InterPro : IPR025660

Name  Cysteine peptidase, histidine active site Short Name  Pept_his_AS
Type  Active_site Description  Thiol (cysteine) proteases (EC 3.4.22.-) []are a family of proteolytic enzymes which contain an active site cysteine. Catalysis proceeds through a thioester intermediate and is facilitated by a nearby histidine side chain; an asparagine completes the essential catalytic triad.Cysteine peptidases have characteristic molecular topologies, which can be seen not only in their three-dimensional structures, but commonly also in the two-dimensional structures. These are peptidases in which the nucleophile is the sulphydryl group of a cysteine residue. Cysteine proteases are divided into clans (proteins which are evolutionary related), and further sub-divided into families, on the basis of the architecture of their catalytic dyad (cysteine-histidene) or triad [].Modification of the catalytic triad, especially of its first amino acid (cysteine), has been postulated as a suitable target for a chemical modulation of enzyme function. This is the case for silicateins, where the cysteine residue has been replaced by a serine []. Silicateins represent a group of enzymes possessing bi-functional activity; in addition to the silica-condensing activity, they possess a proteolytic (cathepsin-like) activity [].The sequences around the three active site residues are well conserved. This entry represents the histidine active site. The catalytic triad consists of this entry, and . This catalytic triad detects mainly proteases of the C1 family, including papain and several cathepsins.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

0 Found In

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Barrett AJ Evolutionary lines of cysteine peptidases. 2001 Biol Chem 382 727-33
Dufour E Sequence homologies, hydrophobic profiles and secondary structures of cathepsins B, H and L: comparison with papain and actinidin. 1988 Biochimie 70 1335-42
Müller WE Silicateins, the major biosilica forming enzymes present in demosponges: protein analysis and phylogenetic relationship. 2007 Gene 395 62-71
Schröder HC Biofabrication of biosilica-glass by living organisms. 2008 Nat Prod Rep 25 455-74

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)