The domain within your query sequence starts at position 456 and ends at position 1012; the E-value for the PLAc domain shown below is 1.99e-10.

All catalytic sites are present in this domain. Check the literature (PubMed 10319815 ) for details.

LVRLVFPTSQEPLMRLELKKEEGPKELAVRLGCGPCPEEQAFLSKRKQVVAAALKKALQL
DQDLHEDEIPVIAVMATGGGIRAMTSLYGQLAGLQELGLLDCISYITGASGSTWALANLY
EDPEWSQKDLAGPTEVLKTQVTKSKLGALAPSQLWRYRQELAERARLGHPTCFTNLWALI
NEALLHDKPHEHKLSDQREALSRGQNPLPIYCALNSKEQGLSTFDFGEWCEFSPYEVGFP
KYGAFISSELFGSEFFMGRLVKQLPESRICFLEGIWSNLFAASLQDSLYWSSEPSQFWDR
WAQDQANLDKEQVPHLKIAEPPTMAGRIAELFTDLLTKRPLAHATHNFTRGLHFHKDYFQ
NSHFSAWKASKLDRLPNQLTPTEPHLCLLDVGYLINTSCPPLLQPTRDVDLILSLDYNLY
GAFQQLQLLSRFCQEQGIPFPSISPSPEEQRQPQECHLFCDPAQPEAPAVLHFPLVNDSF
QDYSAPGVPRTSEEKAAGEVNLSSSDSPYHYTKVTYSQEDVDKLLRLTHYNICNNQDRLR
EAMHQAVQRRRKRKQFR

PLAc

Cytoplasmic phospholipase A2, catalytic subunit
PLAc
SMART accession number:SM00022
Description: Cytosolic phospholipases A2 hydrolyse arachidonyl phospholipids. Family includes phospholipases B isoforms.
Interpro abstract (IPR002642):

This family consists of lysophospholipase / phospholipase B EC 3.1.1.5 and cytosolic phospholipase A2 which also has a C2 domain IPR000008 . Phospholipase B enzymes catalyse the release of fatty acids from lysophsopholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells [ (PUBMED:8027085) ]. Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca 2+ and selectively hydrolyses arachidonyl phospholipids [ (PUBMED:8051052) ], the aligned region corresponds the carboxy-terminal Ca 2+ -independent catalytic domain of the protein as discussed in [ (PUBMED:8051052) ].

GO process:phospholipid catabolic process (GO:0009395)
GO function:phospholipase activity (GO:0004620)
Family alignment:
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There are 4116 PLAc domains in 4116 proteins in SMART's nrdb database.

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