CATH Classification

Domain Context

CATH Clusters

Superfamily Trypsin-like serine proteases
Functional Family

Enzyme Information

2.1.1.57
Methyltransferase cap1.
based on mapping to UniProt P06935
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 P06935
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.
2.1.1.56
mRNA (guanine-N(7)-)-methyltransferase.
based on mapping to UniProt P06935
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 P06935
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.
3.6.4.13
RNA helicase.
based on mapping to UniProt P06935
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).
2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt P06935
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 (2)

P00974
BPT1_BOVIN
Bos taurus
Pancreatic trypsin inhibitor
P06935
POLG_WNV
West Nile virus
Genome polyprotein

PDB Structure

PDB 2IJO
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold.
Aleshin, A.E., Shiryaev, S.A., Strongin, A.Y., Liddington, R.C.
Protein Sci.