The domain within your query sequence starts at position 81 and ends at position 414; the E-value for the LCAT domain shown below is 1.7e-111.

FFTIWLDFNLFLPLGVDCWIDNTRIVYNHSSGRVSNAPGVQIRVPGFGKTESVEYVDDNK
LAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLAPHQQDEYYKKLAGLVEEMYAAYGKPVF
LIGHSLGCLHVLHFLLRQPQSWKDHFIDGFISLGAPWGGSIKAMRILASGDNQGIPILSN
IKLKEEQRITTTSPWMLPAPHVWPEDHVFISTPNFNYTVQDFERFFTDLHFEEGWHMFLQ
SRDLLERLPAPGVEVYCLYGVGRPTPHTYIYDHNFPYKDPVAALYEDGDDTVATRSTELC
GQWQGRQSQPVHLLPMNETDHLNMVFSNKTLEHI

LCAT

 LCAT
PFAM accession number:PF02450
Interpro abstract (IPR003386):

This entry represents a group of lipid metabolizing enzymes, including LACT and LPLA2 from humans, and PDAT from plants.

Lecithin:cholesterol acyltransferase (LACT), also known as phosphatidylcholine-sterol acyltransferase ( EC 2.3.1.43 ), is involved in extracellular metabolism of plasma lipoproteins, including cholesterol. It esterifies the free cholesterol transported in plasma lipoproteins, and is activated by apolipoprotein A-I. Its structure has been revealed [ (PUBMED:26195816) ]. Defects in LACT cause Fish eye disease and familial LCAT deficiency [ (PUBMED:8326012) ].

Phospholipid:diacylglycerol acyltransferase (PDAT)( EC 2.3.1.158 ) is involved in triacylglycerol formation by an acyl-CoA independent pathway. The enzyme specifically transfers acyl groups from the sn-2 position of a phospholipid to diacylglycerol, thus forming an sn-1-lysophospholipid [ (PUBMED:12963726) ].

Lysosomal phospholipase A2 (LPLA2) ( EC 3.1.1.5 ) plays important roles for lung surfactant metabolism and maturation of invariant natural killer T cells. Its structure has been revealed [ (PUBMED:25727495) ].

GO process:lipid metabolic process (GO:0006629)
GO function:O-acyltransferase activity (GO:0008374)

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