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
- Proline-tRNA ligase, class II, C-terminal
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Prolyl-tRNA synthetase, class II
- Anticodon-binding
- Anticodon-binding domain superfamily
- Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)
2 more domains
Structure analysis Details
Assemblies composition:
Assembly name:
Proline--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-184695 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proline--tRNA ligase
Molecule details ›
Chains: A, B
Length: 497 amino acids
Theoretical weight: 57.8 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 497 amino acids
Theoretical weight: 57.8 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8I5R7 (Residues: 254-746; Coverage: 66%)
Sequence domains:
- tRNA synthetase class II core domain (G, H, P, S and T)
- Anticodon binding domain
- Prolyl-tRNA synthetase, C-terminal
