Conserved Protein Domain Family

cl17499: Peptidase_M14NE-CP-C_like Superfamily (this model, PSSM-Id:266731 is obsolete)
Click on image for an interactive view with Cn3D
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain
This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that 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. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.
Taxonomy: root
PubMed: 20 links
Protein: Related Protein
Related Structure
Accession: cl17499
PSSM Id: 266731
Name: Peptidase_M14NE-CP-C_like
Created: 13-Mar-2013
Updated: 16-Jan-2014
| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap