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Conserved domains on  [gi|2462584944|ref|XP_054181637|]
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group 3 secretory phospholipase A2 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
 133-246 1.87e-34

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: 121.48  E-value: 1.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584944 133 HQKGSKRPSKANTTA-LQDPMVSPRLdvaptglqgpqgglKPQGARWVCRSFRRHlDQCEHQIGPREIEFQLLNSAQEPL 211
Cdd:cd04705     1 TRLTSERRGLEKTGAiASSPDVSPFL--------------SEGEFKEPDRCCWKH-KQCPGHIIPPFSSDGHHNFHLHSV 65

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462584944 212 FHCNCTRRLARFLRLHSPPEVTNMLWELLGTTCFK 246
Cdd:cd04705    66 SHCDCDSRLKDCLRLSSSSRVGPTCSHLLGTTCFN 100
PLA2_like super family cl05417
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 35-66 2.47e-10

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.


The actual alignment was detected with superfamily member cd04704:

Pssm-ID: 471240  Cd Length: 97  Bit Score: 56.54  E-value: 2.47e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462584944  35 RFQQCLQNQHDSISDIVGVAFFNVLEIPCFVL 66
Cdd:cd04704    66 RFRQCLKNVNDSTSNQVGKIYFNVLQVPCFEL 97
 
Name Accession Description Interval E-value
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
 133-246 1.87e-34

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: 121.48  E-value: 1.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584944 133 HQKGSKRPSKANTTA-LQDPMVSPRLdvaptglqgpqgglKPQGARWVCRSFRRHlDQCEHQIGPREIEFQLLNSAQEPL 211
Cdd:cd04705     1 TRLTSERRGLEKTGAiASSPDVSPFL--------------SEGEFKEPDRCCWKH-KQCPGHIIPPFSSDGHHNFHLHSV 65

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462584944 212 FHCNCTRRLARFLRLHSPPEVTNMLWELLGTTCFK 246
Cdd:cd04705    66 SHCDCDSRLKDCLRLSSSSRVGPTCSHLLGTTCFN 100
PLA2_bee_venom_like cd04704
PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a ...
 35-66 2.47e-10

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: 56.54  E-value: 2.47e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462584944  35 RFQQCLQNQHDSISDIVGVAFFNVLEIPCFVL 66
Cdd:cd04704    66 RFRQCLKNVNDSTSNQVGKIYFNVLQVPCFEL 97
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
 35-67 1.95e-08

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


Pssm-ID: 461751  Cd Length: 97  Bit Score: 51.37  E-value: 1.95e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462584944  35 RFQQCLQNQHDSISDIVGVAFFNVLEIPCFVLE 67
Cdd:pfam05826  65 RFRRCLKNTNSSVSNAVGFIYFNVLQVKCFRLI 97
 
Name Accession Description Interval E-value
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
 133-246 1.87e-34

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: 121.48  E-value: 1.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462584944 133 HQKGSKRPSKANTTA-LQDPMVSPRLdvaptglqgpqgglKPQGARWVCRSFRRHlDQCEHQIGPREIEFQLLNSAQEPL 211
Cdd:cd04705     1 TRLTSERRGLEKTGAiASSPDVSPFL--------------SEGEFKEPDRCCWKH-KQCPGHIIPPFSSDGHHNFHLHSV 65

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462584944 212 FHCNCTRRLARFLRLHSPPEVTNMLWELLGTTCFK 246
Cdd:cd04705    66 SHCDCDSRLKDCLRLSSSSRVGPTCSHLLGTTCFN 100
PLA2_bee_venom_like cd04704
PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a ...
 35-66 2.47e-10

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: 56.54  E-value: 2.47e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462584944  35 RFQQCLQNQHDSISDIVGVAFFNVLEIPCFVL 66
Cdd:cd04704    66 RFRQCLKNVNDSTSNQVGKIYFNVLQVPCFEL 97
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
 35-67 1.95e-08

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


Pssm-ID: 461751  Cd Length: 97  Bit Score: 51.37  E-value: 1.95e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462584944  35 RFQQCLQNQHDSISDIVGVAFFNVLEIPCFVLE 67
Cdd:pfam05826  65 RFRRCLKNTNSSVSNAVGFIYFNVLQVKCFRLI 97
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 165-227 1.15e-06

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: 46.02  E-value: 1.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462584944 165 QGPQGGLKPQGARWVCRSFRRHlDQCEHQIGPRE-------------IEFQLLNSAQEPLFHCNCTRRLARFLRLH 227
Cdd:cd00618     9 PGGSACPSGQPVDETDRCCRKH-DCCYDQISDGGccdgclsysfsegGVTCLTNSDLCTRSHCDCDRRLAICLARA 83
 
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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