Function and Biology Details
Reaction catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Translational (tr)-type GTP-binding domain
- Elongation factor Ts, dimerisation domain superfamily
- P-loop containing nucleoside triphosphate hydrolase
- Translation elongation factor EFTu/EF1A, bacterial/organelle
- Translation elongation factor Ts, conserved site
- Translation elongation factor EFTs/EF1B
- RNA-directed RNA polymerase, catalytic domain, bacteriophage
- DNA/RNA polymerase superfamily
11 more domains
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-238696 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct RNA molecules
2 distinct RNA molecules
Macromolecules (3 distinct):
Elongation factor Ts; Elongation factor Tu; RNA-directed RNA polymerase subunit beta
Molecule details ›
Chain: A
Length: 1289 amino acids
Theoretical weight: 141.42 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 1289 amino acids
Theoretical weight: 141.42 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
- Canonical:
P0A6P3 (Residues: 1-283; Coverage: 100%) - Canonical: P0A6N3 (Residues: 1-394; Coverage: 100%)
- Canonical: P14647 (Residues: 1-589; Coverage: 100%)
Sequence domains:
- Elongation factor TS
- Elongation factor Tu GTP binding domain
- Elongation factor Tu domain 2
- Elongation factor Tu C-terminal domain
- RNA replicase, beta-chain
