SMART: Pfam domain Peptidase

The domain within your query sequence starts at position 20 and ends at position 211; the E-value for the Peptidase_S37 domain shown below is 1.4e-4.

IPPRLKTLGSPHLSASPTPDPAVARKYSVLYFEQKVDHFGFADMRTFKQRYLVADKHWQR
NGGSILFYTGNEGDIVWFCNNTGFMWDVAEELKAMLVFAEHRYYGESLPFGQDSFKDSQH
LNFLTSEQALADFAELIRHLEKTIPGAQGQPVIAIGGSYGGMLAAWFRMKYPHIVVGALA
ASAPIWQLDGMV

Peptidase_S37

PFAM accession number:	PF05576
Interpro abstract (IPR008761):	Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ (PUBMED:7845208) ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identified, these being grouped into clans on the basis of structural similarity and other functional evidence [ (PUBMED:7845208) ]. Structures are known for members of the clans and the structures indicate that some appear to be totally unrelated, suggesting different evolutionary origins for the serine peptidases [ (PUBMED:7845208) ]. Not withstanding their different evolutionary origins, there are similarities in the reaction mechanisms of several peptidases. Chymotrypsin, subtilisin and carboxypeptidase C have a catalytic triad of serine, aspartate and histidine in common: serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base [ (PUBMED:7845208) ]. The geometric orientations of the catalytic residues are similar between families, despite different protein folds [ (PUBMED:7845208) ]. The linear arrangements of the catalytic residues commonly reflect clan relationships. For example the catalytic triad in the chymotrypsin clan (PA) is ordered HDS, but is ordered DHS in the subtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) [ (PUBMED:7845208) (PUBMED:8439290) ]. These group of serine peptidases belong to MEROPS peptidase family S37 (clan SC). The members of this group of secreted peptidases are restricted to bacteria. In Streptomyces lividans the peptidase removes tripeptides from the N terminus of extracellular proteins (tripeptidyl aminopeptidase,Tap) [ (PUBMED:8920189) (PUBMED:7487044) ].

PFAM accession number:

PF05576

Interpro abstract (IPR008761):

Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ (PUBMED:7845208) ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identified, these being grouped into clans on the basis of structural similarity and other functional evidence [ (PUBMED:7845208) ]. Structures are known for members of the clans and the structures indicate that some appear to be totally unrelated, suggesting different evolutionary origins for the serine peptidases [ (PUBMED:7845208) ].

Not withstanding their different evolutionary origins, there are similarities in the reaction mechanisms of several peptidases. Chymotrypsin, subtilisin and carboxypeptidase C have a catalytic triad of serine, aspartate and histidine in common: serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base [ (PUBMED:7845208) ]. The geometric orientations of the catalytic residues are similar between families, despite different protein folds [ (PUBMED:7845208) ]. The linear arrangements of the catalytic residues commonly reflect clan relationships. For example the catalytic triad in the chymotrypsin clan (PA) is ordered HDS, but is ordered DHS in the subtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) [ (PUBMED:7845208) (PUBMED:8439290) ].

These group of serine peptidases belong to MEROPS peptidase family S37 (clan SC). The members of this group of secreted peptidases are restricted to bacteria. In Streptomyces lividans the peptidase removes tripeptides from the N terminus of extracellular proteins (tripeptidyl aminopeptidase,Tap) [ (PUBMED:8920189) (PUBMED:7487044) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_S37