Blast Analysis : gnl|CDD|199842

Analysis  rpsblast_cdd Start  1
End  79 Strand  +
Length  79 Note  Gaps:8
Hit Coverage  29.69 Hit Length  293
Hit Pident  47.13 E Val  4e-34
Hit Description  cd03858 M14_CP_N-E_like Peptidase M14 carboxypeptidase subfamily N/E-like. Carboxypeptidase (CP) N/E-like 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. The N/E subfamily includes eight members of which five (CPN CPE CPM CPD CPZ) are considered enzymatically active while the other three are non-active (CPX1 PCX2 ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form rather they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. 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. Hit Pcons  17.24
Name  Qrob_P0562420.2

1 Protein

Protein Identifier
Organism . Name
Score Score Type Protein Description Alias (in v1) Code Enzyme Gene Prediction Quality
Qrob_P0562420.2 Quercus robur 75.1 egn (M=2) 3.4.17.22 - Metallocarboxypeptidase D.   EC:3.4.17.22 validated