CATH Classification

Domain Context

CATH Clusters

Superfamily 2.60.40.350
Functional Family Genome polyprotein

Enzyme Information

2.1.1.56
mRNA (guanine-N(7)-)-methyltransferase.
based on mapping to UniProt Q01299
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.
2.1.1.57
Methyltransferase cap1.
based on mapping to UniProt Q01299
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.
3.6.1.15
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt Q01299
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 Q01299
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.
3.6.4.13
RNA helicase.
based on mapping to UniProt Q01299
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).
3.4.21.91
Flavivirin.
based on mapping to UniProt Q01299
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.

UniProtKB Entries (1)

Q01299
POLG_TBEVH
Tick-borne encephalitis virus (strain HYPR)
Genome polyprotein

PDB Structure

PDB 5O6V
External Links
Method ELECTRON MICROSCOPY
Organism
Primary Citation
Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody.
Fuzik, T., Formanova, P., Ruzek, D., Yoshii, K., Niedrig, M., Plevka, P.
Nat Commun
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