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
ATGAAAAGATTACAAGAAAGATTTTTACGTTATGTAAAAATAGATACACAATCAGATCCA
AACTCTACAACTTTTCCTTCTACTTTAAAACAACTTGATTTATCTAAGTTGTTAGTTGAA
GAAATATCATCAATGGGTTTTGATGCAAGATTAGATAAAGACGGCTACGTTTATGCCAAA
ATCGATTCTAATATCGATAAGAAGGTGCCAAGTATTGGTTTTATCGCACACGTGGATACT
TCTCCAGATGCACCAGGTAAAGATGTAAATCCTAGAATTATTAAAAACTATGATGGTTCA
TTAATTAAACTAAACGAAACATTTCAGATGCATCCAGATAAGTACCCTTCGTTAAAAAAG
GTAATTGGTGAAGATATTATTGTCACTGACGGTAACACTTTATTAGGTGCCGATGATAAA
GCAGGTGTTGCAGAAATTATGGAACTACTTCATAGAATCGCTGATGATAAGTCTATCAAA
CATGGTGACATCTATATTTGTTTCACACCGGATGAAGAAATCGGACAAGGTGCTGATAGA
TTTGATTATGAATGGTTCAAAGCTGATTTTGCATATACTTTAGATGGTAGCGAAGTTGGT
GGTATTGAATACGAAAACTTTAACGCTGCAAGTGCAGACGTTAAATTTATCGGTAACTCC
ATACACCCAGGTAGTGCTAAAAATAAAATGATTAACGCACTTCACCTACAAATGGAGTTC
CATAGTATGTTACCTAAGTTTCTAGATCCAGCAATTACTGAAGGTTATGAAGGTTTTAAC
CACTTATCGAATGTAACTGGTCAAGTTGAAGAGGCTTCTGCACACTATATTATTAGAAAT
CACCATATGGCTAAGTTTTTAGAACAACAAAAAACTTTTGAAGCGATTAAAAACTATATG
AATGAAAAGTATGGTTATGAAGCTGTTGTATTACATATTAAAGAATCTTACTTAAATATG
TATGAAATTATTAAAGATCACATGTACGTGATTGATTATGCAGTCAATGCAACCAAAGCT
GCAGGCTTAACGCCTAAATTTGAAGCAATTCGTGGCGGTACAGATGGCGCTAGATTAACT
TATGGTGGACTTATTTGTCCAAACCTCGGTACAGGTGCATATCACTTCCATGGACGTTTA
GAGTTTGCAAGTATTAACCAAATGGAAAAAGCTGTTGAAGTTATGTTTAATATCATAAAG
GAAGTACAAAAATAA


>protein sequence
MKRLQERFLRYVKIDTQSDPNSTTFPSTLKQLDLSKLLVEEISSMGFDARLDKDGYVYAK
IDSNIDKKVPSIGFIAHVDTSPDAPGKDVNPRIIKNYDGSLIKLNETFQMHPDKYPSLKK
VIGEDIIVTDGNTLLGADDKAGVAEIMELLHRIADDKSIKHGDIYICFTPDEEIGQGADR
FDYEWFKADFAYTLDGSEVGGIEYENFNAASADVKFIGNSIHPGSAKNKMINALHLQMEF
HSMLPKFLDPAITEGYEGFNHLSNVTGQVEEASAHYIIRNHHMAKFLEQQKTFEAIKNYM
NEKYGYEAVVLHIKESYLNMYEIIKDHMYVIDYAVNATKAAGLTPKFEAIRGGTDGARLT
YGGLICPNLGTGAYHFHGRLEFASINQMEKAVEVMFNIIKEVQK






















© Fisunov Lab of Proteomics, 2016.