Peptidase S8A, subtilisin-related, cyanobacteria-1 (IPR017295)

Short name: Pept_S8A_subtilisin_cyanobac-1

Overlapping homologous superfamilies

Family relationships


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 [PMID: 10656993]. 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 [PMID: 9572109]. 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.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.