SMART: Pfam domain Peptidase_S9

The domain within your query sequence starts at position 7 and ends at position 423; the E-value for the Peptidase_S9_N domain shown below is 1.2e-170.

PDVYRDETSVQEYHGHKICDPYSWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKER
MTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNTLSDDGTVA
LRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFTCMAWTHDGKGMF
YNSYPQQDGKSDGTETSTNLHQKLCYHVLGTDQSEDILCAEFPDEPKWMGGAELSDDGRY
VLLSIWEGCDPVNRLWYCDLQQEPNGITGILKWVKLIDNFEGEYDYVTNEGTVFTFKTNR
NSPNYRLINIDFTDPDESKWKVLVPEHEKDVLEWVACVRSNFLVLCYLHDVKNILQLHDL
TTGALLKTFPLDVGSVVGYSGRKKDSEIFYQFTSFLSPGVIYHCDLTKEELEPMVFR

Peptidase_S9_N

PFAM accession number:	PF02897
Interpro abstract (IPR023302):	This entry represents the beta-propeller domain found at the N-terminal of prolyl oligopeptidase from the MEROPS peptidase family S9A. The prolyl oligopeptidase family consist of a number of evolutionary related peptidases whose catalytic activity seems to be provided by a charge relay system similar to that of the trypsin family of serine proteases, but which evolved by independent convergent evolution. The N-terminal domain of prolyl oligopeptidases form an unusual 7-bladed beta-propeller consisting of seven 4-stranded beta-sheet motifs. Prolyl oligopeptidase is a large cytosolic enzyme involved in the maturation and degradation of peptide hormones and neuropeptides, which relate to the induction of amnesia. The enzyme contains a peptidase domain, where its catalytic triad (Ser554, His680, Asp641) is covered by the central tunnel of the N-terminal beta-propeller domain. In this way, large structured peptides are excluded from the active site, thereby protecting larger peptides and proteins from proteolysis in the cytosol [ (PUBMED:9695945) ].
GO function:	serine-type endopeptidase activity (GO:0004252)

PFAM accession number:

PF02897

Interpro abstract (IPR023302):

This entry represents the beta-propeller domain found at the N-terminal of prolyl oligopeptidase from the MEROPS peptidase family S9A. The prolyl oligopeptidase family consist of a number of evolutionary related peptidases whose catalytic activity seems to be provided by a charge relay system similar to that of the trypsin family of serine proteases, but which evolved by independent convergent evolution. The N-terminal domain of prolyl oligopeptidases form an unusual 7-bladed beta-propeller consisting of seven 4-stranded beta-sheet motifs.

Prolyl oligopeptidase is a large cytosolic enzyme involved in the maturation and degradation of peptide hormones and neuropeptides, which relate to the induction of amnesia. The enzyme contains a peptidase domain, where its catalytic triad (Ser554, His680, Asp641) is covered by the central tunnel of the N-terminal beta-propeller domain. In this way, large structured peptides are excluded from the active site, thereby protecting larger peptides and proteins from proteolysis in the cytosol [ (PUBMED:9695945) ].

GO function:

serine-type endopeptidase activity (GO:0004252)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_S9_N