Family C27
Summary for family C27
Family type peptidase | C27.001 - rubella virus peptidase (Rubella virus), MEROPS Accession MER0002110 (peptidase unit: 1110-1275) |
Content of family | Peptidase family C27 contains the non-structural polyprotein processing endopeptidase from the rubella virus. |
History |
Identifier created: Perspect.Drug Discov.Des. 6:1-11 (1996) Rubella virus is a positive-strand RNA virus related to togaviruses such as Sindbis virus. The viral genome contains two polyprotein genes, one for structural proteins and a larger one for non-structural proteins. The structural polyprotein is processed by the host signalase (S26.010). The discovery that the endopeptidase is metal-dependent has led to the proposal that it is a metallopeptidase rather than a cysteine peptidase (Liu et al., 2000). |
Catalytic type | Cysteine |
Active site residues | C1152 H1273 |
Active site | The catalytic dyad, Cys1151 and His1272, has been identified by site-directed mutagenesis (Marr et al., 1994; Chen et al., 1996). However, His1272 has also been shown to be a zinc ligand (Liu et al., 2000). |
Activities and specificities | The endopeptidase processes the non-structural polyprotein at one site only, Gly1300Gly1301 (Chen et al., 1996). Cleavage occurs both in cis and in trans and divalent cations such as Zn2+ enhance activity (Liu et al., 1998). |
Inhibitors | High concentrations of the metal chelator phosphoramidon (1 mM) and the metallopeptidase inhibitor captopril (1 mM) have been shown to inhibit (Liu et al., 2000). |
Molecular structure | The limits of the endopeptidase within the polyprotein have been defined only approximately. The metal ligands have been determined by site-directed mutagenesis to be Cys1174, Cys1177, Cys1226 and His1272 (Liu et al., 2000). |
Clan | unassigned |
Basis of clan assignment | Active site residues for members of this family and family C1 occur in the same order in the sequence: C, H. |
Distribution of family
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Bacteria |
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Archaea |
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Protozoa |
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Fungi |
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Plants |
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Animals |
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Viruses |
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Peptidases and Homologues |
MEROPS ID |
Structure |
rubella virus peptidase | C27.001 | - |
Family C27 unassigned peptidases | unassigned | - |