CATH Classification

Domain Context

CATH Clusters

Superfamily Vaccinia Virus protein VP39
Functional Family Genome polyprotein

Enzyme Information

2.1.1.56
mRNA (guanine-N(7)-)-methyltransferase.
based on mapping to UniProt Q5UB51
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.
3.6.1.15
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt Q5UB51
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.
3.4.21.91
Flavivirin.
based on mapping to UniProt Q5UB51
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.
2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt Q5UB51
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.
2.1.1.57
Methyltransferase cap1.
based on mapping to UniProt Q5UB51
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.
3.6.4.13
RNA helicase.
based on mapping to UniProt Q5UB51
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).

UniProtKB Entries (1)

Q5UB51
POLG_DEN3I
Dengue virus 3 Singapore/8120/1995
Genome polyprotein

PDB Structure

PDB 4V0R
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
A Crystal Structure of the Dengue Virus Ns5 Protein Reveals a Novel Inter-Domain Interface Essential for Protein Flexibility and Virus Replication.
Zhao, Y., Soh, T.S., Zheng, J., Chan, K.W.K., Phoo, W.W., Lee, C.C., Tay, M.Y.F., Swaminathan, K., Cornvik, T.C., Lim, S.P., Shi, P., Lescar, J., Vasudevan, S.G., Luo, D.
Plos Pathog.
CATH-Gene3D is a Global Biodata Core Resource Learn more...