Pathways & interactions
Peptidase S8A, subtilisin-related, cyanobacteria-1 (IPR017295)
Short name: Pept_S8A_subtilisin_cyanobac-1
Overlapping homologous superfamilies
- Peptidase S8/S53 domain superfamily (IPR036852)
- Peptidase S8, subtilisin-related (IPR015500)
- Peptidase S8A, subtilisin-related, cyanobacteria-1 (IPR017295)
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.
- PIRSF037851 (Subtilisin_cyano)