Summary for clan CM
| History | MEROPS 7.60 (23 October 2006) |
| Description | Cysteine nucleophile; active peptidase is a homodimer with active site His and Glu from one monomer and Cys from the other. Catalytic residues in the order His, Glu, Cys in each monomer. |
| Contents of clan | Clan CM contains viral polyprotein endopeptidases. |
| Evidence | (See Protein fold.) |
| Catalytic mechanism | (See family C18.) |
| Peptidase activity | (See family C18.) |
| Protein fold | The tertiary structure has been determined for the NS2 protein from hepatitis C virus (Lorenz et al., 2006). The fold consists of a helical N-terminal subdomain, a long linker and a C-terminal domain containing a beta sheet. |
| Homologous non-peptidase families | The fold is unique for members of clan CM. |
| Activation mechanism | The active peptidase is a homodimer with two active sites each of which contains His and Glu from one monomer and Cys from the other (Lorenz et al., 2006). |
Families
| C18 |
hepatitis C virus peptidase 2 (hepatitis C virus) |
Yes |
Distribution of clan CM among Kingdoms of Organisms
