The domain within your query sequence starts at position 10 and ends at position 539; the E-value for the COesterase domain shown below is 3.2e-157.
QALIWVIWIFGAIIEGSVTEEPHRYTKLGWVQGKQATVLGRLEPVNVFLGIPFAAPPLGP LRFSKPQPPIPWDNLREATAYPNLCFQNLEWLFIYQNLLKVSYPILGMSEDCLYLNIYAP CHANNGSSLPVMVWIPGGGFETGSASIFDGSALAVYEDVLVVTIQYRLGIFGFFTTQNQH APGNWAFWDQLAALLWVRENIKYFGGNPDSVTIFGNSAGAISISSLILSPLSADLFHRAI MQSGVAIIPSLKSSDNDLKHDLQVVANVCDCNVSDSKALLKCLREKSSLELMSLSQKAKS FTRVVDGSFFSEEPLELLSQKTLKIVPSIIGVNNQECGYILPVRDTPEILLGSNESTALT LIHTLLHIPTQHLYIVTKEYFHGKHSPTDIRDTLLDLFGDVFFVVPGLVTARYHRDSGGP VYFYEFQHRPHCFQNSRPAFVKADHTDEIRFVFGGPFLKGDVVMFEEATEEEKLLSRKMM KYWANFARSGDPNGADLPPWPVYDENEQYLELDVNISTGRRLKDQRVEFW
COesterase |
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PFAM accession number: | PF00135 |
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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