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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046858371 151 WTIPGTLWCGVGNSAENASELGMFHGPDFCCREHDQCPQTISPLQYNYGIRNFRFHTISHCDCDARCRT 219
Cdd:cd04704     1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQ 69

PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is 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. Bee venom PLA2 has fewer conserved disulfide bridges than most canonical PLA2s.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046858371 151 WTIPGTLWCGVGNSAENASELGMFHGPDFCCREHDQCPQTISPLQYNYGIRNFRFHTISHCDCDARCRT 219
Cdd:cd04704     1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQ 69

PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 is 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858371 254 PSWKRGPQQTPARhhstttvtplqtpaiSSRPDMmIPRgqpgvshpglqdgPKRQGAHRVCRSLRHLDQCEHQIKPQETK 333
Cdd:cd04705     4 TSERRGLEKTGAI---------------ASSPDV-SPF-------------LSEGEFKEPDRCCWKHKQCPGHIIPPFSS 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1046858371 334 FHLLNSAQTPLFHCNCTRRLARFLRHHSLPANTNKVWELLGTTCFK 379
Cdd:cd04705    55 DGHHNFHLHSVSHCDCDSRLKDCLRLSSSSRVGPTCSHLLGTTCFN 100

Phospholipase A2;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858371  147 RRRGWTIPGTLWC--GVGNSAENASELgmfhgpDFCCREHDQCPQTISPLQYNygirnfRFHTISHCDCD 214
Cdd:smart00085  14 GKRAWLSYGDYGCycGWGGSGTPVDAT------DRCCFVHDCCYGKAEKEGCN------PKTTTYSYSCD 71

PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is 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. Bee venom PLA2 has fewer conserved disulfide bridges than most canonical PLA2s.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046858371 151 WTIPGTLWCGVGNSAENASELGMFHGPDFCCREHDQCPQTISPLQYNYGIRNFRFHTISHCDCDARCRT 219
Cdd:cd04704     1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQ 69

PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 is 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858371 254 PSWKRGPQQTPARhhstttvtplqtpaiSSRPDMmIPRgqpgvshpglqdgPKRQGAHRVCRSLRHLDQCEHQIKPQETK 333
Cdd:cd04705     4 TSERRGLEKTGAI---------------ASSPDV-SPF-------------LSEGEFKEPDRCCWKHKQCPGHIIPPFSS 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1046858371 334 FHLLNSAQTPLFHCNCTRRLARFLRHHSLPANTNKVWELLGTTCFK 379
Cdd:cd04705    55 DGHHNFHLHSVSHCDCDSRLKDCLRLSSSSRVGPTCSHLLGTTCFN 100

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046858371 153 IPGTLWCGVGNSAENASELGmfHGPDFCCREHDQCPQTISPLQYNYGI-------------RNFRFHTISHCDCDARCR 218
Cdd:cd00618     1 LPYGCYCGPGGSACPSGQPV--DETDRCCRKHDCCYDQISDGGCCDGClsysfseggvtclTNSDLCTRSHCDCDRRLA 77

Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from insects.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046858371 313 VCRSLRHLDQCEHQIKPQETKFHLLNSAQTPLFHCNCTRRLARFLRH-HSLPANT--NKVWELLGTTCFKL 380
Cdd:pfam05826  26 TDRCCREHDHCPDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKNtNSSVSNAvgFIYFNVLQVKCFRL 96