The domain within your query sequence starts at position 10 and ends at position 174; the E-value for the COesterase domain shown below is 6.9e-61.



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