CATH Classification

Domain Context

CATH Clusters

Superfamily P-loop containing nucleotide triphosphate hydrolases
Functional Family

Enzyme Information

2.1.1.56
mRNA (guanine-N(7)-)-methyltransferase.
based on mapping to UniProt Q32ZD5
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.
3.6.4.13
RNA helicase.
based on mapping to UniProt Q32ZD5
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 Q32ZD5
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 Q32ZD5
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 Q32ZD5
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.
3.4.21.91
Flavivirin.
based on mapping to UniProt Q32ZD5
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)

Q32ZD5
POLG_KOKV
Kokobera virus
Genome polyprotein

PDB Structure

PDB 2V6J
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure and Biochemical Analysis of Kokobera Virus Helicase
Speroni, S., De Colibus, L., Mastrangelo, E., Gould, E., Coutard, B., Forrester, N.L., Blanc, S., Canard, B., Mattevi, A.
Proteins: Struct., Funct., Bioinf.