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Conserved domains on  [gi|157822409|ref|NP_001099485|]
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group 3 secretory phospholipase A2 precursor [Rattus norvegicus]

Protein Classification

PLA2_bee_venom_like and PLA2_group_III_like domain-containing protein( domain architecture ID 10140434)

PLA2_bee_venom_like and PLA2_group_III_like 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 ...
151-247 4.31e-50

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: 166.32  E-value: 4.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822409 151 WTIPGTLWCGVGNSAENASELGMFHGPDFCCREHDQCPQTISPLQYNYGIRNFRFHTISHCDCDARFQQCLRSQGDSIAD 230
Cdd:cd04704    1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTSN 80
                         90
                 ....*....|....*..
gi 157822409 231 IMGVAFFNVLEIPCFVL 247
Cdd:cd04704   81 QVGKIYFNVLQVPCFEL 97
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
299-424 2.33e-26

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: 102.60  E-value: 2.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822409 299 PSWKRGPQQTPARhhstttvtplqtpaiSSRPDMmIPRgqpgvshpglqdgPKRQGAHRVCRSLRHLDQCEHQIKPQETK 378
Cdd:cd04705    4 TSERRGLEKTGAI---------------ASSPDV-SPF-------------LSEGEFKEPDRCCWKHKQCPGHIIPPFSS 54
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 157822409 379 FHLLNSAQTPLFHCNCTRRLARFLRHHSLPANTNKVWELLGTTCFK 424
Cdd:cd04705   55 DGHHNFHLHSVSHCDCDSRLKDCLRLSSSSRVGPTCSHLLGTTCFN 100
 
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 ...
151-247 4.31e-50

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: 166.32  E-value: 4.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822409 151 WTIPGTLWCGVGNSAENASELGMFHGPDFCCREHDQCPQTISPLQYNYGIRNFRFHTISHCDCDARFQQCLRSQGDSIAD 230
Cdd:cd04704    1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTSN 80
                         90
                 ....*....|....*..
gi 157822409 231 IMGVAFFNVLEIPCFVL 247
Cdd:cd04704   81 QVGKIYFNVLQVPCFEL 97
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
152-248 2.51e-45

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


Pssm-ID: 461751  Cd Length: 97  Bit Score: 153.84  E-value: 2.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822409  152 TIPGTLWCGVGNSAENASELGMFHGPDFCCREHDQCPQTISPLQYNYGIRNFRFHTISHCDCDARFQQCLRSQGDSIADI 231
Cdd:pfam05826   1 IYPGTKWCGTGNIAENYDDLGEFDETDRCCREHDHCPDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKNTNSSVSNA 80
                          90
                  ....*....|....*..
gi 157822409  232 MGVAFFNVLEIPCFVLK 248
Cdd:pfam05826  81 VGFIYFNVLQVKCFRLI 97
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
299-424 2.33e-26

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: 102.60  E-value: 2.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822409 299 PSWKRGPQQTPARhhstttvtplqtpaiSSRPDMmIPRgqpgvshpglqdgPKRQGAHRVCRSLRHLDQCEHQIKPQETK 378
Cdd:cd04705    4 TSERRGLEKTGAI---------------ASSPDV-SPF-------------LSEGEFKEPDRCCWKHKQCPGHIIPPFSS 54
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 157822409 379 FHLLNSAQTPLFHCNCTRRLARFLRHHSLPANTNKVWELLGTTCFK 424
Cdd:cd04705   55 DGHHNFHLHSVSHCDCDSRLKDCLRLSSSSRVGPTCSHLLGTTCFN 100
PA2c smart00085
Phospholipase A2;
147-245 9.98e-05

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 41.81  E-value: 9.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822409   147 RRRGWTIPGTLWC--GVGNSAENASELgmfhgpDFCCREHDQCPQTISPLQYNygirnfRFHTISHCDCDARFQQCLrsq 224
Cdd:smart00085  14 GKRAWLSYGDYGCycGWGGSGTPVDAT------DRCCFVHDCCYGKAEKEGCN------PKTTTYSYSCDNGFITCG--- 78
                           90       100
                   ....*....|....*....|.
gi 157822409   225 GDSIADIMGVAFFNVLEIPCF 245
Cdd:smart00085  79 GKNTACLVFVCECDRAAAICF 99
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
358-425 5.47e-04

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


Pssm-ID: 461751  Cd Length: 97  Bit Score: 39.05  E-value: 5.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157822409  358 VCRSLRHLDQCEHQIKPQETKFHLLNSAQTPLFHCNCTRRLARFLRHhslpANTNK-------VWELLGTTCFKL 425
Cdd:pfam05826  26 TDRCCREHDHCPDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKN----TNSSVsnavgfiYFNVLQVKCFRL 96
 
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 ...
151-247 4.31e-50

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: 166.32  E-value: 4.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822409 151 WTIPGTLWCGVGNSAENASELGMFHGPDFCCREHDQCPQTISPLQYNYGIRNFRFHTISHCDCDARFQQCLRSQGDSIAD 230
Cdd:cd04704    1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTSN 80
                         90
                 ....*....|....*..
gi 157822409 231 IMGVAFFNVLEIPCFVL 247
Cdd:cd04704   81 QVGKIYFNVLQVPCFEL 97
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
152-248 2.51e-45

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


Pssm-ID: 461751  Cd Length: 97  Bit Score: 153.84  E-value: 2.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822409  152 TIPGTLWCGVGNSAENASELGMFHGPDFCCREHDQCPQTISPLQYNYGIRNFRFHTISHCDCDARFQQCLRSQGDSIADI 231
Cdd:pfam05826   1 IYPGTKWCGTGNIAENYDDLGEFDETDRCCREHDHCPDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKNTNSSVSNA 80
                          90
                  ....*....|....*..
gi 157822409  232 MGVAFFNVLEIPCFVLK 248
Cdd:pfam05826  81 VGFIYFNVLQVKCFRLI 97
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
299-424 2.33e-26

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: 102.60  E-value: 2.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822409 299 PSWKRGPQQTPARhhstttvtplqtpaiSSRPDMmIPRgqpgvshpglqdgPKRQGAHRVCRSLRHLDQCEHQIKPQETK 378
Cdd:cd04705    4 TSERRGLEKTGAI---------------ASSPDV-SPF-------------LSEGEFKEPDRCCWKHKQCPGHIIPPFSS 54
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 157822409 379 FHLLNSAQTPLFHCNCTRRLARFLRHHSLPANTNKVWELLGTTCFK 424
Cdd:cd04705   55 DGHHNFHLHSVSHCDCDSRLKDCLRLSSSSRVGPTCSHLLGTTCFN 100
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
172-238 5.81e-19

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: 81.80  E-value: 5.81e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157822409 172 GMFHGPDFCCREHDQCPQTISPLQYNYGIRNFRFHTISHCDCDARFQQCLR-----SQGDSIADIMGVAFFN 238
Cdd:cd04705   29 GEFKEPDRCCWKHKQCPGHIIPPFSSDGHHNFHLHSVSHCDCDSRLKDCLRlssssRVGPTCSHLLGTTCFN 100
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
153-223 4.97e-16

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: 72.98  E-value: 4.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822409 153 IPGTLWCGVGNSAENASELGmfHGPDFCCREHDQCPQTISPLQYNYGI-------------RNFRFHTISHCDCDARFQQ 219
Cdd:cd00618    1 LPYGCYCGPGGSACPSGQPV--DETDRCCRKHDCCYDQISDGGCCDGClsysfseggvtclTNSDLCTRSHCDCDRRLAI 78

                 ....
gi 157822409 220 CLRS 223
Cdd:cd00618   79 CLAR 82
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
343-403 3.12e-05

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: 42.55  E-value: 3.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822409 343 HPGLQDGPKRQGAHRVCRSLRHLDQCEHQIKPQETKFHLL-------------NSAQTPLFHCNCTRRLARFLR 403
Cdd:cd00618    8 GPGGSACPSGQPVDETDRCCRKHDCCYDQISDGGCCDGCLsysfseggvtcltNSDLCTRSHCDCDRRLAICLA 81
PA2c smart00085
Phospholipase A2;
147-245 9.98e-05

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 41.81  E-value: 9.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822409   147 RRRGWTIPGTLWC--GVGNSAENASELgmfhgpDFCCREHDQCPQTISPLQYNygirnfRFHTISHCDCDARFQQCLrsq 224
Cdd:smart00085  14 GKRAWLSYGDYGCycGWGGSGTPVDAT------DRCCFVHDCCYGKAEKEGCN------PKTTTYSYSCDNGFITCG--- 78
                           90       100
                   ....*....|....*....|.
gi 157822409   225 GDSIADIMGVAFFNVLEIPCF 245
Cdd:smart00085  79 GKNTACLVFVCECDRAAAICF 99
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
358-425 5.47e-04

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


Pssm-ID: 461751  Cd Length: 97  Bit Score: 39.05  E-value: 5.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157822409  358 VCRSLRHLDQCEHQIKPQETKFHLLNSAQTPLFHCNCTRRLARFLRHhslpANTNK-------VWELLGTTCFKL 425
Cdd:pfam05826  26 TDRCCREHDHCPDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKN----TNSSVsnavgfiYFNVLQVKCFRL 96
 
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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