The domain within your query sequence starts at position 144 and ends at position 408; the E-value for the DLH domain shown below is 2.9e-9.

VRATLFLPPEPGPFPGIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKNMETM
HMEYFEEAVNYLRSHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGN
TISYKDETIPPVTILRNQVKMTKDGLKDVVDALQSPLVDKKSFIPVERSDTTFLFLVGQD
DHNWKSEFYADEISKRLQAHGKEKPQIICYPAAGHYIEPPYFPLCSAGMHLLVGANITFG
GEPKPHAMAQLDAWQQLQTFFHKQL

DLH

DLH
PFAM accession number:PF01738
Interpro abstract (IPR002925):

Dienelactone hydrolases play a crucial role in chlorocatechol degradation via the modified ortho cleavage pathway. Enzymes induced in 4-fluorobenzoate-utilizing bacteria have been classified into three groups on the basis of their specificity towards cis- and trans-dienelactone [ (PUBMED:7684040) ]. Some proteins contain repeated small fragments of this domain (for example rat kan-1 protein).

GO function:hydrolase activity (GO:0016787)

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