The domain within your query sequence starts at position 19 and ends at position 209; the E-value for the Lipase_GDSL_2 domain shown below is 2.8e-27.



PFAM accession number:PF13472
Interpro abstract (IPR013830):

This entry represents the SGNH hydrolase-type esterase domain, which has a similar fold to flavoproteins, namely a three-layer alpha/beta/alpha structure, where the beta-sheets are composed of five parallel strands. Enzymes containing this domain act as esterases and lipases, but have little sequence homology to true lipases [ (PUBMED:10801485) (PUBMED:15522763) ]. Proteins containing this type of esterase domain have been found in a variety of hydrolases; those with structural information include an esterase from Streptomyces scabies [ (PUBMED:7773790) ]; the esterase domain of viral haemagglutinin-esterase surface glycoproteins (influenza C virus, coronaviruses and toroviruses) [ (PUBMED:9817207) ]; mammalian acetylhydrolases [ (PUBMED:11522926) ]; fungal rhamnogalacturonan acetylesterase [ (PUBMED:11752785) ]; and the multifunctional enzyme thioesterase I (TAP) from Escherichia coli [ (PUBMED:12842470) ]. SGNH hydrolase-type esterase domains contain unique hydrogen bond network that stabilises their catalytic centres; they usually contain the catalytic triad Ser/Acid/His.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Lipase_GDSL_2