CATH Classification

Domain Context

CATH Clusters

Superfamily 6.10.250.1750
Functional Family

Enzyme Information

3.6.4.13
RNA helicase.
based on mapping to UniProt O39928
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).
3.4.22.-
Cysteine endopeptidases.
based on mapping to UniProt O39928
3.4.21.98
Hepacivirin.
based on mapping to UniProt O39928
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.
2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt O39928
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.
3.6.1.15
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt O39928
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.

UniProtKB Entries (1)

O39928
POLG_HCVEV
Hepatitis C virus (isolate EUH1480)
Genome polyprotein

PDB Structure

PDB 2M6X
External Links
Method SOLUTION NMR
Organism
Primary Citation
Unusual architecture of the p7 channel from hepatitis C virus
OuYang, B., Xie, S., Berardi, M.J., Zhao, X., Dev, J., Yu, W., Sun, B., Chou, J.J.
Nature
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