Function and Biology Details
Reaction catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- RNA-directed RNA polymerase, palm domain superfamily, Birnavirus
- RNA-directed RNA polymerase, C-terminal domain superfamily, Avibirnavirus
- RNA-directed RNA polymerase, C-terminal, birnavirus
- RNA-directed RNA polymerase, thumb domain superfamily, Birnavirus
- RNA-directed RNA polymerase, thumb domain, birnavirus
- DNA/RNA polymerase superfamily
- Birnavirus RNA-directed RNA polymerase, palm domain
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
RNA-directed RNA polymerase (preferred)
PDBe Complex ID:
PDB-CPX-192981 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-directed RNA polymerase
Molecule details ›
Chain: A
Length: 852 amino acids
Theoretical weight: 94.65 KDa
Source organism: Infectious bursal disease virus
Expression system: Trichoplusia ni
UniProt:
Sequence domains:
Length: 852 amino acids
Theoretical weight: 94.65 KDa
Source organism: Infectious bursal disease virus
Expression system: Trichoplusia ni
UniProt:
- Canonical:
Q9Q6Q5 (Residues: 1-845; Coverage: 96%)
Sequence domains:
- Birnavirus RNA dependent RNA polymerase (VP1), palm domain
- Birnavirus RNA dependent RNA polymerase (VP1), thumb domain
- Birnavirus RNA dependent RNA polymerase (VP1), C-terminal
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID14-2
Spacegroup:
P6122
Expression system: Trichoplusia ni
