Function and Biology Details
Reaction catalysed:
ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Threonine-tRNA ligase, class IIa
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Anticodon-binding
- Threonine-tRNA ligase, class IIa, anticodon-binding domain
- Anticodon-binding domain superfamily
- Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)
- Aminoacyl-tRNA synthetase, class II
- Threonine-tRNA ligase catalytic core domain
2 more domains
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Threonine--tRNA ligase, mitochondrial and RNA (preferred)
PDBe Complex ID:
PDB-CPX-139446 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Threonine--tRNA ligase, mitochondrial
Molecule details ›
Chains: A, B
Length: 460 amino acids
Theoretical weight: 53.47 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 460 amino acids
Theoretical weight: 53.47 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical:
P07236 (Residues: 26-462; Coverage: 95%)
Sequence domains:
Structure domains:
