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  Domain Name: M14_CPO
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase O subgroup. Peptidase M14 carboxypeptidase (CP) O (CPO, also known as metallocarboxypeptidase C; EC 3.4.17.) belongs to the carboxypeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPO has not been well characterized as yet, and little is known about it. Based on modeling studies, CPO has been suggested to have specificity for acidic residues rather than aliphatic/aromatic residues as in A-like enzymes or basic residues as in B-like enzymes. It remains to be demonstrated that CPO is functional as an MCP.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 16
Total Disease Mutations Found: 2
This domain occurred 9 times on human genes (11 proteins).



  EPILEPSY, FAMILIAL TEMPORAL LOBE, 5
  FEBRILE SEIZURES, FAMILIAL, 11


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
Zn binding site
putative active site















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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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