InterPro : IPR008740

Name  Peptidase C30, Coronavirus endopeptidase Short Name  Peptidase_C30
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 group of cysteine peptidases correspond to MEROPS peptidase family C30 (clan PA(C)). These peptidases are related to serine endopeptidases of family S1 and are restricted to RNA viruses, where they are involved in viral polyprotein processing during replication [, , ].This entry represents the CoV M-pro which comprises three domains. Domains I and II are six-stranded antiparallel beta barrels and together resemble the architecture of chymotrypsin and of picornaviruses 3C proteinases. The substrate-binding site is located in a cleft between these two domains. The catalytic site is situated at the centre of the cleft. A long loop connects domain II to the C-terminal domain (domain III). This latter domain, a globular cluster of five helices, has been implicated in the proteolytic activity of M-pro. In the active site of M-pro, Cys and His form a catalytic dyad. In contrast to serine proteinases and other cysteine proteinases, which have a catalytic triad, there is no third catalytic residue present [, , , ].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

1 Found In

Id Name Short Name Type
IPR009003 Trypsin-like cysteine/serine peptidase domain Trypsin-like_Pept_dom Domain

0 Parent Features

7 Publications

First Author Title Year Journal Volume Pages
Barrett AJ Evolutionary lines of cysteine peptidases. 2001 Biol Chem 382 727-33
Ziebuhr J Virus-encoded proteinases and proteolytic processing in the Nidovirales. 2000 J Gen Virol 81 853-79
Anand K Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain. 2002 EMBO J 21 3213-24
Hegyi A Conservation of substrate specificities among coronavirus main proteases. 2002 J Gen Virol 83 595-9
Anand K Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. 2003 Science 300 1763-7
Xue X Structures of two coronavirus main proteases: implications for substrate binding and antiviral drug design. 2008 J Virol 82 2515-27
Zhao Q Structure of the main protease from a global infectious human coronavirus, HCoV-HKU1. 2008 J Virol 82 8647-55

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)