CATH Classification

Domain Context

CATH Clusters

Superfamily P-loop containing nucleotide triphosphate hydrolases
Functional Family

Enzyme Information

3.4.21.98
Hepacivirin.
based on mapping to UniProt O92972
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.
3.6.4.13
RNA helicase.
based on mapping to UniProt O92972
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 O92972
3.6.1.15
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt O92972
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.
2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt O92972
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.

UniProtKB Entries (1)

O92972
POLG_HCVJ4
Hepatitis C virus isolate HC-J4
Genome polyprotein

PDB Structure

PDB 2F55
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural and biological identification of residues on the surface of NS3 helicase required for optimal replication of the hepatitis C virus
Mackintosh, S.G., Lu, J.Z., Jordan, J.B., Harrison, M.K., Sikora, B., Sharma, S.D., Cameron, C.E., Raney, K.D., Sakon, J.
J.Biol.Chem.