Function and Biology Details
Reaction catalysed:
ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Glutaminyl-tRNA synthetase, class Ib, non-specific RNA-binding domain 2
- Glutaminyl-tRNA synthetase, class Ib, non-specific RNA-binding domain, N-terminal, subdomain 2
- Glutaminyl-tRNA synthetase, class Ib, non-specific RNA-binding domain, N-terminal
- Glutaminyl-tRNA synthetase, class Ib, non-specific RNA-binding domain, N-terminal, subdomain 1
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Glutamine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-146493 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine--tRNA ligase
Molecule details ›
Chain: X
Length: 187 amino acids
Theoretical weight: 21.5 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Saccharomyces cerevisiae
UniProt:
Sequence domains: Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1
Structure domains:
Length: 187 amino acids
Theoretical weight: 21.5 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Saccharomyces cerevisiae
UniProt:
- Canonical:
P13188 (Residues: 1-187; Coverage: 23%)
Sequence domains: Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1
Structure domains:
