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Conserved domains on  [gi|665390248|ref|NP_001285008|]
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phospholipase A2 group III, isoform C [Drosophila melanogaster]

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 ...
 84-181 3.48e-51

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: 160.93  E-value: 3.48e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390248  84 LIAPNTRWCGRGNLANGtYNDLGGASKADKCCRKHDHCKMWIDGMSNRYDLFNYRPYTLSHCSCDLRFRTCLKMAGDEDA 163
Cdd:cd04704    1 FIVPGTKWCGPGNIATN-YSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTS 79

                         90
                 ....*....|....*...
gi 665390248 164 NAIGKLFFNVVQTQCFGL 181
Cdd:cd04704   80 NQVGKIYFNVLQVPCFEL 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 ...
 84-181 3.48e-51

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: 160.93  E-value: 3.48e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390248  84 LIAPNTRWCGRGNLANGtYNDLGGASKADKCCRKHDHCKMWIDGMSNRYDLFNYRPYTLSHCSCDLRFRTCLKMAGDEDA 163
Cdd:cd04704    1 FIVPGTKWCGPGNIATN-YSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTS 79

                         90
                 ....*....|....*...
gi 665390248 164 NAIGKLFFNVVQTQCFGL 181
Cdd:cd04704   80 NQVGKIYFNVLQVPCFEL 97
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
 85-182 1.47e-45

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


Pssm-ID: 461751  Cd Length: 97  Bit Score: 146.52  E-value: 1.47e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390248   85 IAPNTRWCGRGNLANgTYNDLGGASKADKCCRKHDHCKMWIDGMSNRYDLFNYRPYTLSHCSCDLRFRTCLKMAGDEDAN 164
Cdd:pfam05826   1 IYPGTKWCGTGNIAE-NYDDLGEFDETDRCCREHDHCPDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKNTNSSVSN 79

                          90
                  ....*....|....*...
gi 665390248  165 AIGKLFFNVVQTQCFGLK 182
Cdd:pfam05826  80 AVGFIYFNVLQVKCFRLI 97
PA2c smart00085
Phospholipase A2;
84-181 1.13e-03

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 37.57  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390248    84 LIAPNTRWCGRGNLANGTYNDlggasKADKCCRKHDHCKmwiDGMSNRYdlfnYRPY-TLSHCSCDLRFRTCLkMAGDED 162
Cdd:smart00085  18 WLSYGDYGCYCGWGGSGTPVD-----ATDRCCFVHDCCY---GKAEKEG----CNPKtTTYSYSCDNGFITCG-GKNTAC 84

                           90
                   ....*....|....*....
gi 665390248   163 ANAIGKlfFNVVQTQCFGL 181
Cdd:smart00085  85 LVFVCE--CDRAAAICFAK 101
 
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 ...
 84-181 3.48e-51

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: 160.93  E-value: 3.48e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390248  84 LIAPNTRWCGRGNLANGtYNDLGGASKADKCCRKHDHCKMWIDGMSNRYDLFNYRPYTLSHCSCDLRFRTCLKMAGDEDA 163
Cdd:cd04704    1 FIVPGTKWCGPGNIATN-YSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTS 79

                         90
                 ....*....|....*...
gi 665390248 164 NAIGKLFFNVVQTQCFGL 181
Cdd:cd04704   80 NQVGKIYFNVLQVPCFEL 97
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
 85-182 1.47e-45

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


Pssm-ID: 461751  Cd Length: 97  Bit Score: 146.52  E-value: 1.47e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390248   85 IAPNTRWCGRGNLANgTYNDLGGASKADKCCRKHDHCKMWIDGMSNRYDLFNYRPYTLSHCSCDLRFRTCLKMAGDEDAN 164
Cdd:pfam05826   1 IYPGTKWCGTGNIAE-NYDDLGEFDETDRCCREHDHCPDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKNTNSSVSN 79

                          90
                  ....*....|....*...
gi 665390248  165 AIGKLFFNVVQTQCFGLK 182
Cdd:pfam05826  80 AVGFIYFNVLQVKCFRLI 97
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 87-158 1.24e-09

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: 53.34  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390248  87 PNTRWCGRGNLAN--GTYNDlggasKADKCCRKHDHCKMWIDGMSNRYD-------------LFNYRPYTLSHCSCDLRF 151
Cdd:cd00618    2 PYGCYCGPGGSACpsGQPVD-----ETDRCCRKHDCCYDQISDGGCCDGclsysfseggvtcLTNSDLCTRSHCDCDRRL 76


                 ....*..
gi 665390248 152 RTCLKMA 158
Cdd:cd00618   77 AICLARA 83
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
 106-179 2.79e-06

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: 44.44  E-value: 2.79e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665390248 106 GGASKADKCCRKHDHCKMWIDGMSNRYDLFNYRPYTLSHCSCDLRFRTCLKmagDEDANAIGKLFFNVVQTQCF 179
Cdd:cd04705   29 GEFKEPDRCCWKHKQCPGHIIPPFSSDGHHNFHLHSVSHCDCDSRLKDCLR---LSSSSRVGPTCSHLLGTTCF 99
PA2c smart00085
Phospholipase A2;
84-181 1.13e-03

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 37.57  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390248    84 LIAPNTRWCGRGNLANGTYNDlggasKADKCCRKHDHCKmwiDGMSNRYdlfnYRPY-TLSHCSCDLRFRTCLkMAGDED 162
Cdd:smart00085  18 WLSYGDYGCYCGWGGSGTPVD-----ATDRCCFVHDCCY---GKAEKEG----CNPKtTTYSYSCDNGFITCG-GKNTAC 84

                           90
                   ....*....|....*....
gi 665390248   163 ANAIGKlfFNVVQTQCFGL 181
Cdd:smart00085  85 LVFVCE--CDRAAAICFAK 101
 
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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