ACL_RS04935
  | Uniprot: A9NGX8
Description: peptidase T EC number: 3.-.-.-; 3.4.11.-; 3.4.11.4 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: Release of the N-terminal residue from a tripeptide. {ECO:0000256|SAAS:SAAS00064296}. Cofactor: COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR037215-2}; ; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR037215-2} Enzyme regulation: Function [CC]: FUNCTION: Cleaves the N-terminal amino acid of tripeptides. {ECO:0000256|SAAS:SAAS00370935}. Pathway: Active site: ACT_SITE 79 79 {ECO:0000256|PIRSR:PIRSR037215-1}.; ACT_SITE 172 172 Proton acceptor. {ECO:0000256|PIRSR:PIRSR037215-1}. Binding site: Calcium binding: DNA binding: Metal binding: METAL 77 77 Zinc 1. {ECO:0000256|PIRSR:PIRSR037215-2}.; METAL 138 138 Zinc 1. {ECO:0000256|PIRSR:PIRSR037215-2}.; METAL 138 138 Zinc 2. {ECO:0000256|PIRSR:PIRSR037215-2}.; METAL 173 173 Zinc 2. {ECO:0000256|PIRSR:PIRSR037215-2}.; METAL 195 195 Zinc 1. {ECO:0000256|PIRSR:PIRSR037215-2}.; METAL 377 377 Zinc 2. {ECO:0000256|PIRSR:PIRSR037215-2}. Nucleotide binding: Site: Gene names (primary): Gene names (synonym): Mass: 45,479 Subunit structure [CC]: Gene ontology (GO): cytoplasm [GO:0005737]; metallopeptidase activity [GO:0008237]; tripeptide aminopeptidase activity [GO:0045148]; zinc ion binding [GO:0008270]; peptide metabolic process [GO:0006518] Gene ontology IDs: GO:0005737; GO:0006518; GO:0008237; GO:0008270; GO:0045148 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the peptidase M20B family. {ECO:0000256|SAAS:SAAS00561302}. Protein families: Peptidase M20B family Coiled coil: Domain [FT]: DOMAIN 204 304 M20_dimer. {ECO:0000259|Pfam:PF07687}. Motif: Region: EMBL: CP000896 ProteinModelPortal: A9NGX8 MEROPS: EnsemblBacteria KO: ABX81608 UniPathway: K01258 CDD: Gene3D: cd03892 HAMAP: 3.30.70.360 InterPro: PANTHER: IPR001261;IPR002933;IPR011650;IPR010161 PIRSF: PRINTS: PIRSF037215 PROSITE: Pfam: PS00758;PS00759 ProDom: PF07687;PF01546 SMART: SUPFAM: TIGRFAMs: SSF55031 |
1019661-1020876(+) >nucleotide sequence AACTCTACAACTTTTCCTTCTACTTTAAAACAACTTGATTTATCTAAGTTGTTAGTTGAA GAAATATCATCAATGGGTTTTGATGCAAGATTAGATAAAGACGGCTACGTTTATGCCAAA ATCGATTCTAATATCGATAAGAAGGTGCCAAGTATTGGTTTTATCGCACACGTGGATACT TCTCCAGATGCACCAGGTAAAGATGTAAATCCTAGAATTATTAAAAACTATGATGGTTCA TTAATTAAACTAAACGAAACATTTCAGATGCATCCAGATAAGTACCCTTCGTTAAAAAAG GTAATTGGTGAAGATATTATTGTCACTGACGGTAACACTTTATTAGGTGCCGATGATAAA GCAGGTGTTGCAGAAATTATGGAACTACTTCATAGAATCGCTGATGATAAGTCTATCAAA CATGGTGACATCTATATTTGTTTCACACCGGATGAAGAAATCGGACAAGGTGCTGATAGA TTTGATTATGAATGGTTCAAAGCTGATTTTGCATATACTTTAGATGGTAGCGAAGTTGGT GGTATTGAATACGAAAACTTTAACGCTGCAAGTGCAGACGTTAAATTTATCGGTAACTCC ATACACCCAGGTAGTGCTAAAAATAAAATGATTAACGCACTTCACCTACAAATGGAGTTC CATAGTATGTTACCTAAGTTTCTAGATCCAGCAATTACTGAAGGTTATGAAGGTTTTAAC CACTTATCGAATGTAACTGGTCAAGTTGAAGAGGCTTCTGCACACTATATTATTAGAAAT CACCATATGGCTAAGTTTTTAGAACAACAAAAAACTTTTGAAGCGATTAAAAACTATATG AATGAAAAGTATGGTTATGAAGCTGTTGTATTACATATTAAAGAATCTTACTTAAATATG TATGAAATTATTAAAGATCACATGTACGTGATTGATTATGCAGTCAATGCAACCAAAGCT GCAGGCTTAACGCCTAAATTTGAAGCAATTCGTGGCGGTACAGATGGCGCTAGATTAACT TATGGTGGACTTATTTGTCCAAACCTCGGTACAGGTGCATATCACTTCCATGGACGTTTA GAGTTTGCAAGTATTAACCAAATGGAAAAAGCTGTTGAAGTTATGTTTAATATCATAAAG GAAGTACAAAAATAA >protein sequence IDSNIDKKVPSIGFIAHVDTSPDAPGKDVNPRIIKNYDGSLIKLNETFQMHPDKYPSLKK VIGEDIIVTDGNTLLGADDKAGVAEIMELLHRIADDKSIKHGDIYICFTPDEEIGQGADR FDYEWFKADFAYTLDGSEVGGIEYENFNAASADVKFIGNSIHPGSAKNKMINALHLQMEF HSMLPKFLDPAITEGYEGFNHLSNVTGQVEEASAHYIIRNHHMAKFLEQQKTFEAIKNYM NEKYGYEAVVLHIKESYLNMYEIIKDHMYVIDYAVNATKAAGLTPKFEAIRGGTDGARLT YGGLICPNLGTGAYHFHGRLEFASINQMEKAVEVMFNIIKEVQK |
© Fisunov Lab of Proteomics, 2016.