InterPro : IPR010259

Name  Peptidase S8 propeptide/proteinase inhibitor I9 Short Name  S8pro/Inhibitor_I9
Type  Domain 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 [], despite often low sequence identities []. 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 []. The propeptide is removed by proteolytic cleavage; removal activating the enzyme. This domain is also found in members of MEROPS proteinase inhibitor family I9.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

6 Found In

Id Name Short Name Type
IPR015500 Peptidase S8, subtilisin-related Peptidase_S8_subtilisin-rel Family
IPR017292 Peptidase S8A, Vpr Peptidase_S8A_Vpr Family
IPR012103 Peptidase S8A, bacillopeptidase F Pept_S8A_Bpr Family
IPR017311 Peptidase S8A, subtilisin-related, shewanella Pept_S8A_subtilisin_shewanella Family
IPR017312 Peptidase S8A, subtilisin-related, shewanella-2 Pept_S8A_subtilisin_shewan-2 Family
IPR017319 Peptidase S8A, subtilisin-related, prokarya Pept_S8A_subtilisin_pro Family

1 Parent Features

Id Name Short Name Type
IPR009020 Proteinase inhibitor, propeptide Prot_inh_propept Domain

3 Publications

First Author Title Year Journal Volume Pages
Jain SC The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 A resolution. 1998 J Mol Biol 284 137-44
Tangrea MA Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus. 2002 J Mol Biol 320 801-12
Li Y Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants. 1995 J Biol Chem 270 25127-32

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)