Description

IPR034185 is a Site-1 peptidase catalytic domain.

<p>Site-1 peptidase (also known as SKI-1 or type I membrane-bound subtilisin-kexin-isoenzyme; MEROPS identifier S08.063) is a secretory Ca²⁺-dependent serine endopeptidase and a member of the subtilisin family S8, subfamily S8A [[cite:PUB00000522]]. It cleaves at nonbasic residues: Thr, Leu, and Lys. Site-1 peptidase plays a critical role in the regulation of the synthesis and metabolism of cholesterol and fatty acid metabolism [[cite:PUB00082832]].</p> <p>The subtilisin family is one of the largest serine peptidase families characterised to date. Over 200 subtilisins are presently known, more than 170 of which have their complete amino acid sequence [[cite:PUB00006225]]. It is widespread, being found in eubacteria, archaebacteria, eukaryotes and viruses [[cite:PUB00003576]]. The vast majority of the family are endopeptidases, although there is an exopeptidase, tripeptidyl peptidase [[cite:PUB00003576], [cite:PUB00000522]]. 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 [[cite:PUB00003576], [cite:PUB00000522]]. Some subtilisins are mosaic proteins, while others contain N- and C-terminal extensions that show no sequence similarity to any other known protein [[cite:PUB00003576]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 1

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: