Function and Biology Details
Reaction catalysed:
ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- tRNA synthetase, B5-domain
- Phenylalanyl tRNA synthetase beta chain, core domain
- B3/B4 tRNA-binding domain
- Putative DNA-binding domain superfamily
- Phenylalanyl-tRNA synthetase-like, B3/B4
- Phenylalanine-tRNA ligase, class IIc, beta subunit
- Phenylalanine--tRNA ligase beta subunit, B1 domain
8 more domains
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Phenylalanyl-tRNA synthetase complex (preferred)
PDBe Complex ID:
PDB-CPX-192591 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Phenylalanine--tRNA ligase alpha subunit
Molecule details ›
Chains: A, C, E, G, I, K, M, O
Length: 508 amino acids
Theoretical weight: 57.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 508 amino acids
Theoretical weight: 57.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9Y285 (Residues: 1-508; Coverage: 100%)
Sequence domains:
- PheRS DNA binding domain 1
- PheRS DNA binding domain 3
- PheRS DNA binding domain 2
- tRNA synthetases class II core domain (F)
Phenylalanine--tRNA ligase beta subunit
Molecule details ›
Chains: B, D, F, H, J, L, N, P
Length: 589 amino acids
Theoretical weight: 66.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 589 amino acids
Theoretical weight: 66.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q9NSD9 (Residues: 1-589; Coverage: 100%)
Sequence domains:
- Phe-tRNA synthetase beta subunit B1 domain
- B3/4 domain
- tRNA synthetase B5 domain
- Phenylalanyl tRNA synthetase beta chain CLM domain
