The domain within your query sequence starts at position 14 and ends at position 350; the E-value for the Lipase domain shown below is 1.1e-136.

CIFIQSSACGQGVGTEPFGRSLGATEASKPLKKPETRFLLFQDENDRLGCRLRPQHPETL
QECGFNSSQPLIMIIHGWSVDGLLENWIWKIVSALKSRQSQPVNVGLVDWISLAYQHYTI
AVQNTRIVGQDVAALLLWLEESAKFSRSKVHLIGYSLGAHVSGFAGSSMDGKNKIGRITG
LDPAGPMFEGTSPNERLSPDDANFVDAIHTFTREHMGLSVGIKQPIAHYDFYPNGGSFQP
GCHFLELYKHIAEHGLNAITQTIKCAHERSVHLFIDSLQHSDLQSIGFQCSDMGSFSQGL
CLSCKKGRCNTLGYDIRKDRSGKSKRLFLITRAQSPF

Lipase

Lipase
PFAM accession number:PF00151
Interpro abstract (IPR013818):

Triglyceride lipases (EC 3.1.1.3) are lipolytic enzymes that hydrolyse ester linkages of triglycerides [(PUBMED:3147715)]. Lipases are widely distributed in animals, plants and prokaryotes. At least three tissue-specific isozymes exist in higher vertebrates, pancreatic, hepatic and gastric/lingual. These lipases are closely related to each other and to lipoprotein lipase (EC 3.1.1.34), which hydrolyses triglycerides of chylomicrons and very low density lipoproteins (VLDL) [(PUBMED:2917565)]. The most conserved region in all these proteins is centred around a serine residue which has been shown [(PUBMED:2304545)] to participate, with an histidine and an aspartic acid residue, in a charge relay system. Such a region is also present in lipases of prokaryotic origin and in lecithin-cholesterol acyltransferase (EC 2.3.1.43) (LCAT) [(PUBMED:3458198)], which catalyzes fatty acid transfer between phosphatidylcholine and cholesterol.

Lipoprotein lipases also exhibit homology with a region of Drosophila vitellogenins. That region, represented by this entry, is entirely within the N-terminal domain of lipoprotein lipase and constitutes the segment where the similarity to hepatic and pancreatic lipases is most pronounced [(PUBMED:2917565)].

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