Subtilisin SUB1-like catalytic domain (IPR034204)

Short name: PfSUB1-like_cat_dom

Overlapping homologous superfamilies

Domain relationships


This entry contains members of the peptidase family S8 (subtilisin) [PMID: 8439290]. Included in this entry are: PfSUB1 from the malaria parasite Plasmodium (MEROPS identifier S08.012), which activates the merozoite surface protein MSP1 allowing it to bind spectrin in the host erythrocyte membrane prior to egress [PMID: 26468747]; perkinsin from the pathogenic marine protozoan Perkinsus (S08.041); and MCP-01 peptidase from the deep-sea bacterium Pseudoalteromonas (S08.130), which degrades insoluble collagen [PMID: 18977758].

The subtilisin family is one of the largest serine peptidase families characterised to date. Over 200 subtilises are presently known, more than 170 of which with their complete amino acid sequence [PMID: 9070434]. It is widespread, being found in eubacteria, archaebacteria, eukaryotes and viruses [PMID: 7845208]. The vast majority of the family are endopeptidases, although there is an exopeptidase, tripeptidyl peptidase [PMID: 7845208, PMID: 8439290]. Structures have been determined for several members of the subtilisin family: they exploit the same catalytic triad as the chymotrypsins, although the residues occur in a different order (HDS in chymotrypsin and DHS in subtilisin), but the structures show no other similarity [PMID: 7845208, PMID: 8439290]. Some subtilisins are mosaic proteins, while others contain N- and C-terminal extensions that show no sequence similarity to any other known protein [PMID: 7845208].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
  • cd07473 (Peptidases_S8_Subtilisin_like)