InterPro : IPR002470

Name  Peptidase S9A, prolyl oligopeptidase Short Name  Peptidase_S9A
Type  Family Description  Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes []. 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 []. 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 [].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 []. The geometric orientations of the catalytic residues are similar between families, despite different protein folds []. 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) [, ].This group of serine peptidases belong to MEROPS peptidase family S9 (clan SC), subfamily S9A (prolyl oligopeptidase). The active site of members of this clan consists of a lineararrangement of serine, histidine and threonine catalytic residues []. Prolyl oligopeptidases are either located in the cytosol or they are membrane bound, where they cleave peptide bonds with prolyl P1 specificities (but cleavage of alanyl bonds has been detected). The proline must adopt a trans configuration within the chain. Peptides of up to 30 residues are cleaved [].
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

2 Contains

Id Name Short Name Type
IPR001375 Peptidase S9, prolyl oligopeptidase, catalytic domain Peptidase_S9 Domain
IPR002471 Peptidase S9, serine active site Pept_S9_AS Active_site

0 Found In

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Rawlings ND Evolutionary families of peptidases. 1993 Biochem J 290 ( Pt 1) 205-18
Rawlings ND Families of serine peptidases. 1994 Methods Enzymol 244 19-61



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)