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
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- YbaK/aminoacyl-tRNA synthetase-associated domain superfamily
- Anticodon-binding
- Proline--tRNA ligase, anticodon binding domain
- Anticodon-binding domain superfamily
- YbaK/aminoacyl-tRNA synthetase-associated domain
- Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)
4 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Proline--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-182776 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proline--tRNA ligase
Molecule details ›
Chains: A, B
Length: 572 amino acids
Theoretical weight: 64.34 KDa
Source organism: Enterococcus faecalis
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 572 amino acids
Theoretical weight: 64.34 KDa
Source organism: Enterococcus faecalis
Expression system: Escherichia coli
UniProt:
- Canonical:
Q831W7 (Residues: 1-572; Coverage: 100%)
Sequence domains:
- tRNA synthetase class II core domain (G, H, P, S and T)
- Aminoacyl-tRNA editing domain
- Anticodon binding domain
