CATH Classification
Level | CATH Code | Description |
---|---|---|
![]() |
1 | Mainly Alpha |
![]() |
1.10 | Orthogonal Bundle |
![]() |
1.10.820 | RNA Helicase; Chain A, domain 3 |
![]() |
1.10.820.10 | RNA Helicase Chain A , domain 3 |
Domain Context
CATH Clusters
Superfamily | RNA Helicase Chain A , domain 3 |
Functional Family | Genome polyprotein |
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).
|
3.6.1.15 |
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.
|
3.4.22.- |
Cysteine endopeptidases.
based on mapping to UniProt O92972
|
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
J.Biol.Chem.
|