The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes.

Article Details

Citation

Thommes P, Fett R, Schray B, Kunze N, Knippers R

The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes.

Nucleic Acids Res. 1988 Jun 24;16(12):5391-406.

PubMed ID
3290852 [ View in PubMed
]
Abstract

We have isolated from a Lambda-gt 11 library a human cDNA clone with one open reading frame of about 2400 bases. A stretch of about 350 amino acids in the deduced amino acid sequence is up to 40 percent identical with parts of the known amino acid sequences of E. coli and yeast glutaminyl (Gln)-tRNA synthetase. The isolated cDNA sequence corresponds to an internal section of a 5500 bases long mRNA that codes for a 170 kDa polypeptide associated with Gln-tRNA synthetase. Thus, the human enzyme is about three times larger than the E. coli and two times larger than the yeast Gln-tRNA synthetase. The three enzymes share an evolutionarily conserved core but differ in amino acid sequences linked to the N-terminal and C-terminal side of the core.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Bifunctional glutamate/proline--tRNA ligaseP07814Details