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Conserved domains on  [gi|50295448|gb|AAT73043|]
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platelet phospholipase A2 [Homo sapiens]

Protein Classification

PLA2c domain-containing protein( domain architecture ID 11081504)

PLA2c domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 22-130 1.04e-52

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: 162.01  E-value: 1.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50295448    22 LVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCG-TKFLSYKFSNSGSRITCAKQ 100
Cdd:pfam00068   1 LWQFGEMIKCTTGRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCGnPYLLSYNYSCSDGTITCSGN 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 50295448   101 DSCRSQLCECDKAAATCFARNktTYNKKYQ 130
Cdd:pfam00068  81 SSCEKQLCECDKAAAECFARA--TYNKKYK 108
 
Name Accession Description Interval E-value
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 22-130 1.04e-52

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: 162.01  E-value: 1.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50295448    22 LVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCG-TKFLSYKFSNSGSRITCAKQ 100
Cdd:pfam00068   1 LWQFGEMIKCTTGRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCGnPYLLSYNYSCSDGTITCSGN 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 50295448   101 DSCRSQLCECDKAAATCFARNktTYNKKYQ 130
Cdd:pfam00068  81 SSCEKQLCECDKAAAECFARA--TYNKKYK 108
PLA2c cd00125
PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca ...
 21-137 3.88e-50

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: 155.87  E-value: 3.88e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50295448  21 NLVNFHRMIKLTTGKEAaLSYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCA-K 99
Cdd:cd00125   1 NLLQFGKMIKCTTGRSA-LDYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGCSPYFTSYSYTCSDGQITCSdA 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 50295448 100 QDSCRSQLCECDKAAATCFARNKttYNKKYQYYSNKHC 137
Cdd:cd00125  80 NDKCARALCECDRAAALCFARAP--YNPKYRNYDKKRC 115
PA2c smart00085
Phospholipase A2;
21-137 1.89e-47

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 149.28  E-value: 1.89e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50295448     21 NLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITC-AK 99
Cdd:smart00085   1 NLWQFGNMIQCATGKRAWLSYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEKEGCNPKTTTYSYSCDNGFITCgGK 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 50295448    100 QDSCRSQLCECDKAAATCFARNktTYNKK-YQYYSNKHC 137
Cdd:smart00085  81 NTACLVFVCECDRAAAICFAKN--PYNKKnYNIDTKKRC 117
 
Name Accession Description Interval E-value
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 22-130 1.04e-52

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: 162.01  E-value: 1.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50295448    22 LVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCG-TKFLSYKFSNSGSRITCAKQ 100
Cdd:pfam00068   1 LWQFGEMIKCTTGRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCGnPYLLSYNYSCSDGTITCSGN 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 50295448   101 DSCRSQLCECDKAAATCFARNktTYNKKYQ 130
Cdd:pfam00068  81 SSCEKQLCECDKAAAECFARA--TYNKKYK 108
PLA2c cd00125
PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca ...
 21-137 3.88e-50

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: 155.87  E-value: 3.88e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50295448  21 NLVNFHRMIKLTTGKEAaLSYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCA-K 99
Cdd:cd00125   1 NLLQFGKMIKCTTGRSA-LDYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGCSPYFTSYSYTCSDGQITCSdA 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 50295448 100 QDSCRSQLCECDKAAATCFARNKttYNKKYQYYSNKHC 137
Cdd:cd00125  80 NDKCARALCECDRAAALCFARAP--YNPKYRNYDKKRC 115
PA2c smart00085
Phospholipase A2;
21-137 1.89e-47

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 149.28  E-value: 1.89e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50295448     21 NLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITC-AK 99
Cdd:smart00085   1 NLWQFGNMIQCATGKRAWLSYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEKEGCNPKTTTYSYSCDNGFITCgGK 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 50295448    100 QDSCRSQLCECDKAAATCFARNktTYNKK-YQYYSNKHC 137
Cdd:smart00085  81 NTACLVFVCECDRAAAICFAKN--PYNKKnYNIDTKKRC 117
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 43-121 2.26e-19

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: 76.83  E-value: 2.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50295448  43 FYGCHCGVGGRGS----PKDATDRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGsRITCAKQDSCRSQLCECDKAAATCF 118
Cdd:cd00618   2 PYGCYCGPGGSACpsgqPVDETDRCCRKHDCCYDQISDGGCCDGCLSYSFSEGG-VTCLTNSDLCTRSHCDCDRRLAICL 80


                ...
gi 50295448 119 ARN 121
Cdd:cd00618  81 ARA 83
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 44-142 1.63e-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: 62.49  E-value: 1.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50295448  44 YGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCGT-KFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFARnk 122
Cdd:cd04707  20 YGCYCGQEGEGLPVDELDRCCFQHRCCLEQASEMGCLQdRKLSTEVTCVDHKPKCEGVSVCEKLLCTCDKTAAECMAA-- 97

                        90       100
                ....*....|....*....|
gi 50295448 123 TTYNKKYQYYSNKHCRGSTP 142
Cdd:cd04707  98 AHFNSSLNSLDVSSCPGQVP 117
PLA2_plant cd04706
PLA2_plant: Plant-specific sub-family of Phospholipase A2, a super-family of secretory and ...
 44-117 1.09e-03

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: 36.64  E-value: 1.09e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50295448  44 YGCHCGVGGRG----SPKDATDRCCVTHDCCYKRLEKRGCGTKfLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATC 117
Cdd:cd04706  24 YGKYCGPGYSGcpgeRPCDDLDACCMTHDACVQAKKNDYLSLE-CNEKFKNCVRRFRKARKPTFEGNKCIVTFVIPVI 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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