Function and Biology Details
Reactions catalysed:
ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)
ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
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)
2 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Bifunctional glutamate/proline--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-139773 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional glutamate/proline--tRNA ligase
Molecule details ›
Chain: A
Length: 535 amino acids
Theoretical weight: 60.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 535 amino acids
Theoretical weight: 60.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P07814 (Residues: 1000-1512; Coverage: 34%)
Sequence domains:
- tRNA synthetase class II core domain (G, H, P, S and T)
- Anticodon binding domain
- Prolyl-tRNA synthetase, C-terminal
