Function and Biology Details
Reactions catalysed:
ATP + H(2)O = ADP + phosphate
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.
NTP + H(2)O = NDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151111 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase S29 domain-containing protein
Molecule details ›
Chains: A, B
Length: 181 amino acids
Theoretical weight: 19.18 KDa
Source organism: Hepacivirus C
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains:
Length: 181 amino acids
Theoretical weight: 19.18 KDa
Source organism: Hepacivirus C
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q91RS4 (Residues: 1-181; Coverage: 100%)
Structure domains:
Non-structural protein 4A
Molecule details ›
Chains: C, D
Length: 21 amino acids
Theoretical weight: 2.08 KDa
Source organism: Hepatitis C virus (isolate H)
Expression system: Not provided
UniProt:
Length: 21 amino acids
Theoretical weight: 2.08 KDa
Source organism: Hepatitis C virus (isolate H)
Expression system: Not provided
UniProt:
- Canonical: P27958 (Residues: 1678-1696; Coverage: 1%)
