PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers.

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                ....*....|....*....|....*....|....*....|..
gi 38638476  12 RFGRYCGPLkikTAAVLDPAPYDDLDHCIGCHRHAVDGHEHG 53
Cdd:cd04706  23 RYGKYCGPG---YSGCPGERPCDDLDACCMTHDACVQAKKND 61

PLA2_plant: Plant-specific sub-family of Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. This sub-family does not appear to have a conserved active site and metal-binding loop.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 38638476  12 RFGRYCGPLkikTAAVLDPAPYDDLDHCIGCHRHAVDGHEHG 53
Cdd:cd04706  23 RYGKYCGPG---YSGCPGERPCDDLDACCMTHDACVQAKKND 61

PLA2_plant: Plant-specific sub-family of Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. This sub-family does not appear to have a conserved active site and metal-binding loop.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 38638476  12 RFGRYCGPLkikTAAVLDPAPYDDLDHCIGCHRHAVDGHEHG 53
Cdd:cd04706  23 RYGKYCGPG---YSGCPGERPCDDLDACCMTHDACVQAKKND 61