The domain within your query sequence starts at position 28 and ends at position 104; the E-value for the Propep_M14 domain shown below is 2.3e-17.



PFAM accession number:PF02244
Interpro abstract (IPR003146):

The peptidases are synthesised as inactive molecules, zymogens, with propeptides that must be removed by proteolytic cleavage to activate the enzyme. Structural studies of carboxypeptidases A and B reveal the propeptide to exist as a globular domain, followed by an extended alpha-helix; this shields the catalytic site, without specifically binding to it, while the substrate-binding site is blocked by making specific contacts [ (PUBMED:7674922) (PUBMED:1548696) ].

This entry represents a propeptide associated with peptidases belonging to MEROPS peptidase family M14A. It is found in the carboxypeptidases A [ (PUBMED:9384570) ] and B [ (PUBMED:12162965) ].

Carboxypeptidases are found in abundance in pancreatic secretions. The pro-segment moiety (propeptide or activation peptide) accounts for up to a quarter of the total length of the peptidase.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Propep_M14