISSLQTALEMKSAEMKELRQKNQNLSLQVDEIPLKELEISKWKHKSNEYKQMLDQKINGEKILVQQIEDLRRKQIHDEEEKEAMKRSFDLMQFKYENGDDPNVTSVMSAPMESRFSTPTKVQFRSRSSASGSRPISMATSNGGDQRLSTSSHHDDSMNRSTISMYTSHIRLPENHADDVIYAPDEIISSRSGSISQRLAISIENDGEPTIKSESSRIGNTSDSGIGLVM
Protein: Glucose-1-phosphate thymidylyltransferase (EC 2.7.7.24) (dTDP-glucose pyrophosphorylase) (dTDP-glucose synthase) (P55253)
Organism: Escherichia coli
Function: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.
Interaction partners:
Sequence:
MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQPSPDGLAQAFIIGEDFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDNNGTAISLEEKPLEPKSNYAVTGLYFYDNDVVEMARKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIEERQGLKVSCPEEIAYRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKGY
Protein: Protein mono-ADP-ribosyltransferase PARP16 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 15) (Poly [ADP-ribose] polymerase 16) (PARP-16) (Q8N5Y8)
Organism: Homo sapiens (Human)
Function: Intracellular mono-ADP-ribosyltransferase that plays a role in different processes, such as protein translation and unfolded protein response (UPR), through the mono-ADP-ribosylation of proteins involved in those processes. Acts as an inhibitor of protein translation by catalyzing mono-ADP-ribosylation of ribosomal subunits, such as RPL14 and RPS6, thereby inhibiting polysome assembly and mRNA loading. Mono-ADP-ribosylation of ribosomal subunits is promoted by NMNAT2. Involved in the unfolded protein response (UPR) by ADP-ribosylating and activating EIF2AK3 and ERN1, two important UPR effectors. May also mediate mono-ADP-ribosylation of karyopherin KPNB1 a nuclear import factor. May not modify proteins on arginine or cysteine residues compared to other mono-ADP-ribosyltransferases.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23103912}; Single-pass type IV membrane protein {ECO:0000269|PubMed:22701565}.
Interaction partners:
- Protein mono-ADP-ribosyltransferase PARP15
- Protein mono-ADP-ribosyltransferase PARP4
- Protein mono-ADP-ribosyltransferase PARP10
- Protein mono-ADP-ribosyltransferase PARP3
- Protein mono-ADP-ribosyltransferase TIPARP
- Protein mono-ADP-ribosyltransferase PARP12
- Protein mono-ADP-ribosyltransferase PARP14
- Protein mono-ADP-ribosyltransferase PARP11
- Poly [ADP-ribose] polymerase 2
Sequence:
MQPSGWAAAREAAGRDMLAADLRCSLFASALQSYKRDSVLRPFPASYARGDCKDFEALLADASKLPNLKELLQSSGDNHKRAWDLVSWILSSKVLTIHSAGKAEFEKIQKLTGAPHTPVPAPDFLFEIEYFDPANAKFYETKGERDLIYAFHGSRLENFHSIIHNGLHCHLNKTSLFGEGTYLTSDLSLALIYSPHGHGWQHSLLGPILSCVAVCEVIDHPDVKCQTKKKDSKEIDRRRARIKHSEGGDIPPKYFVVTNNQLLRVKYLLVYSQKPPKRASSQLSWFSSHWFTVMISLYLLLLLIVSVINSSAFQHFWNRAKR