Function and Biology Details
Reactions catalysed:
(1a) S-adenosyl-L-methionine + G(5')pppAACA-[mRNA] = S-adenosyl-L-homocysteine + G(5')pppAmACA-[mRNA]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
(1a) (5')pppAACA-[mRNA] + (protein L)-L-histidine = diphosphate + (protein L)-L-histidyl-(5')phosphonato-AACA-[mRNA] + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Filoviridae VP35 protein
- Filoviruses VP35 interferon inhibitory domain
- Filoviruses VP35 interferon inhibitory domain, beta-sheet subdomain
- Filoviruses VP35 interferon inhibitory domain, helical subdomain
- Mononegavirales RNA-directed RNA polymerase catalytic domain
- Mononegavirus L protein 2-O-ribose methyltransferase
- RNA-directed RNA polymerase L, C-terminal
- Mononegavirales mRNA-capping domain V
1 more domain
Structure analysis Details
Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-103299 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RNA-directed RNA polymerase L
Molecule details ›
Chain: A
Length: 2212 amino acids
Theoretical weight: 252.86 KDa
Source organism: Ebola virus
Expression system: Spodoptera aff. frugiperda 1 BOLD-2017
UniProt:
Sequence domains:
Length: 2212 amino acids
Theoretical weight: 252.86 KDa
Source organism: Ebola virus
Expression system: Spodoptera aff. frugiperda 1 BOLD-2017
UniProt:
- Canonical:
A0A1C4HDB0 (Residues: 1-2212; Coverage: 100%)
Sequence domains:
Polymerase cofactor VP35
Molecule details ›
Chains: B, C, D, E
Length: 340 amino acids
Theoretical weight: 37.49 KDa
Source organism: Ebola virus
Expression system: Spodoptera aff. frugiperda 1 BOLD-2017
UniProt:
Sequence domains: Filoviridae VP35
Length: 340 amino acids
Theoretical weight: 37.49 KDa
Source organism: Ebola virus
Expression system: Spodoptera aff. frugiperda 1 BOLD-2017
UniProt:
- Canonical: A0A1C4HDK9 (Residues: 1-340; Coverage: 100%)
Sequence domains: Filoviridae VP35
