The domain within your query sequence starts at position 34 and ends at position 139; the E-value for the COesterase domain shown below is 1.1e-6.



PFAM accession number:PF00135
Interpro abstract (IPR002018):

Higher eukaryotes have many distinct esterases. Among the different types are those which act on carboxylic esters ( EC 3.1.1 ). Carboxyl-esterases have been classified into three categories (A, B and C) on the basis of differential patterns of inhibition by organophosphates. The sequence of a number of type-B carboxylesterases indicates [ (PUBMED:3163407) (PUBMED:1862088) (PUBMED:8453375) ] that the majority are evolutionary related. As is the case for lipases and serine proteases, the catalytic apparatus of esterases involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.

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