wanglab/gogpt-training-data huggingface dataset:
Protein: PHD finger protein 1 (Protein PHF1) (Polycomb-like protein 1) (mPCl1) (T-complex testis-expressed 3) (Q9Z1B8)
Organism: Mus musculus (Mouse)
Function: Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Involved in DNA damage response and is recruited at double-strand breaks (DSBs). Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex: it is however unclear whether recruitment of the PRC2 complex to H3K36me3 leads to enhance or inhibit H3K27me3 methylation mediated by the PRC2 complex. According to some reports, PRC2 recruitment by PHF1 promotes H3K27me3 and subsequent gene silencing by inducing spreading of PRC2 and H3K27me3 into H3K36me3 loci. According to other reports, PHF1 recruits the PRC2 complex at double-strand breaks (DSBs) and inhibits the activity of PRC2. Regulates p53/TP53 stability and prolonges its turnover: may act by specifically binding to a methylated from of p53/TP53.
Subcellular location: Nucleus {ECO:0000269|PubMed:18086877}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes specifically to the promoters of numerous target genes. Localizes to double-strand breaks (DSBs) sites following DNA damage. Colocalizes with NEK6 in the centrosome (By similarity). {ECO:0000250}.
Interaction partners:
- Protein Jumonji
- Histone-lysine N-methyltransferase EZH2
- Zinc finger protein AEBP2
- Polycomb protein Suz12
- Histone-lysine N-methyltransferase EZH1
- Histone-binding protein RBBP7
- Polycomb protein EED
- Elongin BC and Polycomb repressive complex 2-associated protein
- Histone-binding protein RBBP4
- PHD finger protein 19
Sequence:
MAQLPRLSRLGAPSLWDPASPAPTSGPRPRLWEGQDVLARWTDGLLYLGTIKKVDSAREVCLVQFEDDSQFLVLWKDISPAALPGEELLCCVCRSETVVPGNRLVSCEKCRHAYHQDCHVPRAPAPGEGEGASWVCRQCVFAIATKRGGALKKGPYARAMLGMKLSLPYGLKGLDWDAGHLSNRQQSYCYCGGPGEWNLKMLQCRSCLQWFHEACTQCLSKPLLYGDRFYEFECCVCRGGPEKVRRLQLRWVDVAHLVLYHLSVCCKKKYFDFDREILPFTSENWDSLLLGELSDTPKGERSSQLLSALNSHKDRFISGREIKKRKCLFGLHARTPPPVELLTGDGAPTSFPSGQGPGGGVSRPLGKRWRSEPEPLRRRQKGKVEELGPPTAAHSRHGSREQRALQASVSPPPPSPNQSYEGSSGYNFRPTDARCLPSSPIRMFASFHPSASTAGTSGDSEPPDRSPLGLHIGFPTDTPKSSPHSVTASSSSVPALTPGFSRHSPPSPLCRSLSPGTGGGVRGGVSYLSRGDPVRVLARRVRPDGSVQYLVEWGGGGIF
Protein: ATP-dependent RNA helicase DDX25 (EC 3.6.4.13) (DEAD box protein 25) (Gonadotropin-regulated testicular RNA helicase) (Q9QY15)
Organism: Mus musculus (Mouse)
Function: ATP-dependent RNA helicase. Required for mRNA export and translation regulation during spermatid development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15096601, ECO:0000269|PubMed:16968703}. Nucleus {ECO:0000269|PubMed:15096601, ECO:0000269|PubMed:16968703}. Note=Detected in both cytoplasm and nucleus of testicular cells. Also detected in chromatoid bodies of round spermatids. {ECO:0000269|PubMed:15096601, ECO:0000269|PubMed:16968703, ECO:0000269|PubMed:32665638}.
Interaction partners:
- Nuclear pore complex protein Nup214
- mRNA export factor GLE1
- Tudor domain-containing protein 6
Sequence:
MASLLWGGDAGAAESERLNSHFSNLVHPRKNLRGIRSTTVPNIDGSLNTEDDDDDEDDVVDLAANSLLNKLIRQSLIESSHRVEVLQKDPSSPLYSVKTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVERMGKFCVDVEVMYAIRGNRIPRGTEVTKQIIIGTPGTVLDWCFKRKLIDLTKIRVFVLDEADVMIDTQGFSDQSIRIQRALPSECQMLLFSATFEDSVWQFAERIIPDPNVIKLRKEELTLNNIRQYYVLCENRKGKYQALCNIYGGITIGQAIIFCQTRRNAKWLTVEMMQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVNQSEEPDYETYLHRIGRTGRFGKKGLAFNMIEVDKLPLLMKIQDHFNSNIKQLDPEDMDEIEKIEY
Protein: Probable dehydrogenase (Q9HWU9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable nonribosomal peptide synthetase
Sequence:
MHNVLIVGASRGIGLGLADAFLQRGAQVFAVARRPQGSPGLQALAERAGERLQAVTGDLNQHDCAERIGEMLGERRIDRLIVNAGIYGPQQQDVAEIDAEQTAQLFLTNAIAPLRLARALSGRVSRGGVVAFMSSQMASLALGLSATMPLYGASKAALNSLVRSWEGEFEELPFSLLLLHPGWVRTEMGGDSAPLSVEESAAGLVAAVEDAAGVNACRFVDYRNQPLPW
Protein: HAT1-interacting factor 1 (Q12373)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Histone H3 and H4 specific chaperone component of the nuclear histone acetyltransferase B (HAT-B) complex. Involved in chromatin assembly and telomere silencing.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14761951, ECO:0000269|PubMed:15099519}.
Interaction partners:
- Histone acetyltransferase type B catalytic subunit
- Histone acetyltransferase type B subunit 2
- Histone H4
- Histone chaperone ASF1
- Histone H3
- Histone H2A.1
- Histone H2B.1
- Histone H3-like centromeric protein CSE4
- DNA mismatch repair protein HSM3
- FACT complex subunit SPT16
Sequence:
MKLRAEDVLANGTSRHKVQIDMERQVQIAKDLLAQKKFLEAAKRCQQTLDSLPKDGLLPDPELFTIFAQAVYNMEVQNSGNLFGDALLAGDDGSGSESESEPESDVSNGEEGNENGQTEIPNSRMFQFDQEEEDLTGDVDSGDSEDSGEGSEEEEENVEKEEERLALHELANFSPANEHDDEIEDVSQLRKSGFHIYFENDLYENALDLLAQALMLLGRPTADGQSLTENSRLRIGDVYILMGDIEREAEMFSRAIHHYLKALGYYKTLKPAEQVTEKVIQAEFLVCDALRWVDQVPAKDKLKRFKHAKALLEKHMTTRPKDSELQQARLAQIQDDIDEVQENQQHGSKRPLSQPTTSIGFPALEKPLGDFNDLSQLVKKKPRRH
Protein: Tumor necrosis factor receptor superfamily member 13B (Transmembrane activator and CAML interactor) (CD antigen CD267) (O14836)
Organism: Homo sapiens (Human)
Function: Receptor for TNFSF13/APRIL and TNFSF13B/TALL1/BAFF/BLYS that binds both ligands with similar high affinity. Mediates calcineurin-dependent activation of NF-AT, as well as activation of NF-kappa-B and AP-1. Involved in the stimulation of B- and T-cell function and the regulation of humoral immunity.
Subcellular location: Membrane; Single-pass type III membrane protein.
Interaction partners:
- Tumor necrosis factor ligand superfamily member 13
- Tumor necrosis factor ligand superfamily member 13B
- Guided entry of tail-anchored proteins factor CAMLG
- Tumor necrosis factor receptor superfamily member 13C
- Tumor necrosis factor receptor superfamily member 17
- CD40 ligand
- TNF receptor-associated factor 6
- Tumor necrosis factor receptor superfamily member 5
- Inducible T-cell costimulator
- Myeloid differentiation primary response protein MyD88
Sequence:
MSGLGRSRRGGRSRVDQEERFPQGLWTGVAMRSCPEEQYWDPLLGTCMSCKTICNHQSQRTCAAFCRSLSCRKEQGKFYDHLLRDCISCASICGQHPKQCAYFCENKLRSPVNLPPELRRQRSGEVENNSDNSGRYQGLEHRGSEASPALPGLKLSADQVALVYSTLGLCLCAVLCCFLVAVACFLKKRGDPCSCQPRSRPRQSPAKSSQDHAMEAGSPVSTSPEPVETCSFCFPECRAPTQESAVTPGTPDPTCAGRWGCHTRTTVLQPCPHIPDSGLGIVCVPAQEGGPGA
Protein: Glycerol-3-phosphate dehydrogenase [NAD(+)] 2 (EC 1.1.1.8) (Q59W33)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: May catalyze the production and accumulation of glycerol during hyperosmotic stress conditions (By similarity). Glycerol acts as a osmoregulator that prevents loss of water and turgor of the cells (By similarity). Mediates evasion of the host innate immune system by binding inhibitory components of the host alternative complement system, in a manner dependent on estrogen-induced inhibition of EBP1.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:23204165}. Secreted {ECO:0000269|PubMed:23204165}. Cytoplasm {ECO:0000250|UniProtKB:Q00055}. Peroxisome {ECO:0000250|UniProtKB:Q00055}. Note=Localizes to the cell wall in both yeast and hyphae. {ECO:0000269|PubMed:23204165}.
Interaction partners:
- Glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase [NAD
- Bifunctional glycerol-3-phosphate/glycerone-phosphate O-acyltransferase
- Bifunctional glycerol-3-phosphate/glycerone-phosphate O-acyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Glycerol-1-phosphatase
- Dihydroxyacetone kinase
- Lysophosphatidic acid acyltransferase
- Phosphatidate phosphatase
- Dpp1p
Sequence:
MTTSPYPIETPFKVCIVGSGNWGTAVAKLVAENCAEKPNIFQRDVKMWVFEEEIEGRKLTEIINTEHENVKYLPEIKLPTNLVANPDIVDTVQDADLIVFNIPHQFLGRIVKQIEGKVKPTARAISCLKGLDVSPEGCKLLSTSITDTLKIYCGVLSGANIANEVAKGNWSETSIAYTVPEDFRGAGKDIDPFILKEAFHRPYFHVRVIEDVVGASIAGALKNVIACSVGFVEGAGWGDNAKAAIMRIGIKETIRFASYWELFKIKALSPPNPKTFTEESAGVADLITTCSGGRNVKVARYMIKNNVDAFEAEKIVLKGQSSQGILTAKEVHELLTNFNLQDEFPLLEATYKVIYENGSVDDFPQLLEGDQ
Protein: Translin-associated factor X-interacting protein 1 N-terminal domain-containing protein (Q387F7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Probable eukaryotic initiation factor 4A
- Histone chaperone RTT106/FACT complex subunit SPT16-like middle domain-containing protein
- FACT complex subunit
- Histone H3, putative
- Histone H3 variant
- Uncharacterized protein
Sequence:
MPHKEAEVGTLGFKTPARRSRCIGDQGFHSATKPWVSPHSLVKVSPRLRVPSTSRLPALAEAPVFPRALVPSKALGPVAISKAPLAAQLEAFVRREYKIYSTGNRDCTHVDTLHIVREAFSVFLEHFSEYREVLSLIRDEYEAAFQELLSEVKRLRAVELETSSDRSVHAMEMLKQREAFKSIVSNHYAQLQATEGIVHSLRDQITSYEESNETLRAQLKKAKEETREATDTSKLLTKSMIEEAARNSQLLAARTANEREIGRLKVQVDMVREELKDVESRYTALLEKTLCTGGPDTIFKGKDVRAKKKLDQECEQEAKKKLEESEENARQKASEEEERRNRDNAYFALINERIDELLLEREQLKQQLADALASRCASACGSGGGGRPASTSRARRFSADPGALENDRRLVEGDATYSRLIAAWLREEQMTGAELDRLDVLIPPGASEDHPFGFLKATLPVRNRYLKREDTIDMLNSWWGFRRNSFDSSIKHHFMCWLQKTTGSESGAQELGVNIVHVCEHNIYDPDCRAFLLIFRECVPEDVVHAWTKDIAYFEELCRESMSAHRFVRCSVLYDKLRNKLQEKTYLNMLELRLYLWRNSDANGMISVDFLFRKDSRFLYLLKKQLLREVEEFTLRVVEAIRSVALDADTVKLQDVVNALSAQDPGIPQGTLRRLVAEATQLTSMDVATCGVDFTVRLRPLIYRFRSAVLLRRVTPPVDTSQLNPNIFDAKAIVEEAEEV
Protein: Excisionase (P68927)
Organism: Escherichia phage HK022 (Bacteriophage HK022)
Function: Excisionase and integrase are necessary for the excision of prophage from the host genome by site-specific recombination at the att site.
Interaction partners:
Sequence:
MYLTLQEWNARQRRPRSLETVRRWVRECRIFPPPVKDGREYLFHESAVKVDLNRPVTGSLLKRIRNGKKAKS
Protein: ATP-dependent RNA helicase DeaD (EC 3.6.4.13) (Cold-shock DEAD box protein A) (Translation factor W2) (P0A9P6)
Organism: Escherichia coli (strain K12)
Function: DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity at low temperature. Involved in 50S ribosomal subunit assembly, acting after SrmB, and could also play a role in the biogenesis of the 30S ribosomal subunit. In addition, is involved in mRNA decay, via formation of a cold-shock degradosome with RNase E. Also stimulates translation of some mRNAs, probably at the level of initiation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00964, ECO:0000269|PubMed:8552679}.
Interaction partners:
- ATP-dependent DNA helicase RecQ
- Ribonuclease E
- Uncharacterized protein YrbN
- Polyribonucleotide nucleotidyltransferase
- Large ribosomal subunit protein uL3
- Lipoprotein NlpI
Sequence:
MAEFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKRRLEKFAAKVQQQLESSDLDQYRALLSKIQPTAEGEELDLETLAAALLKMAQGERTLIVPPDAPMRPKREFRDRDDRGPRDRNDRGPRGDREDRPRRERRDVGDMQLYRIEVGRDDGVEVRHIVGAIANEGDISSRYIGNIKLFASHSTIELPKGMPGEVLQHFTRTRILNKPMNMQLLGDAQPHTGGERRGGGRGFGGERREGGRNFSGERREGGRGDGRRFSGERREGRAPRRDDSTGRRRFGGDA
Protein: NADH-ubiquinone oxidoreductase chain 4L (EC 7.1.1.2) (NADH dehydrogenase subunit 4L) (P03903)
Organism: Mus musculus (Mouse)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 5
- NADH-ubiquinone oxidoreductase chain 2
- Acyl carrier protein, mitochondrial
- NADH-ubiquinone oxidoreductase chain 6
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 4
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH-ubiquinone oxidoreductase chain 1
Sequence:
MPSTFFNLTMAFSLSLLGTLMFRSHLMSTLLCLEGMVLSLFIMTSVTSLNSNSMSSMPIPITILVFAACEAAVGLALLVKVSNTYGTDYVQNLNLLQC
Protein: GTP:AMP phosphotransferase, mitochondrial (EC 2.7.4.10) (Adenylate kinase 3) (AK 3) (P26364)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities. Does not accept ATP as phosphate donor.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03169, ECO:0000269|PubMed:1620094}.
Interaction partners:
- Adenylosuccinate lyase
- Nucleoside diphosphate kinase
- Adenine phosphoribosyltransferase 2
- Adenine phosphoribosyltransferase 1
- Ribonucleoside-diphosphate reductase large chain 2
- Ribonucleoside-diphosphate reductase large chain 1
- Adenosine kinase
- Ribonucleoside-diphosphate reductase small chain 1
- Ribonucleoside-diphosphate reductase small chain 2
- Adenylate kinase isoenzyme 6 homolog FAP7
Sequence:
MKADAKQITHLLKPLRLLLLGAPGSGKGTQTSRLLKQIPQLSSISSGDILRQEIKSESTLGREATTYIAQGKLLPDDLITRLITFRLSALGWLKPSAMWLLDGFPRTTAQASALDELLKQHDASLNLVVELDVPESTILERIENRYVHVPSGRVYNLQYNPPKVPGLDDITGEPLTKRLDDTAEVFKKRLEEYKKTNEPLKDYYKKSGIFGTVSGETSDIIFRNY
Protein: Small proline-rich protein 2D (O70555)
Organism: Mus musculus (Mouse)
Function: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Small proline-rich protein 2I
- Small proline-rich protein 2E
- Small proline-rich protein 2H
- Small proline-rich protein 2F
- Repetin
Sequence:
MSYQQQQCKQPCQPPPVCPPKKCPEPCPPLKCPEPCPPPKCPEPCPPPKCPEPCPEPCPPPSCQQKCPPAQPPPPCQQKCPPKSK
Protein: Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1) (Q00637)
Organism: Drosophila melanogaster (Fruit fly)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Superoxide dismutase
- Small ribosomal subunit protein mS29
- Extracellular superoxide dismutase
- superoxide dismutase
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL17m
Sequence:
MFVARKISPNCKPGVRGKHTLPKLPYDYAALEPIICREIMELHHQKHHQTYVNNLNAAEEQLEEAKSKSDTTKLIQLAPALRFNGGGHINHTIFWQNLSPNKTQPSDDLKKAIESQWKSLEEFKKELTTLTVAVQGSGWGWLGFNKKSGKLQLAALPNQDPLEASTGLIPLFGIDVWEHAYYLQYKNVRPSYVEAIWDIANWDDISCRFQEAKKLGC
Protein: Xylosyltransferase 1 (EC 2.4.2.26) (Peptide O-xylosyltransferase 1) (Xylosyltransferase I) (XT-I) (XylT-I) (Q86Y38)
Organism: Homo sapiens (Human)
Function: Catalyzes the first step in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans, such as DCN. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein. Required for normal embryonic and postnatal skeleton development, especially of the long bones. Required for normal maturation of chondrocytes during bone development, and normal onset of ossification (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:23982343, ECO:0000269|PubMed:28462984}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:11087729, ECO:0000269|PubMed:16571645}. Note=Detected predominantly in the Golgi apparatus. {ECO:0000269|PubMed:28462984}.
Interaction partners:
- Beta-1,4-galactosyltransferase 7
- Xylosyltransferase 2
- Syndecan-1
- BOS complex subunit NOMO3
- ATP-binding cassette sub-family C member 6
- Beta-1,3-galactosyltransferase 6
- BOS complex subunit NOMO2
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
- Glycosaminoglycan xylosylkinase
Sequence:
MVAAPCARRLARRSHSALLAALTVLLLQTLVVWNFSSLDSGAGERRGGAAVGGGEQPPPAPAPRRERRDLPAEPAAARGGGGGGGGGGGGRGPQARARGGGPGEPRGQQPASRGALPARALDPHPSPLITLETQDGYFSHRPKEKVRTDSNNENSVPKDFENVDNSNFAPRTQKQKHQPELAKKPPSRQKELLKRKLEQQEKGKGHTFPGKGPGEVLPPGDRAAANSSHGKDVSRPPHARKTGGSSPETKYDQPPKCDISGKEAISALSRAKSKHCRQEIGETYCRHKLGLLMPEKVTRFCPLEGKANKNVQWDEDSVEYMPANPVRIAFVLVVHGRASRQLQRMFKAIYHKDHFYYIHVDKRSNYLHRQVLQVSRQYSNVRVTPWRMATIWGGASLLSTYLQSMRDLLEMTDWPWDFFINLSAADYPIRTNDQLVAFLSRYRDMNFLKSHGRDNARFIRKQGLDRLFLECDAHMWRLGDRRIPEGIAVDGGSDWFLLNRRFVEYVTFSTDDLVTKMKQFYSYTLLPAESFFHTVLENSPHCDTMVDNNLRITNWNRKLGCKCQYKHIVDWCGCSPNDFKPQDFHRFQQTARPTFFARKFEAVVNQEIIGQLDYYLYGNYPAGTPGLRSYWENVYDEPDGIHSLSDVTLTLYHSFARLGLRRAETSLHTDGENSCRYYPMGHPASVHLYFLADRFQGFLIKHHATNLAVSKLETLETWVMPKKVFKIASPPSDFGRLQFSEVGTDWDAKERLFRNFGGLLGPMDEPVGMQKWGKGPNVTVTVIWVDPVNVIAATYDILIESTAEFTHYKPPLNLPLRPGVWTVKILHHWVPVAETKFLVAPLTFSNRQPIKPEEALKLHNGPLRNAYMEQSFQSLNPVLSLPINPAQVEQARRNAASTGTALEGWLDSLVGGMWTAMDICATGPTACPVMQTCSQTAWSSFSPDPKSELGAVKPDGRLR
Protein: LexA repressor (EC 3.4.21.88) (Q49848)
Organism: Mycobacterium leprae (strain TN)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
- Protein RecA
- Arginine repressor
- ATP-dependent Clp protease ATP-binding subunit ClpX
- Heat-inducible transcription repressor HrcA
- Cell division protein FtsZ
Sequence:
MSDSTDISGITVDGRLHSMDSGLTERQRTILNVIRASVTSRGYPPSIREIADAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVNVRGVEETQAAGPAVLTEVAGSDVLPEPTFVPILGRIAAGSPIFAEGTVEDIFPLPRELVGEGTLFLLKVTGDSMVEAAICDGDWVVVRQQKVADNGDIVAAMIDGEATVKTFKRAGGQVWLIPHNPAFDPIPGNDATVLGKVVTVIRKI
Protein: UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase (EC 6.3.2.10) (D-alanyl-D-alanine-adding enzyme) (UDP-MurNAc-pentapeptide synthetase) (P11880)
Organism: Escherichia coli (strain K12)
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02019, ECO:0000269|PubMed:2186811}.
Interaction partners:
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- D-alanine--D-alanine ligase B
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UDP-N-acetylmuramate--L-alanine ligase
- Probable peptidoglycan glycosyltransferase FtsW
- D-alanine--D-alanine ligase A
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- Peptidoglycan D,D-transpeptidase FtsI
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Sequence:
MISVTLSQLTDILNGELQGADITLDAVTTDTRKLTPGCLFVALKGERFDAHDFADQAKAGGAGALLVSRPLDIDLPQLIVKDTRLAFGELAAWVRQQVPARVVALTGSSGKTSVKEMTAAILSQCGNTLYTAGNLNNDIGVPMTLLRLTPEYDYAVIELGANHQGEIAWTVSLTRPEAALVNNLAAAHLEGFGSLAGVAKAKGEIFSGLPENGIAIMNADNNDWLNWQSVIGSRKVWRFSPNAANSDFTATNIHVTSHGTEFTLQTPTGSVDVLLPLPGRHNIANALAAAALSMSVGATLDAIKAGLANLKAVPGRLFPIQLAENQLLLDDSYNANVGSMTAAVQVLAEMPGYRVLVVGDMAELGAESEACHVQVGEAAKAAGIDRVLSVGKQSHAISTASGVGEHFADKTALITRLKLLIAEQQVITILVKGSRSAAMEEVVRALQENGTC
Protein: Non-specific phospholipase C6 (EC 3.1.-.-) (Q8H965)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Phospholipase D beta 1
- Phospholipase D delta
- Phospholipase D alpha 1
- Choline/ethanolaminephosphotransferase 1
- Phosphatase IMPL1, chloroplastic
- Phosphoinositide phosphatase SAC7
- Inositol-phosphate phosphatase
- Phospholipase D gamma 1
- Phosphatidylinositol 4-kinase beta 1
Sequence:
MKPSSASRFSLTFSHFLTLYCLLTQTHVAQGSHQWQSPIKTVVVLVLENRSFDHLLGWMKNSVNPTINGVTGQECNPVPNSTQTICFTSDAEFVDPDPGHSFEAVEQQVFGSGPGQIPSMMGFVEQALSMPGNLSETVMKGFRPEAVPVYAELVKEFAVFDRWFSSIPGPTQPNRLFVYSATSHGSTSHVKKQLAQGYPQKTIFDSLHSNDIDFGIYFQNIPTTLFYRNLRQLKYIFNLHQYDLKFKKDAAKGKLPSLTVIEPRYFDLKGLPANDDHPSHDVANGQKLVKEVYEALRSSPQWNETLLVITYDEHGGFYDHVKTPYVGIPNPDGNTGPAPGFFKFDRLGVRVPTIMVSPWIQKGTVVSEAKGPTESSEYEHSSIPATIKKLFNLSSNFLTHRDAWAATFEDVVSHLTTPRTDCPMTLPEVAPMRATEPKEDAALSEFQGEVVQLAAVLNGDHFLSSFPEEIGKKMTVKQAHEYVKGATSRFIRASKEAMKLGADKSAIVDMRSSLTTRPHN
Protein: Small ribosomal subunit protein uS7 (40S ribosomal protein S5) (Q5AG43)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:35613268}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein eS30
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein eL13
- Small ribosomal subunit protein uS8A
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein uL6
Sequence:
MSDVEEQYQEEQQPVVQEELQVVELATTIPLDVQEAQREVKLFNKWSFEDVEVKDVSLVDYIQIRNPVFVSHTAGKYASKRFRKAQCPIVERLTNSLMMNGRNNGKKLKAVRIVKHALEIIHVLTEQNPIQVVVDAIVNSGAREDSTRIGSSGTVRRQAVDVSPLRRVNQAIALLTIGAREASFRNIKTIAECLAEELINAAKGSSTSYAIKKKDELERVAKSNR
Protein: Succinate--CoA ligase [ADP-forming] subunit alpha (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) (Q51567)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. Can also generate UTP or CTP, although it preferentially synthesizes ATP and/or GTP.
Interaction partners:
- Succinate--CoA ligase subunit beta
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- 2-oxoglutarate dehydrogenase E1 component
- Succinate dehydrogenase iron-sulfur subunit
- Succinate dehydrogenase flavoprotein subunit
- Succinate dehydrogenase cytochrome b556 subunit
- Succinate dehydrogenase hydrophobic membrane anchor subunit
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- NADH-quinone oxidoreductase subunit C/D
- Citrate synthase
Sequence:
MSVLINKDTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGLPVFNTVKEAVEATGAEASVIYVPAPFCKDSILEAAFGGIKLIVCITEGIPTLDMLDAKVKCDELGVRLIGPNCPGVITPGECKIGIMPGHIHLPGKVGIVSRSGTLTYEAVKQTTDAGFGQSTCVGIGGDPIPGSNFIDILKLFQEDPQTEAIVMIGEIGGSAEEEAAAFIKANVTKPVVSYIAGVTAPPGKRMGHAGAIISGGKGTADEKFAALQDAGVKTVRSLADIGKALAELTGWEVKKA
Protein: Nattererin-1 (P86913)
Organism: Physalaemus nattereri (Cuyaba dwarf frog) (Eupemphix nattereri)
Function: Probably has antibacterial activity.
Subcellular location: Secreted {ECO:0000269|PubMed:26443407}.
Interaction partners:
Sequence:
GLKDMIKNLAKEAAVKLAGAVINKFSPQPQ