The domain within your query sequence starts at position 43 and ends at position 149; the E-value for the Lipase_GDSL_2 domain shown below is 2.2e-12.

VFIGDSLVQLMHQCEIWRELFSPLHALNFGIGGDSTQHVLWRLENGELEHIRPKIVVVWV
GTNNHSHTAEQVTGGIKAIVQLVNKLQPQARVVVLVRALEEWQRKRG

Lipase_GDSL_2

Lipase_GDSL_2
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