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Conserved domains on  [gi|79325386|ref|NP_001031744|]
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Phospholipase A2 family protein [Arabidopsis thaliana]

Protein Classification

PLA2_plant domain-containing protein( domain architecture ID 10140445)

PLA2_plant domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLA2_plant cd04706
PLA2_plant: Plant-specific sub-family of Phospholipase A2, a super-family of secretory and ...
 114-253 3.06e-47

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: 152.97  E-value: 3.06e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325386 114 PYVSKVPWHTGTRAFLSQL-FPRYGHYCGPNWSSGkdggsmvWDQRPIDWLDHCCYCHDIGYDTHdqaellKADMAFLEC 192
Cdd:cd04706   1 ISVPEECSRTCESYFCSGPpFLRYGKYCGPGYSGC-------PGERPCDDLDACCMTHDACVQAK------KNDYLSLEC 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79325386 193 LESNKRVVTRGDAQ-VAHFYKTMCITGLKSILIPYRSylvkiqygqnllDFGWIVSNLSKRS 253
Cdd:cd04706  68 NEKFKNCVRRFRKArKPTFEGNKCIVTFVIPVITVVM------------DAALIASKLGKRP 117
 
Name Accession Description Interval E-value
PLA2_plant cd04706
PLA2_plant: Plant-specific sub-family of Phospholipase A2, a super-family of secretory and ...
 114-253 3.06e-47

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: 152.97  E-value: 3.06e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325386 114 PYVSKVPWHTGTRAFLSQL-FPRYGHYCGPNWSSGkdggsmvWDQRPIDWLDHCCYCHDIGYDTHdqaellKADMAFLEC 192
Cdd:cd04706   1 ISVPEECSRTCESYFCSGPpFLRYGKYCGPGYSGC-------PGERPCDDLDACCMTHDACVQAK------KNDYLSLEC 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79325386 193 LESNKRVVTRGDAQ-VAHFYKTMCITGLKSILIPYRSylvkiqygqnllDFGWIVSNLSKRS 253
Cdd:cd04706  68 NEKFKNCVRRFRKArKPTFEGNKCIVTFVIPVITVVM------------DAALIASKLGKRP 117
PA2c smart00085
Phospholipase A2;
123-176 2.77e-03

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 36.80  E-value: 2.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 79325386    123 TGTRAFLSQLFprYGHYCGPnwssgkdGGSmvwdQRPIDWLDHCCYCHDIGYDT 176
Cdd:smart00085  13 TGKRAWLSYGD--YGCYCGW-------GGS----GTPVDATDRCCFVHDCCYGK 53
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 122-175 3.37e-03

Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognized. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognizes both families.


Pssm-ID: 459659  Cd Length: 108  Bit Score: 36.43  E-value: 3.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 79325386   122 HTGTRAFLSqlFPRYGHYCGPnwssgkdGGSMvwdqRPIDWLDHCCYCHDIGYD 175
Cdd:pfam00068  11 TTGRNPPLD--YNDYGCYCGL-------GGSG----TPVDATDRCCQAHDCCYE 51
 
Name Accession Description Interval E-value
PLA2_plant cd04706
PLA2_plant: Plant-specific sub-family of Phospholipase A2, a super-family of secretory and ...
 114-253 3.06e-47

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: 152.97  E-value: 3.06e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325386 114 PYVSKVPWHTGTRAFLSQL-FPRYGHYCGPNWSSGkdggsmvWDQRPIDWLDHCCYCHDIGYDTHdqaellKADMAFLEC 192
Cdd:cd04706   1 ISVPEECSRTCESYFCSGPpFLRYGKYCGPGYSGC-------PGERPCDDLDACCMTHDACVQAK------KNDYLSLEC 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79325386 193 LESNKRVVTRGDAQ-VAHFYKTMCITGLKSILIPYRSylvkiqygqnllDFGWIVSNLSKRS 253
Cdd:cd04706  68 NEKFKNCVRRFRKArKPTFEGNKCIVTFVIPVITVVM------------DAALIASKLGKRP 117
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 135-226 2.32e-13

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: 63.74  E-value: 2.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325386 135 RYGHYCGPNWSSGKDGgsmvwdqRPIDWLDHCCYCHDIGYDTHDQAELLKADMAFLEClesNKRVVTRGDAQVAHFYKTM 214
Cdd:cd00618   2 PYGCYCGPGGSACPSG-------QPVDETDRCCRKHDCCYDQISDGGCCDGCLSYSFS---EGGVTCLTNSDLCTRSHCD 71

                        90
                ....*....|..
gi 79325386 215 CITGLKSILIPY 226
Cdd:cd00618  72 CDRRLAICLARA 83
PA2c smart00085
Phospholipase A2;
123-176 2.77e-03

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 36.80  E-value: 2.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 79325386    123 TGTRAFLSQLFprYGHYCGPnwssgkdGGSmvwdQRPIDWLDHCCYCHDIGYDT 176
Cdd:smart00085  13 TGKRAWLSYGD--YGCYCGW-------GGS----GTPVDATDRCCFVHDCCYGK 53
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 122-175 3.37e-03

Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognized. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognizes both families.


Pssm-ID: 459659  Cd Length: 108  Bit Score: 36.43  E-value: 3.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 79325386   122 HTGTRAFLSqlFPRYGHYCGPnwssgkdGGSMvwdqRPIDWLDHCCYCHDIGYD 175
Cdd:pfam00068  11 TTGRNPPLD--YNDYGCYCGL-------GGSG----TPVDATDRCCQAHDCCYE 51
 
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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