Function and Biology Details
Reaction catalysed:
ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Valine-tRNA ligase
- Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain
- Rossmann-like alpha/beta/alpha sandwich fold
- Valyl-tRNA synthetase, tRNA-binding arm
- Class I and II aminoacyl-tRNA synthetase, tRNA-binding arm
- Valyl-tRNA synthetase, tRNA-binding arm superfamily
- Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding
- Aminoacyl-tRNA synthetase, class Ia, anticodon-binding
4 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Valine--tRNA ligase and RNA (preferred)
PDBe Complex ID:
PDB-CPX-161206 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Valine--tRNA ligase
Molecule details ›
Chains: A, B
Length: 862 amino acids
Theoretical weight: 98.91 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 862 amino acids
Theoretical weight: 98.91 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
- Canonical:
P96142 (Residues: 1-862; Coverage: 100%)
Sequence domains:
- tRNA synthetases class I (I, L, M and V)
- Anticodon-binding domain of tRNA ligase
- Valyl tRNA synthetase tRNA binding arm
