Peptidase S8A, subtilisin-related protease, kinetoplastidia (IPR017294)

Short name: Subtilisin-like_kinetoplast

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 putative subtilisin-related proteases from Kinetoplastida (Trypanosomatid protozoa).

Contributing signatures

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