Function and Biology Details
Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|- and the P1' position is occupied by Gly-|-
NTP + H(2)O = NDP + phosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
3C-like protease (preferred)
PDBe Complex ID:
PDB-CPX-182857 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3C-like protease
Molecule details ›
Chains: A, B
Length: 182 amino acids
Theoretical weight: 19.58 KDa
Source organism: Norovirus Hu/1968/US
Expression system: Escherichia coli
UniProt:
Sequence domains: Southampton virus-type processing peptidase
Structure domains: Trypsin-like serine proteases
Length: 182 amino acids
Theoretical weight: 19.58 KDa
Source organism: Norovirus Hu/1968/US
Expression system: Escherichia coli
UniProt:
- Canonical:
Q83883 (Residues: 1100-1281; Coverage: 10%)
Sequence domains: Southampton virus-type processing peptidase
Structure domains: Trypsin-like serine proteases
