wanglab/gogpt-training-data huggingface dataset:
Protein: Probable NADP-dependent mannitol dehydrogenase (MtDH) (EC 1.1.1.138) (Mannitol 2-dehydrogenase [NADP(+)]) (Short chain dehydrogenase/reductase) (YlSDR) (Q6CEE9)
Organism: Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Function: Versatile oxidoreductase that catalyzes the oxidation and reduction of polar as well as non-polar substrates at a very broad pH range. Preferentially oxidizes secondary alcohols. Has highest activity for racemic 2-heptanol and racemic octanol. Is also an efficient reductase for selected substrates. Substrate selectivity was found for medium chain length ketones with the carbonyl function at position C-2. Has highest activities for ribulose and fructose. The enzyme is (R)-selective in the reduction direction and produces exclusively the (R)-enantiomer.
Interaction partners:
- YALI0E05643p
- YALI0D18964p
Sequence:
MPAPATYATGLTPLPTPVPKVSKNIMERFSLKGKVASITGSSSGIGFAVAEAFAQAGADVAIWYNSKPSDEKAEYLSKTYGVRSKAYKCAVTNAKQVETTIQTIEKDFGKIDIFIANAGIPWTAGPMIDVPNNEEWDKVVDLDLNGAYYCAKYAGQIFKKQGYGSFIFTASMSGHIVNIPQMQACYNAAKCAVLHLSRSLAVEWAGFARCNTVSPGYMATEISDFIPRDTKEKWWQLIPMGREGDPSELAGAYIYLASDASTYTTGADILVDGGYCCP
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (Q583K6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Protein phosphatase methylesterase 1
- TAP42-like protein
- Serine/threonine-protein phosphatase 2A activator
Sequence:
MQEEEGNLEELVYFYPPSTTPPAVGKYTQLISDLLQSVSIVDALPRGAAQAGILCQDTKEVLESENTVLEIAIPRQDNLVIVGDIHGQFADMLSNVLSIQLNLNNTKATDGRGSPSTEIYKFLFLGDYVDRGPQSLEVITLLFALKVEYPEHIFLLRGNHEEAQTSRLYGFFQECKSKLEGTGDRGPASVDITSSTWLQYNTVFCWLPLAAVVACPSGMFFCTHGGLSPHTLSVPLLRSLRRNEYGMVDDFEDTFYTPTSRGGDDMLEGPGAKARLVIDGLLWSDPEDQVSGCQMNNRGCGFIFGPDVTRSFLDRNYSYGFPPSKRQLIGEMKPGMQFILRGHQCAREGYMWCHGGLVLTLFSAPNYCGMHGNKGAVALLRGQVQAGKDRVELEFNVYDTVVRGGSDNLVACLSPFAFAHYFSGDS
Protein: Propionate kinase (EC 2.7.2.15) (P11868)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. It can also use acetyl phosphate as phosphate group acceptor.
Interaction partners:
- Phosphate acetyltransferase
- Threonine/serine transporter TdcC
- PFL-like enzyme TdcE
- L-threonine dehydratase catabolic TdcB
- Propionate--CoA ligase
- Phosphate acetyltransferase EutD
- Putative reactive intermediate deaminase TdcF
- Acetyl-coenzyme A synthetase
- Acetate kinase
- L-serine dehydratase TdcG
Sequence:
MNEFPVVLVINCGSSSIKFSVLDASDCEVLMSGIADGINSENAFLSVNGGEPAPLAHHSYEGALKAIAFELEKRNLNDSVALIGHRIAHGGSIFTESAIITDEVIDNIRRVSPLAPLHNYANLSGIESAQQLFPGVTQVAVFDTSFHQTMAPEAYLYGLPWKYYEELGVRRYGFHGTSHRYVSQRAHSLLNLAEDDSGLVVAHLGNGASICAVRNGQSVDTSMGMTPLEGLMMGTRSGDVDFGAMSWVASQTNQSLGDLERVVNKESGLLGISGLSSDLRVLEKAWHEGHERAQLAIKTFVHRIARHIAGHAASLRRLDGIIFTGGIGENSSLIRRLVMEHLAVLGLEIDTEMNNRSNSCGERIVSSENARVICAVIPTNEEKMIALDAIHLGKVNAPAEFA
Protein: Peroxisomal trans-2-enoyl-CoA reductase (TERP) (EC 1.3.1.38) (Q99MZ7)
Organism: Mus musculus (Mouse)
Function: Participates in chain elongation of fatty acids. Catalyzes the reduction of trans-2-enoyl-CoAs of varying chain lengths from 6:1 to 16:1, having maximum activity with 10:1 CoA. Has no 2,4-dienoyl-CoA reductase activity.
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:Q9JIF5}.
Interaction partners:
- Peroxisomal bifunctional enzyme
- Peroxisomal acyl-coenzyme A oxidase 2
- Peroxisomal targeting signal 1 receptor
Sequence:
MGSWKTGQSYLAAGLLKNQVAVVTGGGTGIGKAVSRELLHLGCNVVIASRKLDRLTAAVDELRASLPPSSSAEVSAIQCNIRKEEEVSNLVKSTLAKYGKINFLVNNGGGQFMAPVEDITAKGWHAVIETNLTGTFYMCKEVYNSWMREHGGSIVNIIVLLNNGFPTAAHTGAAREGVYNLTKSMALAWASSGVRINCVAPGTIYSQTAVDNYGEMGQTLFEMAFDSIPAKRLGVPEEISPLVCFLLSPAASYITGQLINVDGGQALYTHAFSIPDHDNWPVGAGDLSIVKRIKESFKKKAKL
Protein: Protein OPG079 (Protein I3) (P12923)
Organism: Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Function: Plays an essential role in viral DNA replication. Binds to ssDNA with high affinity and localizes to cytoplasmic factories where nascent viral genomes accumulate. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:22438556, ECO:0000269|PubMed:37607234}. Note=Localizes in cytoplasmic virus factories, where it is associated with viral DNA. {ECO:0000269|PubMed:22438556}.
Interaction partners:
Sequence:
MSKVIKKRVETSPRPTASSDSLQTCAGVIEYAKSISKSNAKCIEYVTLNASQYANCSSISIKLTDSLSSQMTSTFIMLEGETKLYKNKSKQDRSDGYFLKIKVTAASPMLYQLLEAVYGNIKHKERIPNSLHSLSVETITEKTFKDESIFINKLNGAMVEYVSTGESSILRSIEGELESLSKRERQLAKAIITPVVFYRSGTETKITFALKKLIIDREVVANVIGLSGDSERVSMTENVEEDLARNLGLVDIDDEYDEDSDKEKPIFNV
Protein: Esculentin-2Rb (P86021)
Organism: Pelophylax ridibundus (Marsh frog) (Rana ridibunda)
Function: Antimicrobial peptide.
Subcellular location: Secreted {ECO:0000269|PubMed:18855342}.
Interaction partners:
Sequence:
GIFSLVKGVAKLAGKTLAKEGGKFGLELAMCKIAKQC
Protein: Cyclin-dependent kinase 10 (EC 2.7.11.22) (F1QKU6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Cyclin-Q
- Cyclin-G2
Sequence:
MESTADTDLEPLKLKSLKTDRTFVIPHSERLGKCRSVKEFEKINRIGEGTYGIVYRARDTRTNEIVALKKVRMDKEKDGIPISSLREINLLIRLRHPNIVELKEVVVGSHLESLFLVMSYCEQDLASLLENMQSPFSEAQVKCIVLQLLKGLAYLHHNFILHRDLKVSNLLMTDKGCVKIADFGLARVYGIPLQPMTPRVVTLWYRAPELLLGTKTQTTALDMWAVGCIFAELLAHKPLLPGASEIQQLDLIVQLLGTPNESIWPGFSRLPLVGQYSLRKQPYNNLKNKFTWLSEAGLRLLNLLFMYNPQRRATAIDCLESSYFKEKPLPCEPELMPTFPHHRNKRSASETEHQTKRSKV
Protein: Oxalate decarboxylase OxdD (EC 4.1.1.2) (O34767)
Organism: Bacillus subtilis (strain 168)
Function: Converts oxalate to formate and CO(2).
Subcellular location: Cytoplasm {ECO:0000305|PubMed:11546787}.
Interaction partners:
- Spore coat protein B
- Quercetin 2,3-dioxygenase
- Oxalate decarboxylase OxdC
- Probable oxidoreductase YjgC
- Formyltetrahydrofolate deformylase
- Putative formate dehydrogenase YrhE
- Spore coat protein Z
- Spore coat protein G
- Spore coat protein C
- Malate dehydrogenase
Sequence:
MLLEQQPINHEDRNVPQPIRSDGAGAIDTGPRNIIRDIQNPNIFVPPVTDEGMIPNLRFSFSDAPMKLDHGGWSREITVRQLPISTAIAGVNMSLTAGGVRELHWHKQAEWAYMLLGRARITAVDQDGRNFIADVGPGDLWYFPAGIPHSIQGLEHCEFLLVFDDGNFSEFSTLTISDWLAHTPKDVLSANFGVPENAFNSLPSEQVYIYQGNVPGSVASEDIQSPYGKVPMTFKHELLNQPPIQMPGGSVRIVDSSNFPISKTIAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVFIGNGTARTFDYRAGDVGYVPSNAGHYIQNTGTETLWFLEMFKSNRYADVSLNQWMALTPKELVQSNLNAGSVMLDSLRKKKVPVVKYPGT
Protein: DNA replication complex GINS protein PSF2 (Partner of Sld five 2) (P40359)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as part of the GINS complex which plays an essential role in the initiation of DNA replication by binding to DNA replication origins and facilitating the assembly of the DNA replication machinery.
Subcellular location: Nucleus {ECO:0000269|PubMed:12730134}.
Interaction partners:
- DNA replication licensing factor MCM3
- Minichromosome maintenance protein 5
- DNA replication complex GINS protein SLD5
- DNA replication complex GINS protein PSF1
- DNA replication complex GINS protein PSF3
- DNA polymerase epsilon subunit B
- DNA replication licensing factor MCM2
- DNA replication licensing factor MCM4
- Cell division control protein 45
- DNA polymerase alpha-binding protein
Sequence:
MSLPAHLQQTFSPEEIQFIVENEPIKIFPRITTRQKIRGDDRGTGNHTRWQLITTDDKALNNMVAMRSTEVVLWIALLLKQQSKCSIVAPQWLTTKELDRKIQYEKTHPDRFSELPWNWLVLARILFNKAKDDFHDPIHELRGKIQDLREIRQIKVLKGLKYLNESHLQLDNLSLLEINELRPFITEIMDKLREIHTASLTAGTENDEEEFNI
Protein: Protein painting of fourth (Zeste-interacting protein 16) (Zip16) (Q9W123)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable RNA-binding protein that specifically binds to the fourth chromosome and may bind an RNA that spreads the fourth chromosome. May be a reminiscence of X chromosome dosage compensation of ancestral Drosophila species in which the X and the fourth chromosomes are one single chromosome.
Subcellular location: Nucleus {ECO:0000269|PubMed:11353870}. Chromosome {ECO:0000269|PubMed:11353870}. Note=Specifically binds to the fourth chromosome.
Interaction partners:
- Ataxin-2 homolog
- PAN2-PAN3 deadenylation complex subunit PAN3
- Eukaryotic translation release factor 3, isoform A
- PAN2-PAN3 deadenylation complex catalytic subunit PAN2
Sequence:
MDSKRAALESGDGPDAKRLDTTDDQDKEASGGDGSQVMLAKHVAPYTGHGCTPPMESYLFEPTPAGSQLLPWKTSVDLDNDAELEKPTSDKKPDTAKLSRRELAKMRREHTLRALALERELTNKPGQTPASEVLLVRFPDPEITAPMLAGLSKDIRDVVLPISVAPRYCLVHLKAGADVEATICDINRVRFGTGHLRAELKPFSDEEQAEFIDPCSLYVGNIPFNMTTSAIKAYFANAMRVDIGVLKREKRARYAFVRYASPDQTMEAFKELVDSPLNSRTLTVRYRRLRKRAGMPMVQCATSFQALQSPNGDDDNTDCKVISPPPLESIIISDSDNCSDSSGNGKEDGKRKKKINEQEREIEKLKRQMAEYGAIIKSLQFRQNSLEDTFIPDLTPKVEPSVNPTGCLLGSNAVHLMRDIKKECDYLGIPDPVPATKPTTQAQDDSQKKAKRSCFGRLFTGPFRRGTSAMKTADEYEKDDRLEELYAQLERDPDP
Protein: Pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1) (Pyruvate synthase) (Q726T1)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-binding domain protein
- Pyruvate ferredoxin oxidoreductase, alpha subunit
- Pyruvate ferredoxin oxidoreductase, beta subunit
- Pyruvate ferredoxin/flavodoxin oxidoreductase, beta subunit, putative
- Pyruvate ferredoxin oxidoreductase, beta subunit, putative
- Pyruvate ferredoxin oxidoreductase, alpha subunit, putative
- L-lactate dehydrogenase
- Succinate--CoA ligase subunit alpha
- Pyruvate ferredoxin/flavodoxin oxidoreductase family protein
- Phosphate acetyltransferase
Sequence:
MAKKMKTMDGNTATAYVAYALSDTAAIYPITPSSNMGEAADEWAAQGKKNIFGQTVAVRQLQSEAGAAGAVHGCLAAGALTSTYTASQGLLLMIPNMYKISGELLPGVFHVSARAIAAHALSIFGDHQDVMAARQTGFAMLASTSVQECMDLALVSHLSAIESSVPFCHFFDGFRTSHELQKIEVIDYDDMKKLVNWEKVENFRQNAMNPEHPHIRGTAQNPDIYYQAREAANPFYAAVPGIVASYMKKVGEITGRKYKPFDYVGHPEADRVIIAMGSGCETIEEVVNYLNAAGQRVGLVKVRLYRPFSVEHLMAVLPASADTITVLDRTKEPGALGEPLYLDVCTAFMERGEMPKLIAGRYGLGSKEFTPAMVKAVYDNMKVNGPKNHFNVGIIDDVTDTSLEVEADLDTVPTGTVQCKFFGLGADGTVGANKQAIKIIGDNTDMYAQGYFAYDSKKSGGFTVSHLRFGKSPIQSTYLVNRADYVACHKSAYVNQYDVLEGIKEGGTFVLNSHWTSVEDMERELPASMRRTIARKQLKFYNVDAVKVATEVGLGGRINMIMQTAFFKLASVIPFEQAVELLKDSIKKAYGKKGDKIVNMNIAAVDKAIDALQEVKYPASWADAVDVPVACAEEPGFITDVVRPILAQQGDKLPVSSFEPDGLFPVGTAAFEKRGVAINVPEWLSENCIQCNQCSFVCPHAAIRPVLATTEELEGAPASFVTIDAKGKELNGLKYRIQVFAQDCLGCGSCAEVCPAKNKALVMKPIETQLDAQVPNLAFAEENIAIKDDLMGRDSLKGSQFQQPLMEFSGACAGCGETPYVKLLTQMFGERMIVANATGCSSIWGASAPTTPYCTNKDGHGPAWGNSLFEDAAEFGYGMGMAFNQRRAKLADLVKEALELDIPAELRAAFEGWLAGKDDAEASRKYGDEILALLGTADDHPVLHEMWHMSDLFTKKSVWIFGGDGWAYDIGYGGVDHVLASGEDINILVMDTEVYSNTGGQSSKATPLGSIAKFAASGKKTGKKDLGRMAMTYGYVYVASISMGANKQQVLKAFKEAEAYKGPSLIIAYAPCINQGIRKGMGKSMEEGKLAVESGYWPLYRFNPELADQGKNPFVLESKAPDGTMQDFLAGENRYALLEKIAPEESKRLRAQIEKEYVERYSMLKQMAEAPAVTAAPGAPVAAAGEAGENCTVSETPEHARTNGGSACDDGRSGK
Protein: Immunoglobulin heavy variable 3-9 (Ig heavy chain V-III region DOB) (P01782)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MELGLSWIFLLAILKGVQCEVQLVESGGGLVQPGRSLRLSCAASGFTFDDYAMHWVRQAPGKGLEWVSGISWNSGSIGYADSVKGRFTISRDNAKNSLYLQMNSLRAEDTALYYCAKD
Protein: Olfactory receptor (A1L3S1)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
Sequence:
MDRSNETAPLSGFILLGLSAHPKLEKTFFVLILLMYLVILLGNGVLILVSILDSHLHTPMYFFLGNLSFLDICYTTSSVPLILDSFLTPRKTISFSGCAVQMFLSFAMGATECVLLSMMAFDRYVAICNPLRYPVVMNKAAYVPMAASSWAGGITNSVVQTSLAMRLPFCGDNVINHFTCEILAVLKLACADISINVISMVVANMIFLAVPVLFIFVSYVFILVTILRIPSAEGRKKAFSTCSAHLTVVLVFYGTILFMYGKPKSKDPLGADKQDLADKLISLFYGVVTPMLNPIIYSLRNKDVRAAVRNLVGQKHLTE
Protein: Uncharacterized oxidoreductase Rv0769 (EC 1.-.-.-) (P9WGQ9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable fatty acid synthase Fas
- Malonyl CoA-acyl carrier protein transacylase
- 3-hydroxyacyl-thioester dehydratase Y
- 
- Uncharacterized oxidoreductase Rv1350
- Enoyl-CoA hydratase ChsH3
- 3-oxoacyl-[acyl-carrier-protein] reductase
- Possible malonyl CoA-acyl carrier protein transacylase FabD2
- Probable aldehyde dehydrogenase NAD dependent AldA
- Possible 4-carboxymuconolactone decarboxylase
Sequence:
MFDSKVAIVTGAAQGIGQAYAQALAREGASVVVADINADGAAAVAKQIVADGGTAIHVPVDVSDEDSAKAMVDRAVGAFGGIDYLVNNAAIYGGMKLDLLLTVPLDYYKKFMSVNHDGVLVCTRAVYKHMAKRGGGAIVNQSSTAAWLYSNFYGLAKVGVNGLTQQLARELGGMKIRINAIAPGPIDTEATRTVTPAELVKNMVQTIPLSRMGTPEDLVGMCLFLLSDSASWITGQIFNVDGGQIIRS
Protein: Large ribosomal subunit protein uL13B (60S ribosomal protein L16-B) (O42991)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL6
- Elongation factor 3
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein uL24
- mRNA export factor elf1
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL20B
- Large ribosomal subunit protein eL20A
Sequence:
MSEFQKVVVIDAKGHLLGRLASVVAKQLLGGQKVVVVRCEELNISGHFFRNKLKYLAYLRKACRYNPSRGAFHFRAPSRIFQKAVRGMLPHKTARGQAALEHLQAVEGIPPPFDKQKRVVVPAALRVLRLKPGRKYCTVGRLSSEVGWKYNDIVAKLEERRKVKSAAFYQAKLAKQKKIASAKEASPVNQKLSQFGY
Protein: Penicillin-binding protein 1F (PBP-1F) (Penicillin-binding protein F) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.99.28) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)] (P38050)
Organism: Bacillus subtilis (strain 168)
Function: Cell wall formation. May be involved in outgrowth of the germinated spore or it could function in the synthesis of the germ cell wall.
Subcellular location: Cell membrane; Single-pass membrane protein.
Interaction partners:
- D-alanyl-D-alanine carboxypeptidase DacA
- Penicillin-binding protein 1A/1B
- D-alanyl-D-alanine carboxypeptidase DacF
- Putative carboxypeptidase YodJ
- D-alanyl-D-alanine carboxypeptidase DacB
- Penicillin-binding protein 2A
- Peptidoglycan glycosyltransferase RodA
- Stage V sporulation protein D
- Sporulation-specific N-acetylmuramoyl-L-alanine amidase
- Penicillin-binding protein 2B
Sequence:
MFKIKKKKLFIPIIILVLTAFLALIGYISIIFLGHYVIDEKKLILHASSKIVDQNGDEVASLYTENREPVSINEIPKQVREAFIAVEDKRFYEHHGIDAKSVGRAVYRDILAGGKVEGGSTITQQLAKNIFLTHDKTFLRKTKEVIIAINLERDYSKDKLLEMYLNQLYFGHGVYGIQAASHYYFNKEVKDLTVSEGAVLAAIPKAPSTYSPILHPDKNKERRDTILGMMNDQGYISAKEAVTAQGRTLGLHVKKQSETPWFDSYIDLVIKEAEDKYSISGEQLLQGGYTIKVPLDSKLQKTAYQVMKEGSYYPGTDQNAEGSAVFINNKTGGVEAAIGGRDYTSKGYNRVTAVRQPGSTFKPLAVYGPAMQEKKFKPYSLLKDELQSYGDYTPKNYDSRYEGEVTMSDAITYSKNAPAVWTLNEIGVETGKSYLKANGIDIPDEGLALALGGLEKGVSPLQLAGAFHTFAANGTYTEPFFISSIIDEDGETIADHKEEGKRVFSKQTSWNMTRMLQQVVKKGTATSGTYHGDLAGKTGSTSYTGVSGATKDAWFAGYTPKITGAVWMGYDKTDQNHYLKAGSSYPTRLFKDILTQAGETGHVFTKPKNVKELESPIELKPVKTLTADYTFKAAGLFTIELKWDAQEDDRAVYRIYVNKDGEETLLDSVEGKGSYEIPYANLFSGASYKIVPYNTQTKREGEGTDYVQPKLFSS
Protein: Thioredoxin-2 (DmTrx-2) (Q9V429)
Organism: Drosophila melanogaster (Fruit fly)
Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. As a reducing substrate of peroxiredoxin 1, thioredoxin 2 is preferred over thioredoxin 1.
Interaction partners:
- Apoptotic signal-regulating kinase 1, isoform C
- Thioredoxin reductase 2, mitochondrial
- Thioredoxin reductase 1, mitochondrial
- Thioredoxin-dependent peroxide reductase, mitochondrial
- Peroxiredoxin-5
- Peroxiredoxin 2
- Methionine-R-sulfoxide reductase B1
- thioredoxin-dependent peroxiredoxin
- Ribonucleoside-diphosphate reductase large subunit
- U6 snRNA-associated Sm-like protein LSm7
Sequence:
MVYQVKDKADLDGQLTKASGKLVVLDFFATWCGPCKMISPKLVELSTQFADNVVVLKVDVDECEDIAMEYNISSMPTFVFLKNGVKVEEFAGANAKRLEDVIKANI
Protein: Uncharacterized protein (Q9VIP6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTLSRKDFQALLIVICFGFWIENLVQGADDYYVYSPVCQMPAVNPFTWDTMSNFHRKTLRHCHNDSDMVTSEFDFETHQYRLHVHEHLAKPIMNRKGNATLECEYQEISRDNSDQKPDNAYNQLRRRPIEQHQFVPNNTDYMITSCYVRDVTKHRELLQQDAISFIEDRLPKEKVKDFVKDESEVHKPSVLIMGLDSTSRINLRRAMPSVYKFVRQPGWFEMQGYNKVGDNTFPNLLAALTGDSEKGVGDYCDVTKPGCLDSLNFIWKRFKKANYTTAFAEDCSSISTFNYLKPGFVKQPTDYYLRPLLFAIEKQFKVTNDFGFAYCVGRHLSFSYVWDFGQQFIDRFLGRSPMFGFLWSNSFTHDYYEGATALDNLLWKYLKSFEESNLFQKSIVILMSDHGHRYNTLRRASTGYFEERMPMMFIYLPPWFRRKYPHLASNLGKNQNRLSSNYDVYMTLQHLLQLDSKSVDEFPDNLRARQCKSCQSLFFELPFNRTCQMAGIEEKWCCCQPTETITNSPHVSTIAEAIVQRMNEHLISHNLSDLCHNFTLDYVEKADRKTILSNGLRPADKNEQVYIIVFETVPKNPIFEATVRWNSRTQRLLHFDVEELSRLTSYKNDANCINRKNAKKYCICKDSLSRPS
Protein: Uncharacterized protein (Q381G4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cytochrome c oxidase assembly protein
- Ubiquinol-cytochrome c reductase complex 14 kDa protein
- Mitochondrial membrane-anchored protein domain-containing protein
Sequence:
MRRNPSLFRSKVEFISPKPEGPIASKEFKCISPALLYRQLLKLYIRKFDTDHKTIVAAWKQTKFEFWCHRNDSPEEAELQNIRGQQIYEGIRAGLIPVYSKGKSNEMFFKYDTDTLRASHNHIDPVSLEEFIRRYHDRIRPEDVEEVKATLKKLGRWNGPNELSDSDLHRVKHKVKRKTKCTDNDGA
Protein: 3-isopropylmalate dehydratase small subunit (EC 4.2.1.33) (Alpha-IPM isomerase) (IPMI) (Isopropylmalate isomerase) (P9WK95)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Interaction partners:
- 3-isopropylmalate dehydratase large subunit
- 3-isopropylmalate dehydrogenase
- 2-isopropylmalate synthase
- Ketol-acid reductoisomerase
- Probable transcriptional regulatory protein
- Dihydroxy-acid dehydratase
- Putative acetolactate synthase small subunit
- 3-methyl-2-oxobutanoate dehydrogenase subunit beta
- Putative malate oxidoreductase
- Pyruvate kinase
Sequence:
MEAFHTHSGIGVPLRRSNVDTDQIIPAVFLKRVTRTGFEDGLFAGWRSDPAFVLNLSPFDRGSVLVAGPDFGTGSSREHAVWALMDYGFRVVISSRFGDIFRGNAGKAGLLAAEVAQDDVELLWKLIEQSPGLEITANLQDRIITAATVVLPFKIDDHSAWRLLEGLDDIALTLRKLDEIEAFEGACAYWKPRTLPAP
Protein: Probable cyclic di-GMP phosphodiesterase PdeB (EC 3.1.4.52) (P77473)
Organism: Escherichia coli (strain K12)
Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Diguanylate cyclase DgcP
- Diguanylate cyclase DgcM
- Probable diguanylate cyclase DgcC
- Diguanylate cyclase DgcN
- Probable diguanylate cyclase DgcT
- Diguanylate cyclase DosC
- Probable diguanylate cyclase DgcJ
- Probable diguanylate cyclase DgcF
- Probable diguanylate cyclase DgcI
- Probable diguanylate cyclase CdgI
Sequence:
MRTRHLVGLISGVLILSVLLPVGLSIWLAHQQVETSFIEELDTYSSRVAIRANKVATQGKDALQELERWQGAACSEAHLMEMRRVSYSYRYIQEVAYIDNNVPQCSSLEHESPPDTFPEPGKISKDGYRVWLTSHNDLGIIRYMVAMGTAHYVVMIDPASFIDVIPYSSWQIDAAIIGNAHNVVITSSDEIAQGIITRLQKTPGEHIENNGIIYDILPLPEMNISIITWASTKMLQKGWHRQVFIWLPLGLVIGLLAAMFVLRILRRIQSPHHRLQDAIENRDICVHYQPIVSLANGKIVGAEALARWPQTDGSWLSPDSFIPLAQQTGLSEPLTLLIIRSVFEDMGDWLRQHPQQHISINLESPVLTSEKIPQLLRDMINHYQVNPRQIALELTEREFADPKTSAPIISRYREAGHEIYLDDFGTGYSSLSYLQDLDVDILKIDKSFVDALEYKNVTPHIIEMAKTLKLKMVAEGIETSKQEEWLRQHGVHYGQGWLYSKALPKEDFLRWAEQHL
Protein: Inner nuclear membrane protein Man1 (LEM domain-containing protein 3) (Q9Y2U8)
Organism: Homo sapiens (Human)
Function: Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:15647271}; Multi-pass membrane protein {ECO:0000269|PubMed:15647271}.
Interaction partners:
- Barrier-to-autointegration factor
- Emerin
- Mothers against decapentaplegic homolog 1
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 3
- Barrier-to-autointegration factor-like protein
- GPI ethanolamine phosphate transferase 1
- Delta
- Prelamin-A/C
- Lamin-B1
Sequence:
MAAAAASAPQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEEQQQHRSGGRGNKTRNSNNNNTAAATVAAAGPAAAAAAGMGVRPVSGDLSYLRTPGGLCRISASGPESLLGGPGGASAAPAAGSKVLLGFSSDESDVEASPRDQAGGGGRKDRASLQYRGLKAPPAPLAASEVTNSNSAERRKPHSWWGARRPAGPELQTPPGKDGAVEDEEGEGEDGEERDPETEEPLWASRTVNGSRLVPYSCRENYSDSEEEDDDDVASSRQVLKDDSLSRHRPRRTHSKPLPPLTAKSAGGRLETSVQGGGGLAMNDRAAAAGSLDRSRNLEEAAAAEQGGGCDQVDSSPVPRYRVNAKKLTPLLPPPLTDMDSTLDSSTGSLLKTNNHIGGGAFSVDSPRIYSNSLPPSAAVAASSSLRINHANHTGSNHTYLKNTYNKPKLSEPEEELLQQFKREEVSPTGSFSAHYLSMFLLTAACLFFLILGLTYLGMRGTGVSEDGELSIENPFGETFGKIQESEKTLMMNTLYKLHDRLAQLAGDHECGSSSQRTLSVQEAAAYLKDLGPEYEGIFNTSLQWILENGKDVGIRCVGFGPEEELTNITDVQFLQSTRPLMSFWCRFRRAFVTVTHRLLLLCLGVVMVCVVLRYMKYRWTKEEEETRQMYDMVVKIIDVLRSHNEACQENKDLQPYMPIPHVRDSLIQPHDRKKMKKVWDRAVDFLAANESRVRTETRRIGGADFLVWRWIQPSASCDKILVIPSKVWQGQAFHLDRRNSPPNSLTPCLKIRNMFDPVMEIGDQWHLAIQEAILEKCSDNDGIVHIAVDKNSREGCVYVKCLSPEYAGKAFKALHGSWFDGKLVTVKYLRLDRYHHRFPQALTSNTPLKPSNKHMNSMSHLRLRTGLTNSQGSS
Protein: SET binding factor 1 (A0A8I6AD51)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MARLADYFVLVAFGPHPRGSGEGQGQILQRFPEKDWEDNPFPQGIELFCQPSGWQLCPERNPPTFFVAVLTDINSERHYCACLTFWEPVESTQEVMCTEDATEKEEEAHGGGQAQLSSTAPAQPGQLFAPKTLVLVSRLDHADVFRNSLGLIYTIHVEGLNVNLENVIGNLLTCTVPLAGGSQLDSVEEGARTISLGAGDRQVIQTPLVDSLPVSRCSVALLFRQLGITNVLSLFCAALTEHKVLFLSRSYQRLADACRGLLALLFPLRYSFTYVPILPAQLLEVLSTPTPFIIGVNAAFQAETQELLDVIVADLDGGTVTVPECVHIPPLPEPLQSQTHNVLSMVLDPELELADLAFPPPTTSASSLKMQDKELRAVFLRLFAQLLQGYRWCLHIVRIHPEPVIRFHKAAFLGQRGLVEDDFLMKVLEGMAFAGFVSERGVPYRSTDLFDELVAHEVARMRADENHPHRVLRHVQELAEQLYKNENPYPAVAMHKVQRPGEASHLRRTHRPFPRLDEGTVQWIVDQAAAKMQGAPPAVKAERRTTVPSGPPMTAILERCSGPHINSARRLEVVRNCISYVFEGKMLEAKKLLPAVLRALKGRAARRCLAHELHLHVQQNRAVLDHQQFDFVVRMMNCCLQDCTSLDEHGIAAALLPLVTAFCRKLSPGVTQFAYSCVQEHVVWSTPQFWEAMFYGDVQTHIRALYLEPSDGVSPTQETGEAQSQDDERSALDVASEQRRLWPTLSREKQQELVQKEESTVFSQAIHYANRMSYLLLPLDSSKSRLLRERAGLGDLESASNSLVTNSMAGSVAESYDTESGFEDAETCDVAGAVVRFINRFVDKVCTESGVTSDHLKGLHVMVPDIVQMHIETLEAVHRESKRLPPIQKPKLLRPRLLPGEECVLDGLRVYLLPDGREEGVGGSGGGPALLPAEGAVFLTTYRVIFTGMPTDPLVGEQVVVRSFPVAALTKEKRISVQTPVDQLLQDGLQLRSCTFQLLKMAFDEEVGSDSAELFRKQLHKLRYPPDIRATFAFTLGSALTPGRPPRVTKDKGPSFRTLSRNLVKNAKKTIGRQYVTRKKYNPPGWEHRGQPPPEDQEDEISVSEELEPSTLTPSSALKPSDRMTMSSLVERACCRDYQRLGLGTLSSSLSRAKSEPFRISPVNRMYAICRSYPGLLIVPQSIQDNALQRVSRCYRQNRFPVVCWRSGRSKAVLLRSGGLHGKGVVGLFKAQNTPSPGQAQADSSSLEQEKYLQAVVSSMPRYADSSGRNTLSSFSSAHMGGHGKWSSVRASGRSSGLGADVGSRLAGRDLLSTPHTNGAPPDSGFLRPQRAALYIIGDKAQLKGVRPDPLQQWELVPIEVFEARQVKASFKKLLKACVPGCPATEPSPASFLRSLEDSEWLIQIHKLLQISVLVVELLDSGSSVLVSLEDGWDITTQVVSLVQLLSDPFYRTLEGFRLLVEKEWLSFGHRFSHRGAHTLAGQSSGFTPVFLQFLDCVHQVHLQFPMEFEFSQFYLKFLGYHHTSRRFRTFLLDSDYERIELGLLYEEKGERRGQLACKSVWEYVDRLSKRTPMFYNYTYAPEDTEVLRPYSNVSNLKVWDFYTEETLAEGPPYDWELAQGPPEPPEEERPDGGAPQSRRRVVWPCYDSRPRVQPDAISRLLEELQRLETELGRPSERWKETWDRVKAAQRLEGRQDGRGTPSSLLVSAVPHHRRSLGVYLQEGPVGSTLSLSLDSDQSSGSTTSSSRQAARRSTSTLYSQFQTAESENRSYEGTLYKKGAFMKPWKARWFVLDKTKHQLRYYDHRVDTECKGVIDLAEVEAVAPGTPTIGAPKTVDEKAFFDVKTTRRVYNFCAQDVPSAQQWVDRIQSCLSDA