InterPro : IPR000081

Name  Peptidase C3, picornavirus core protein 2A Short Name  Peptidase_C3
Type  Domain Description  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 or triad []. This domain defines cysteine peptidases belong to MEROPS peptidase family C3 (picornain, clan PA(C)), subfamilies 3CA and 3CB. The protein fold of this peptidase domain for members of this family resembles that of the serine peptidase, chymotrypsin [], the type example for clan PA.Picornaviral proteins are expressed as a single polyproteinwhich is cleaved by the viral 3C cysteine protease []. The poliovirus polyprotein is selectively cleaved between the Gln-|-Gly bond. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

0 Found In

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Zoll J Genetic analysis of mengovirus protein 2A: its function in polyprotein processing and virus reproduction. 1998 J Gen Virol 79 ( Pt 1) 17-25
Allaire M Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. 1994 Nature 369 72-6
Barrett AJ Evolutionary lines of cysteine peptidases. 2001 Biol Chem 382 727-33

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)