Domain

Peptidase S8 propeptide/proteinase inhibitor I9 (IPR010259)

Short name: S8pro/Inhibitor_I9

Domain relationships

None.

Description

Proteinase propeptide inhibitors (sometimes refered to as activation peptides) are responsible for the modulation of folding and activity of the pro-enzyme or zymogen. The pro-segment docks into the enzyme moiety shielding the substrate binding site, thereby promoting inhibition of the enzyme. Several such propeptides share a similar topology [PMID: 12095256], despite often low sequence identities [PMID: 9811547]. The propeptide region has an open-sandwich antiparallel-alpha/antiparallel-beta fold, with two alpha-helices and four beta-strands with a (beta/alpha/beta)x2 topology.

This entry represents the propeptide domain at the N terminus of peptidases belonging to MEROPS family S8A, subtilisins. The subtilisin propeptides are known to function as molecular chaperones, assisting in the folding of the mature peptidase [PMID: 7559646]. The propeptide is removed by proteolytic cleavage; removal activating the enzyme. This domain is also found in members of MEROPS proteinase inhibitor family I9.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
GENE3D
Pfam