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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145207955 147 WTIPGTLWCGVGNSAENASELGVFHGPDLCCREHDQCPQTISPLQYNYGIRNFRFHTISHCDCDARFQQCLRSQGDSISD 226
Cdd:cd04704    1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTSN 80

                         90
                 ....*....|....*..
gi 145207955 227 IMGVAFFNVLEIPCFVL 243
Cdd:cd04704   81 QVGKIYFNVLQVPCFEL 97

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145207955 147 WTIPGTLWCGVGNSAENASELGVFHGPDLCCREHDQCPQTISPLQYNYGIRNFRFHTISHCDCDARFQQCLRSQGDSISD 226
Cdd:cd04704    1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTSN 80

                         90
                 ....*....|....*..
gi 145207955 227 IMGVAFFNVLEIPCFVL 243
Cdd:cd04704   81 QVGKIYFNVLQVPCFEL 97

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 145207955 295 PSKHPQKRGPQQTQARrhstttttpfqtpaiSSRPDMIPRgqpgvphlgfqdgPKHQSAHRVCRSLRHLDQCEHQIKPQE 374
Cdd:cd04705    1 TRLTSERRGLEKTGAI---------------ASSPDVSPF-------------LSEGEFKEPDRCCWKHKQCPGHIIPPF 52

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 145207955 375 TKFHLLNSAQMPLFHCDCTRRLARFLRLHSPPAGTDKVWDLLGTTCFK 422
Cdd:cd04705   53 SSDGHHNFHLHSVSHCDCDSRLKDCLRLSSSSRVGPTCSHLLGTTCFN 100

Phospholipase A2;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145207955   146 GWTIPGTLWC--GVGNSAENASELgvfhgpDLCCREHDQCPQTISPLQYNygirnfRFHTISHCDCDARFQQCLrsqGDS 223
Cdd:smart00085  17 AWLSYGDYGCycGWGGSGTPVDAT------DRCCFVHDCCYGKAEKEGCN------PKTTTYSYSCDNGFITCG---GKN 81

                           90
                   ....*....|....*...
gi 145207955   224 ISDIMGVAFFNVLEIPCF 241
Cdd:smart00085  82 TACLVFVCECDRAAAICF 99

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145207955 147 WTIPGTLWCGVGNSAENASELGVFHGPDLCCREHDQCPQTISPLQYNYGIRNFRFHTISHCDCDARFQQCLRSQGDSISD 226
Cdd:cd04704    1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTSN 80

                         90
                 ....*....|....*..
gi 145207955 227 IMGVAFFNVLEIPCFVL 243
Cdd:cd04704   81 QVGKIYFNVLQVPCFEL 97

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 145207955 295 PSKHPQKRGPQQTQARrhstttttpfqtpaiSSRPDMIPRgqpgvphlgfqdgPKHQSAHRVCRSLRHLDQCEHQIKPQE 374
Cdd:cd04705    1 TRLTSERRGLEKTGAI---------------ASSPDVSPF-------------LSEGEFKEPDRCCWKHKQCPGHIIPPF 52

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 145207955 375 TKFHLLNSAQMPLFHCDCTRRLARFLRLHSPPAGTDKVWDLLGTTCFK 422
Cdd:cd04705   53 SSDGHHNFHLHSVSHCDCDSRLKDCLRLSSSSRVGPTCSHLLGTTCFN 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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145207955 149 IPGTLWCGVGNSAENASELGvfHGPDLCCREHDQCPQTISPLQYNYGI-------------RNFRFHTISHCDCDARFQQ 215
Cdd:cd00618    1 LPYGCYCGPGGSACPSGQPV--DETDRCCRKHDCCYDQISDGGCCDGClsysfseggvtclTNSDLCTRSHCDCDRRLAI 78

                 ....
gi 145207955 216 CLRS 219
Cdd:cd00618   79 CLAR 82

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145207955  356 VCRSLRHLDQCEHQIKPQETKFHLLNSAQMPLFHCDCTRRLARFLR-LHSPPAGT--DKVWDLLGTTCFKL 423
Cdd:pfam05826  26 TDRCCREHDHCPDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKnTNSSVSNAvgFIYFNVLQVKCFRL 96