CATH Classification

Domain Context

CATH Clusters

Superfamily RNA Helicase Chain A , domain 3
Functional Family Genome polyprotein

Enzyme Information

2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt Q9WMX2
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
-!- Catalyzes RNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- See also EC 2.7.7.6.
3.4.22.-
Cysteine endopeptidases.
based on mapping to UniProt Q9WMX2
3.6.4.13
RNA helicase.
based on mapping to UniProt Q9WMX2
ATP + H(2)O = ADP + phosphate.
-!- RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. -!- Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity. -!- Some helicases unwind DNA as well as RNA. -!- May be identical with EC 3.6.4.12 (DNA helicase).
3.6.1.15
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt Q9WMX2
NTP + H(2)O = NDP + phosphate.
-!- The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria. -!- Also hydrolyzes nucleoside diphosphates, thiamine diphosphate and FAD. -!- The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin.
3.4.21.98
Hepacivirin.
based on mapping to UniProt Q9WMX2
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'.
-!- Encoded by the genome of the viruses of the hepatitis C group, and contributes to the maturation of the precursor polyproteins. -!- The enzyme is greatly activated by binding of the 54-residue NS4A 'cofactor' protein also derived from the viral polyprotein. -!- Belongs to peptidase family S29.

UniProtKB Entries (1)

Q9WMX2
POLG_HCVCO
Hepatitis C virus (isolate Con1)
Genome polyprotein

PDB Structure

PDB 5E4F
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The Spring alpha-Helix Coordinates Multiple Modes of HCV (Hepatitis C Virus) NS3 Helicase Action.
Gu, M., Rice, C.M.
J.Biol.Chem.