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Conserved domains on  [gi|1253558248|ref|NP_001343515|]
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phospholipase A2 isoform 2 precursor [Mus musculus]

Protein Classification

PLA2c domain-containing protein( domain architecture ID 10638107)

PLA2c domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PA2c smart00085
Phospholipase A2;
23-145 2.72e-51

Phospholipase A2;


:

Pssm-ID: 214508  Cd Length: 117  Bit Score: 158.91  E-value: 2.72e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253558248   23 VWQFRNMIKCTIpGSDPLKDYNNYGCYCGLGGWGTPVDDLDRCCQTHDHCYSQAKKlESCkflidNPYTNTYSYSCSGSE 102
Cdd:smart00085   2 LWQFGNMIQCAT-GKRAWLSYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEK-EGC-----NPKTTTYSYSCDNGF 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1253558248  103 ITCSAKNNKCEDFICNCDREAAICFSKVPYNKEYKNLDTGKFC 145
Cdd:smart00085  75 ITCGGKNTACLVFVCECDRAAAICFAKNPYNKKNYNIDTKKRC 117
 
Name Accession Description Interval E-value
PA2c smart00085
Phospholipase A2;
23-145 2.72e-51

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 158.91  E-value: 2.72e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253558248   23 VWQFRNMIKCTIpGSDPLKDYNNYGCYCGLGGWGTPVDDLDRCCQTHDHCYSQAKKlESCkflidNPYTNTYSYSCSGSE 102
Cdd:smart00085   2 LWQFGNMIQCAT-GKRAWLSYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEK-EGC-----NPKTTTYSYSCDNGF 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1253558248  103 ITCSAKNNKCEDFICNCDREAAICFSKVPYNKEYKNLDTGKFC 145
Cdd:smart00085  75 ITCGGKNTACLVFVCECDRAAAICFAKNPYNKKNYNIDTKKRC 117
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 23-137 5.89e-49

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: 152.76  E-value: 5.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253558248  23 VWQFRNMIKCTIpGSDPLKDYNNYGCYCGLGGWGTPVDDLDRCCQTHDHCYSQAKKLeSCKflidNPYTNTYSYSCSGSE 102
Cdd:pfam00068   1 LWQFGEMIKCTT-GRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKL-GCG----NPYLLSYNYSCSDGT 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1253558248 103 ITCSaKNNKCEDFICNCDREAAICFSKVPYNKEYK 137
Cdd:pfam00068  75 ITCS-GNSSCEKQLCECDKAAAECFARATYNKKYK 108
PLA2c cd00125
PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca ...
 22-140 6.91e-48

PLA2c: Phospholipase A2, a 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: 153091  Cd Length: 115  Bit Score: 150.09  E-value: 6.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253558248  22 AVWQFRNMIKCTIpGSDPLkDYNNYGCYCGLGGWGTPVDDLDRCCQTHDHCYSQAKKlESCkflidNPYTNTYSYSCSGS 101
Cdd:cd00125     1 NLLQFGKMIKCTT-GRSAL-DYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEK-GGC-----SPYFTSYSYTCSDG 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1253558248 102 EITCSAKNNKCEDFICNCDREAAICFSKVPYNKEYKNLD 140
Cdd:cd00125    73 QITCSDANDKCARALCECDRAAALCFARAPYNPKYRNYD 111
 
Name Accession Description Interval E-value
PA2c smart00085
Phospholipase A2;
23-145 2.72e-51

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 158.91  E-value: 2.72e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253558248   23 VWQFRNMIKCTIpGSDPLKDYNNYGCYCGLGGWGTPVDDLDRCCQTHDHCYSQAKKlESCkflidNPYTNTYSYSCSGSE 102
Cdd:smart00085   2 LWQFGNMIQCAT-GKRAWLSYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEK-EGC-----NPKTTTYSYSCDNGF 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1253558248  103 ITCSAKNNKCEDFICNCDREAAICFSKVPYNKEYKNLDTGKFC 145
Cdd:smart00085  75 ITCGGKNTACLVFVCECDRAAAICFAKNPYNKKNYNIDTKKRC 117
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 23-137 5.89e-49

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: 152.76  E-value: 5.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253558248  23 VWQFRNMIKCTIpGSDPLKDYNNYGCYCGLGGWGTPVDDLDRCCQTHDHCYSQAKKLeSCKflidNPYTNTYSYSCSGSE 102
Cdd:pfam00068   1 LWQFGEMIKCTT-GRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKL-GCG----NPYLLSYNYSCSDGT 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1253558248 103 ITCSaKNNKCEDFICNCDREAAICFSKVPYNKEYK 137
Cdd:pfam00068  75 ITCS-GNSSCEKQLCECDKAAAECFARATYNKKYK 108
PLA2c cd00125
PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca ...
 22-140 6.91e-48

PLA2c: Phospholipase A2, a 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: 153091  Cd Length: 115  Bit Score: 150.09  E-value: 6.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253558248  22 AVWQFRNMIKCTIpGSDPLkDYNNYGCYCGLGGWGTPVDDLDRCCQTHDHCYSQAKKlESCkflidNPYTNTYSYSCSGS 101
Cdd:cd00125     1 NLLQFGKMIKCTT-GRSAL-DYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEK-GGC-----SPYFTSYSYTCSDG 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1253558248 102 EITCSAKNNKCEDFICNCDREAAICFSKVPYNKEYKNLD 140
Cdd:cd00125    73 QITCSDANDKCARALCECDRAAALCFARAPYNPKYRNYD 111
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 44-130 9.49e-21

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: 80.30  E-value: 9.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253558248  44 NNYGCYCGLGG----WGTPVDDLDRCCQTHDHCYSQAKKLESCkflidnpyTNTYSYSCSGSEITCSAKNNKCEDFICNC 119
Cdd:cd00618     1 LPYGCYCGPGGsacpSGQPVDETDRCCRKHDCCYDQISDGGCC--------DGCLSYSFSEGGVTCLTNSDLCTRSHCDC 72

                          90
                  ....*....|.
gi 1253558248 120 DREAAICFSKV 130
Cdd:cd00618    73 DRRLAICLARA 83
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 25-141 1.34e-13

otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites.


Pssm-ID: 153096  Cd Length: 117  Bit Score: 62.88  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253558248  25 QFRNMIKCtIPGSDPlKDYNNYGCYCGLGGWGTPVDDLDRCCQTHDHCYSQAKKLESckflIDNPYTNTYsYSCSGSEIT 104
Cdd:cd04707     1 QLGEMLKC-LTGRCP-REFEDYGCYCGQEGEGLPVDELDRCCFQHRCCLEQASEMGC----LQDRKLSTE-VTCVDHKPK 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1253558248 105 CSAKNNkCEDFICNCDREAAICFSKVPYNKEYKNLDT 141
Cdd:cd04707    74 CEGVSV-CEKLLCTCDKTAAECMAAAHFNSSLNSLDV 109
PLA2_plant cd04706
PLA2_plant: Plant-specific sub-family of Phospholipase A2, a super-family of secretory and ...
 46-108 8.18e-07

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: 45.12  E-value: 8.18e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1253558248  46 YGCYCGL---GGWG-TPVDDLDRCCQTHDHCYsQAKKlesckflidNPYTNTysySCSGSEITCSAK 108
Cdd:cd04706    24 YGKYCGPgysGCPGeRPCDDLDACCMTHDACV-QAKK---------NDYLSL---ECNEKFKNCVRR 77
 
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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