The domain within your query sequence starts at position 16 and ends at position 545; the E-value for the Phospholip_B domain shown below is 3.7e-198.

LLLLLPLLLQPPWAAGAASQSDPTGVHCATAYWSPESKKVEIKTVLDKNGDAYGYYNDSI
KTTGWGILEIRAGYGSQVLSNEIIMFLAGYLEGYLTALHMYDHFTNLYPQLFKNPSIVKK
VQDFMEKQEMWTRQNIKAQKDDPFWRHTGYVVTQLDGLYLGAQKRASEEKIKPMTMFQIQ
FLNAVGDLLDLIPSLSPTKSSSMMKFKIWEMGHCSALIKVLPGFENIYFAHSSWYTYAAM
LRIYKHWDFNIKDKYTLSKRLSFSSYPGFLESLDDFYILSSGLILLQTTNSVYNKTLLKQ
VVPKTLLAWQRVRVANMMAEGGKEWAQIFSKHNSGTYNNQYMVLDLKKVTINRSLDKGTL
YIVEQIPTYVEYSDQTNVLRKGYWASYNIPFHKTIYNWSGYPLLVHKLGLDYSYDLAPRA
KIFRRDQGNVTDMASMKYIMRYNNYKEDPYSKGDPCSTICCREDLNGASPSPGGCYDTKV
ADIFLASQYKAYAISGPTVQDGLPPFNWNRFNDTLHRGMPEVFDFNFVTM

Phospholip_B

 Phospholip_B
PFAM accession number:PF04916
Interpro abstract (IPR007000):

Phospholipase B (PLB) catalyses the hydrolytic cleavage of both acylester bonds of glycerophospholipids. This family of PLB enzymes has been identified in mammals, flies and nematodes but not in yeast [ (PUBMED:8892229) ]. In Drosophila this protein was named LAMA for laminin ancestor since it is expressed in the neuronal and glial precursors that surround the lamina [ (PUBMED:15193148) ].

GO function:phospholipase activity (GO:0004620)

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