Summary for clan CM

Summary Alignment Structure Literature
HistoryMEROPS 7.60 (23 October 2006)
DescriptionCysteine 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 clanClan CM contains viral polyprotein endopeptidases.
Evidence(See Protein fold.)
Catalytic mechanism(See family C18.)
Peptidase activity(See family C18.)
Protein foldThe 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 familiesThe fold is unique for members of clan CM.
Activation mechanismThe 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).


Family Family Type Peptidase Structure
C18 hepatitis C virus peptidase 2 (hepatitis C virus) Yes

Distribution of clan CM among Kingdoms of Organisms