InterPro : IPR017295

Name  Peptidase S8A, subtilisin-related, cyanobacteria-1 Short Name  Pept_S8A_subtilisin_cyanobac-1
Type  Family Description  Limited proteolysis of most large protein precursors is carried out in vivo by the subtilisin-like pro-protein convertases. Many important biological processes such as peptide hormone synthesis, viral protein processing and receptor maturation involve proteolytic processing by these enzymes []. The subtilisin-serine protease (SRSP) family hormone and pro-protein convertases (furin, PC1/3, PC2, PC4, PACE4, PC5/6, and PC7/7/LPC) act within the secretory pathway to cleave polypeptide precursors at specific basic sites, generating their biologically active forms. Serum proteins, pro-hormones, receptors, zymogens, viral surface glycoproteins, bacterial toxins, amongst others, are activated by this route []. The SRSPs share the same domain structure, including a signal peptide, the pro-peptide, the catalytic domain, the P/middle or homo B domain, and the C terminus.This entry contains predicted subtilisin-related peptidases, predominantly found in cyanobacterial species. The peptides belong to MEROPS peptidase family S8A (subtilisin family, clan SB), and are unassigned.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

1 Contains

Id Name Short Name Type
IPR000209 Peptidase S8/S53 domain Peptidase_S8/S53_dom Domain

0 Found In

1 Parent Features

Id Name Short Name Type
IPR015500 Peptidase S8, subtilisin-related Peptidase_S8_subtilisin-rel Family

2 Publications

First Author Title Year Journal Volume Pages
Bergeron F Subtilase-like pro-protein convertases: from molecular specificity to therapeutic applications. 2000 J Mol Endocrinol 24 1-22
Gensberg K Subtilisin-related serine proteases in the mammalian constitutive secretory pathway. 1998 Semin Cell Dev Biol 9 11-7



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)