Function and Biology Details
Reaction catalysed:
ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Lysyl-tRNA synthetase, class II, C-terminal
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Lysine-tRNA ligase, class II
- Nucleic acid-binding, OB-fold
- Aminoacyl-tRNA synthetase, class II
- Aminoacyl-tRNA synthetase, class II (D/K/N)
- OB-fold nucleic acid binding domain, AA-tRNA synthetase-type
- Lysine-tRNA ligase, class II, N-terminal
1 more domain
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Lysine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-184744 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysine--tRNA ligase
Molecule details ›
Chains: A, B, C, D
Length: 507 amino acids
Theoretical weight: 58.71 KDa
Source organism: Plasmodium falciparum NF54
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 507 amino acids
Theoretical weight: 58.71 KDa
Source organism: Plasmodium falciparum NF54
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8IDJ8 (Residues: 77-583; Coverage: 87%)
Sequence domains:
Structure domains:
