Protein Family Models

Date:

2024-08-14

This entry represents the first of the two ribosomal L25-like domains of the anticodon binding domain. Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organisms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln). [1]. 9562563. How glutaminyl-tRNA synthetase selects glutamine.. Rath VL, Silvian LF, Beijer B, Sproat BS, Steitz TA;. Structure 1998;6:439-449. (from Pfam)

Date:

2024-08-14

Members of this family include glutamate--tRNA ligases and tRNA glutamyl-Q(34) synthetase, both of which bind a tRNA and attach a glutamate residue, although at different sites on tRNA molecules, the latter at the anticodon site. It would be misleading to call the latter a glutamate--tRNA ligase, as the reaction is for base modification, rather than charging the tRNA with an amino acid destined for use in translation.

Date:

2024-08-14

glutamine--tRNA ligase catalyzes the attachment of glutamine to tRNA(Gln)

Date:

2023-03-08

Date:

2021-07-28

This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam HMM tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases.

Gene:

glnS

Date:

2024-05-30