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Conserved domains on  [gi|1992433839|ref|XP_039526793|]
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uncharacterized protein proca1 [Pimephales promelas]

Protein Classification

Phospholip_A2_2 domain-containing protein( domain architecture ID 10140433)

Phospholip_A2_2 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 ...
 192-288 1.51e-57

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: 190.98  E-value: 1.51e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992433839 192 FTYPGTLWCGAGNIADHYEQLGEFEETDKCCRVHDHCPYIIHAFSSNYGYTNFKWHSLSHCDCDNALKECLRLVNDTSSR 271
Cdd:cd04704     1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTSN 80

                          90
                  ....*....|....*..
gi 1992433839 272 VVGQAFFNVIEAPCFEF 288
Cdd:cd04704    81 QVGKIYFNVLQVPCFEL 97
 
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 ...
 192-288 1.51e-57

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: 190.98  E-value: 1.51e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992433839 192 FTYPGTLWCGAGNIADHYEQLGEFEETDKCCRVHDHCPYIIHAFSSNYGYTNFKWHSLSHCDCDNALKECLRLVNDTSSR 271
Cdd:cd04704     1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTSN 80

                          90
                  ....*....|....*..
gi 1992433839 272 VVGQAFFNVIEAPCFEF 288
Cdd:cd04704    81 QVGKIYFNVLQVPCFEL 97
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
 193-288 5.87e-49

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


Pssm-ID: 461751  Cd Length: 97  Bit Score: 167.32  E-value: 5.87e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992433839 193 TYPGTLWCGAGNIADHYEQLGEFEETDKCCRVHDHCPYIIHAFSSNYGYTNFKWHSLSHCDCDNALKECLRLVNDTSSRV 272
Cdd:pfam05826   1 IYPGTKWCGTGNIAENYDDLGEFDETDRCCREHDHCPDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKNTNSSVSNA 80

                          90
                  ....*....|....*.
gi 1992433839 273 VGQAFFNVIEAPCFEF 288
Cdd:pfam05826  81 VGFIYFNVLQVKCFRL 96
PA2c smart00085
Phospholipase A2;
184-287 2.48e-10

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 58.37  E-value: 2.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992433839  184 KKTRTKRGFTYPGTLWCGAGNiadhyeqlGE----FEETDKCCRVHDHCpyiihafssnYG-----YTNFKWhSLSHCDC 254
Cdd:smart00085  10 QCATGKRAWLSYGDYGCYCGW--------GGsgtpVDATDRCCFVHDCC----------YGkaekeGCNPKT-TTYSYSC 70

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1992433839  255 DNALKECLRlvNDTSSRvVGQAFFNVIEAPCFE 287
Cdd:smart00085  71 DNGFITCGG--KNTACL-VFVCECDRAAAICFA 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 ...
 192-288 1.51e-57

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: 190.98  E-value: 1.51e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992433839 192 FTYPGTLWCGAGNIADHYEQLGEFEETDKCCRVHDHCPYIIHAFSSNYGYTNFKWHSLSHCDCDNALKECLRLVNDTSSR 271
Cdd:cd04704     1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTSN 80

                          90
                  ....*....|....*..
gi 1992433839 272 VVGQAFFNVIEAPCFEF 288
Cdd:cd04704    81 QVGKIYFNVLQVPCFEL 97
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
 193-288 5.87e-49

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


Pssm-ID: 461751  Cd Length: 97  Bit Score: 167.32  E-value: 5.87e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992433839 193 TYPGTLWCGAGNIADHYEQLGEFEETDKCCRVHDHCPYIIHAFSSNYGYTNFKWHSLSHCDCDNALKECLRLVNDTSSRV 272
Cdd:pfam05826   1 IYPGTKWCGTGNIAENYDDLGEFDETDRCCREHDHCPDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKNTNSSVSNA 80

                          90
                  ....*....|....*.
gi 1992433839 273 VGQAFFNVIEAPCFEF 288
Cdd:pfam05826  81 VGFIYFNVLQVKCFRL 96
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
 213-279 3.47e-22

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: 91.82  E-value: 3.47e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1992433839 213 GEFEETDKCCRVHDHCP-YIIHAFSsNYGYTNFKWHSLSHCDCDNALKECLRLVND-----TSSRVVGQAFFN 279
Cdd:cd04705    29 GEFKEPDRCCWKHKQCPgHIIPPFS-SDGHHNFHLHSVSHCDCDSRLKDCLRLSSSsrvgpTCSHLLGTTCFN 100
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 195-265 4.10e-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: 88.01  E-value: 4.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992433839 195 PGTLWCGAGNIADHYEQLGEfeETDKCCRVHDHCPYIIHAFSSNYG-------------YTNFKWHSLSHCDCDNALKEC 261
Cdd:cd00618     2 PYGCYCGPGGSACPSGQPVD--ETDRCCRKHDCCYDQISDGGCCDGclsysfseggvtcLTNSDLCTRSHCDCDRRLAIC 79


                  ....
gi 1992433839 262 LRLV 265
Cdd:cd00618    80 LARA 83
PA2c smart00085
Phospholipase A2;
184-287 2.48e-10

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 58.37  E-value: 2.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992433839  184 KKTRTKRGFTYPGTLWCGAGNiadhyeqlGE----FEETDKCCRVHDHCpyiihafssnYG-----YTNFKWhSLSHCDC 254
Cdd:smart00085  10 QCATGKRAWLSYGDYGCYCGW--------GGsgtpVDATDRCCFVHDCC----------YGkaekeGCNPKT-TTYSYSC 70

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1992433839  255 DNALKECLRlvNDTSSRvVGQAFFNVIEAPCFE 287
Cdd:smart00085  71 DNGFITCGG--KNTACL-VFVCECDRAAAICFA 100
PLA2c cd00125
PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca ...
 199-263 8.11e-04

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: 39.93  E-value: 8.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992433839 199 WCGAGN---IADhyeqlgefeETDKCCRVHDHC----------PYIIHafssnYGYT-----------NFKWHSLShCDC 254
Cdd:cd00125    26 YCGLGGsgtPVD---------DTDRCCQVHDCCydraekggcsPYFTS-----YSYTcsdgqitcsdaNDKCARAL-CEC 90


                  ....*....
gi 1992433839 255 DNALKECLR 263
Cdd:cd00125    91 DRAAALCFA 99
PLA2_plant cd04706
PLA2_plant: Plant-specific sub-family of Phospholipase A2, a super-family of secretory and ...
 219-272 1.16e-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: 39.34  E-value: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1992433839 219 DKCCRVHDHCpYIIHafssNYGYTnfkwhslsHCDCDNALKECLRLVNDTSSRV 272
Cdd:cd04706    45 DACCMTHDAC-VQAK----KNDYL--------SLECNEKFKNCVRRFRKARKPT 85
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 217-263 8.57e-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: 36.82  E-value: 8.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1992433839 217 ETDKCCRVHDHC-----------PYIIHafssnYGYT---------NFKWHSLSHCDCDNALKECLR 263
Cdd:pfam00068  38 ATDRCCQAHDCCyerlkklgcgnPYLLS-----YNYScsdgtitcsGNSSCEKQLCECDKAAAECFA 99
 
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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