The domain within your query sequence starts at position 22 and ends at position 200; the E-value for the Pept_tRNA_hydro domain shown below is 6.3e-39.

LVAGLGNHGMPGTRHSVGMAVLGQIARRLGVAENWTRDSRCAADLALAPLGDAQLVLLRP
RRLMNVNGRSVARAAELFGLTAEEIYLVHDELDKPLGKLALKLGGSARGHNGVRSCISCL
NSNAMPRLLVGIGRPTHPNMVENHVLGCFSPEEQELLSPLMDQATDLLLDHIRARSQGP

Pept_tRNA_hydro

Pept_tRNA_hydro
PFAM accession number:PF01195
Interpro abstract (IPR001328):

Peptidyl-tRNA hydrolase ( EC 3.1.1.29 ) (PTH) is a bacterial enzyme that cleaves peptidyl-tRNA or N-acyl-aminoacyl-tRNA to yield free peptides or N-acyl-amino acids and tRNA. The natural substrate for this enzyme may be peptidyl-tRNA which drop off the ribosome during protein synthesis [ (PUBMED:1833189) (PUBMED:8635758) ]. Bacterial PTH has been found to be evolutionary related to a yeast protein [ (PUBMED:8563640) ].

This group also contains chloroplast RNA splicing 2 (CRS2), which is closely related nuclear-encoded protein required for the splicing of nine group II introns in chloroplasts [ (PUBMED:12881426) (PUBMED:9303320) (PUBMED:15078105) ].

GO function:aminoacyl-tRNA hydrolase activity (GO:0004045)

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