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glutamate--tRNA ligase family protein
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.
glutamyl-Q tRNA(Asp) synthetase
glutamyl-Q tRNA(Asp) synthetase catalyzes the tRNA-independent activation of glutamate in the presence of ATP and the subsequent transfer of glutamate onto tRNA(Asp)
tRNA glutamyl-Q(34) synthetase GluQRS
This protein resembles a shortened glutamyl-tRNA ligase, but its purpose is to modify tRNA(Asp) at a queuosine position in the anticodon rather than to charge a tRNA with its cognate amino acid.
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