The domain within your query sequence starts at position 69 and ends at position 134; the E-value for the Glu-tRNAGln domain shown below is 2e-11.

REAVDRLEKAIAFADQLHAVDTDGVEPLESVLEDRCLYLRSDNVAEGSCAEELLQNSNHV
VEEYFV

Glu-tRNAGln

Glu-tRNAGln
PFAM accession number:PF02686
Interpro abstract (IPR003837):

This entry includes the C subunit of the bacterial/archaeal aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferases (known as GatC) and eukaryotic Glu-tRNAGln amidotransferases.

Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase ([intenz:6.3.5.-]) allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) [ (PUBMED:9342321) ]. The enzyme is composed of three subunits: A (an amidase), B and C. It also exists in eukaryotes as a protein targeted to the mitochondria.

The heterotrimer GatABC is involved in converting Glu to Gln and/or Asp to Asn, when the amino acid is attached to the appropriate tRNA. In Lactobacillus, GatABC is responsible for producing tRNA(Gln). In Archaea, GatABC is responsible for producing tRNA(Asn), while GatDE is responsible for producing tRNA(Gln). In lineages that include Thermus, Chlamydia, or Acidithiobacillus, the GatABC complex catalyses both tRNA(Gln) and tRNA(Asn).

GO process:regulation of translational fidelity (GO:0006450)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Glu-tRNAGln