SMART: Pfam domain Peptidase

The domain within your query sequence starts at position 6 and ends at position 185; the E-value for the Peptidase_C15 domain shown below is 1.2e-21.

KAVVVTGFGPFGEHTVNASWIAVQELEKLGLGDSVDLHVYEIPVEYQTVQRLIPALWEKH
SPQLVVHVGVSGMATTVTLEKCGHNKGYKGLDNCRFCPGSQCCVEDGPESIDSIIDMDAV
CKRVTTLGLDVSVTISQDAGRYLCDFTYYTSLYQGRGRSAFVHVPPLGKPYNADQLGRAL

Peptidase_C15

PFAM accession number:	PF01470
Interpro abstract (IPR016125):	This group of cysteine peptidases belong to MEROPS peptidase family C15 (pyroglutamyl peptidase I, clan CF). The type example being pyroglutamyl peptidase I of Bacillus amyloliquefaciens. There are similarities in structure between members of clan CF and members of three clans of metallopeptidases (MC, MF and MH) and all four are included in the same superfamily (phosphorylase/hydrolase-like fold) by the SCOP database. Members of clan CF have an alpha/beta/alpha sandwich fold [ (PUBMED:1999) ]. Pyroglutamyl peptidase I (also known as pyrrolidone carboxyl peptidase, Pcp or PYRase) is an exopeptidase that hydrolytically removes the pGlu from pGlu-peptides or pGlu-proteins [ (PUBMED:7824521) (PUBMED:1353026) ]. PYRase has been found in prokaryotes and eukaryotes where at least two different classes have been characterised: the first containing bacterial and animal type I PYRases, and the second containing animal type II and serum PYRases. Type I and bacterial PYRases are soluble enzymes, while type II PYRases are membrane-bound. The primary application of PYRase has been its utilisation for protein or peptide sequencing, and bacterial diagnosis [ (PUBMED:1353026) ]. The conserved residues Cys-144 and His-168 have been identified by inhibition and mutagenesis studies [ (PUBMED:7824521) (PUBMED:7909543) ]. Pyroglutamyl-peptidase 1-like protein belongs to the petidase C15 family, though its exact function is not known.

PFAM accession number:

PF01470

Interpro abstract (IPR016125):

This group of cysteine peptidases belong to MEROPS peptidase family C15 (pyroglutamyl peptidase I, clan CF). The type example being pyroglutamyl peptidase I of Bacillus amyloliquefaciens. There are similarities in structure between members of clan CF and members of three clans of metallopeptidases (MC, MF and MH) and all four are included in the same superfamily (phosphorylase/hydrolase-like fold) by the SCOP database. Members of clan CF have an alpha/beta/alpha sandwich fold [ (PUBMED:1999) ].

Pyroglutamyl peptidase I (also known as pyrrolidone carboxyl peptidase, Pcp or PYRase) is an exopeptidase that hydrolytically removes the pGlu from pGlu-peptides or pGlu-proteins [ (PUBMED:7824521) (PUBMED:1353026) ]. PYRase has been found in prokaryotes and eukaryotes where at least two different classes have been characterised: the first containing bacterial and animal type I PYRases, and the second containing animal type II and serum PYRases. Type I and bacterial PYRases are soluble enzymes, while type II PYRases are membrane-bound. The primary application of PYRase has been its utilisation for protein or peptide sequencing, and bacterial diagnosis [ (PUBMED:1353026) ]. The conserved residues Cys-144 and His-168 have been identified by inhibition and mutagenesis studies [ (PUBMED:7824521) (PUBMED:7909543) ].

Pyroglutamyl-peptidase 1-like protein belongs to the petidase C15 family, though its exact function is not known.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_C15