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Conserved domains on  [gi|37079101|sp|P59888|]
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RecName: Full=Phospholipase A2 imperatoxin-1; AltName: Full=Imperatoxin I; Short=IpTx1; Short=IpTxi; AltName: Full=Imperatoxin inhibitor; Contains: RecName: Full=Imperatoxin-1 large subunit; AltName: Full=Imperatoxin I large subunit; Contains: RecName: Full=Imperatoxin-1 small subunit; AltName: Full=Imperatoxin I small subunit; Flags: Precursor

Protein Classification

Phospholip_A2_2 domain-containing protein( domain architecture ID 10140433)

Phospholip_A2_2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLA2_bee_venom_like cd04704
PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a ...
 32-130 1.23e-44

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.


:

Pssm-ID: 153093  Cd Length: 97  Bit Score: 142.06  E-value: 1.23e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37079101  32 TMWGTKWCGSGNEATDISELGYWSNLDSCCRTHDHCDNIPSG-QTKYGLTNEGKYTMMNCKCETAFEQCLRNVTGGMegp 110
Cdd:cd04704   2 IVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAgEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDST--- 78

                        90       100
                ....*....|....*....|
gi 37079101 111 aAGFVRKTYFDLYGNGCYNV 130
Cdd:cd04704  79 -SNQVGKIYFNVLQVPCFEL 97
 
Name Accession Description Interval E-value
PLA2_bee_venom_like cd04704
PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a ...
 32-130 1.23e-44

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.


Pssm-ID: 153093  Cd Length: 97  Bit Score: 142.06  E-value: 1.23e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37079101  32 TMWGTKWCGSGNEATDISELGYWSNLDSCCRTHDHCDNIPSG-QTKYGLTNEGKYTMMNCKCETAFEQCLRNVTGGMegp 110
Cdd:cd04704   2 IVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAgEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDST--- 78

                        90       100
                ....*....|....*....|
gi 37079101 111 aAGFVRKTYFDLYGNGCYNV 130
Cdd:cd04704  79 -SNQVGKIYFNVLQVPCFEL 97
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
 35-128 1.43e-30

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


Pssm-ID: 461751  Cd Length: 97  Bit Score: 106.46  E-value: 1.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37079101    35 GTKWCGSGNEATDISELGYWSNLDSCCRTHDHC-DNIPSGQTKYGLTNEGKYTMMNCKCETAFEQCLRNVtggmEGPAAG 113
Cdd:pfam05826   4 GTKWCGTGNIAENYDDLGEFDETDRCCREHDHCpDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKNT----NSSVSN 79

                          90
                  ....*....|....*
gi 37079101   114 FVRKTYFDLYGNGCY 128
Cdd:pfam05826  80 AVGFIYFNVLQVKCF 94
 
Name Accession Description Interval E-value
PLA2_bee_venom_like cd04704
PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a ...
 32-130 1.23e-44

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.


Pssm-ID: 153093  Cd Length: 97  Bit Score: 142.06  E-value: 1.23e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37079101  32 TMWGTKWCGSGNEATDISELGYWSNLDSCCRTHDHCDNIPSG-QTKYGLTNEGKYTMMNCKCETAFEQCLRNVTGGMegp 110
Cdd:cd04704   2 IVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAgEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDST--- 78

                        90       100
                ....*....|....*....|
gi 37079101 111 aAGFVRKTYFDLYGNGCYNV 130
Cdd:cd04704  79 -SNQVGKIYFNVLQVPCFEL 97
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
 35-128 1.43e-30

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


Pssm-ID: 461751  Cd Length: 97  Bit Score: 106.46  E-value: 1.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37079101    35 GTKWCGSGNEATDISELGYWSNLDSCCRTHDHC-DNIPSGQTKYGLTNEGKYTMMNCKCETAFEQCLRNVtggmEGPAAG 113
Cdd:pfam05826   4 GTKWCGTGNIAENYDDLGEFDETDRCCREHDHCpDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKNT----NSSVSN 79

                          90
                  ....*....|....*
gi 37079101   114 FVRKTYFDLYGNGCY 128
Cdd:pfam05826  80 AVGFIYFNVLQVKCF 94
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 33-103 4.14e-09

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.


Pssm-ID: 153092  Cd Length: 83  Bit Score: 51.03  E-value: 4.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37079101  33 MWGTKWCGSGNEATDISELGywSNLDSCCRTHDHCDNI--------------PSGQTKYGLTNEGKYTMMNCKCETAFEQ 98
Cdd:cd00618   1 LPYGCYCGPGGSACPSGQPV--DETDRCCRKHDCCYDQisdggccdgclsysFSEGGVTCLTNSDLCTRSHCDCDRRLAI 78


                ....*
gi 37079101  99 CLRNV 103
Cdd:cd00618  79 CLARA 83
PLA2_plant cd04706
PLA2_plant: Plant-specific sub-family of Phospholipase A2, a super-family of secretory and ...
 57-104 5.12e-04

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.


Pssm-ID: 153095  Cd Length: 117  Bit Score: 37.80  E-value: 5.12e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 37079101  57 LDSCCRTHDHCdnipsgqtkyglTNEGKYTMMNCKCETAFEQCLRNVT 104
Cdd:cd04706  44 LDACCMTHDAC------------VQAKKNDYLSLECNEKFKNCVRRFR 79
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
 58-129 9.17e-04

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.


Pssm-ID: 153094  Cd Length: 100  Bit Score: 36.73  E-value: 9.17e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37079101  58 DSCCRTHDHCD-NIPSGQTKYGLTNEGKYTMMNCKCETAFEQCLRNvtggmegPAAGFVRKTYFDLYGNGCYN 129
Cdd:cd04705  35 DRCCWKHKQCPgHIIPPFSSDGHHNFHLHSVSHCDCDSRLKDCLRL-------SSSSRVGPTCSHLLGTTCFN 100
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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