CATH Classification

Domain Context

CATH Clusters

Superfamily Flavivirus RNA-directed RNA polymerase, thumb domain
Functional Family

Enzyme Information

2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt P27395
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 P27395
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.
2.1.1.56
mRNA (guanine-N(7)-)-methyltransferase.
based on mapping to UniProt P27395
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
-!- Adds an N(7)-methylguanine cap to mRNA. -!- The nucleoside next to the terminal guanosine may be either guanosine or adenosine.
3.4.21.91
Flavivirin.
based on mapping to UniProt P27395
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
3.6.4.13
RNA helicase.
based on mapping to UniProt P27395
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).
2.1.1.57
Methyltransferase cap1.
based on mapping to UniProt P27395
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)- (purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)- methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)- [mRNA].
-!- This enzyme catalyzes the methylation of the ribose on the first transcribed nucleotide of mRNA or snRNA molecules, which may be either guanosine or adenosine. -!- This methylation event is known as cap1, and occurs in all mRNAs and snRNAs of higher eukaryotes, including insects, vertebrates and their viruses. -!- The human enzyme can also methylate mRNA molecules that lack methylation on the capping 5'-triphosphoguanosine. -!- Formerly EC 2.1.1.58.

UniProtKB Entries (1)

P27395
POLG_JAEV1
Japanese encephalitis virus strain SA-14
Genome polyprotein

PDB Structure

PDB 4HDH
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
RNA-dependent RNA polymerase of Japanese encephalitis virus binds the initiator nucleotide GTP to form a mechanistically important pre-initiation state.
Surana, P., Satchidanandam, V., Nair, D.T.
Nucleic Acids Res.