The domain within your query sequence starts at position 116 and ends at position 342; the E-value for the DLH domain shown below is 1.1e-6.
GPFKAKESGYPLIILSHGLGGFRASYSAFCMELASRGFVVAAVEHRDQSAAATYFCKPTS QESSPAESLEEEWLPFRRIKEGEKEFHVRNPQVHQRVKECVRVLRILQDASAGKTVVNVF PGGLDLMTLKGSIDRNRVAVMGHSFGGATAVLALTQEVQFRCAIALDAWMFPLERDFYPK ARGPVFFINVEKFQTVESVNLMKKICAQHEQSRIVTVLGAVHRSQTD
DLH |
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PFAM accession number: | PF01738 |
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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