Function and Biology Details
Reaction catalysed:
ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proline-tRNA ligase, class IIa
- Proline-tRNA ligase, class IIa, archaeal-type
- Prolyl-tRNA synthetase, class II
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Proline-tRNA ligase, class II, C-terminal
- Anticodon-binding
- Anticodon-binding domain superfamily
- Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)
3 more domains
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Proline--tRNA ligase and RNA (preferred)
PDBe Complex ID:
PDB-CPX-178240 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Proline--tRNA ligase
Molecule details ›
Chains: A, B
Length: 477 amino acids
Theoretical weight: 54.56 KDa
Source organism: Thermus thermophilus
UniProt:
Sequence domains:
Length: 477 amino acids
Theoretical weight: 54.56 KDa
Source organism: Thermus thermophilus
UniProt:
- Canonical:
Q5SM28 (Residues: 1-477; Coverage: 100%)
Sequence domains:
- tRNA synthetase class II core domain (G, H, P, S and T)
- Anticodon binding domain
- Prolyl-tRNA synthetase, C-terminal
