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
3 more domains
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171573 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lysine--tRNA ligase
Molecule details ›
Chains: A, B
Length: 513 amino acids
Theoretical weight: 59.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 513 amino acids
Theoretical weight: 59.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q15046 (Residues: 70-581; Coverage: 86%)
Sequence domains:
Structure domains:
Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
Molecule details ›
Chain: C
Length: 44 amino acids
Theoretical weight: 5.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: AIMP2 lysyl-tRNA synthetase binding domain
Length: 44 amino acids
Theoretical weight: 5.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q13155 (Residues: 1-36; Coverage: 11%)
Sequence domains: AIMP2 lysyl-tRNA synthetase binding domain
