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