The domain within your query sequence starts at position 11 and ends at position 158; the E-value for the Tyr_Deacylase domain shown below is 6.7e-39.

RALLQQCLHARLQVRPADGDAAAQWVEIRRGLVIYVCFFKGADTDLLPKMVNTLLNVKLS
ETETGKHVSILDLPGDVLIIPQATLGGRVKGRSMQYHSNSGKEEGSELYSQFVSLCEKAV
ANNTKSVEAGVAVAHGTYGNRWSHTQKE

Tyr_Deacylase

 Tyr_Deacylase
PFAM accession number:PF02580
Interpro abstract (IPR003732):

This family consists of D-aminoacyl-tRNA deacylase DTD, also known as D-Tyr-tRNA(Tyr) deacylase. It is an enzyme that cleaves misacetylated D-aminoacyl-tRNA molecules into free tRNAs and D-amino acids [ (PUBMED:11568181) (PUBMED:25441601) ]. Cell growth inhibition by several D-amino acids can be explained by an in vivo production of D-aminoacyl-tRNA molecules.

The enzyme is found in bacteria and in eukaryotes but not in archea. It has a beta barrel-like fold structure and forms homodimers in which two surface cavities serve as the active site for tRNA binding [ (PUBMED:10918062) (PUBMED:10766779) (PUBMED:10383414) ].

GO component:cytoplasm (GO:0005737)
GO function:aminoacyl-tRNA editing activity (GO:0002161), D-aminoacyl-tRNA deacylase activity (GO:0051499)

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