Function and Biology Details
Reactions catalysed:
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
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.
NTP + H(2)O = NDP + phosphate
ATP + H(2)O = ADP + phosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-209319 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Envelope protein E
Molecule details ›
Chain: A
Length: 114 amino acids
Theoretical weight: 12.87 KDa
Source organism: Dengue virus 2 Jamaica/1409/1983
Expression system: Escherichia coli
UniProt:
Structure domains: Immunoglobulin-like
Length: 114 amino acids
Theoretical weight: 12.87 KDa
Source organism: Dengue virus 2 Jamaica/1409/1983
Expression system: Escherichia coli
UniProt:
- Canonical:
P07564 (Residues: 576-680; Coverage: 3%)
Structure domains: Immunoglobulin-like
