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Conserved domains on  [gi|1174229946|ref|WP_081451121|]
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phospholipase A2 [Corynebacterium amycolatum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phospholip_A2_3 super family cl29745
Prokaryotic phospholipase A2; The prokaryotic phospholipase A2 domain is predominantly found ...
 32-111 9.74e-10

Prokaryotic phospholipase A2; The prokaryotic phospholipase A2 domain is predominantly found in bacterial and fungal phospholipases, as well as various hypothetical and putative proteins. It enables the liberation of fatty acids and lysophospholipid by hydrolysing the 2-ester bond of 1,2-diacyl-3-sn-phosphoglycerides. The domain adopts an alpha-helical secondary structure, consisting of five alpha-helices and two helical segments.


The actual alignment was detected with superfamily member pfam09056:

Pssm-ID: 453050  Cd Length: 102  Bit Score: 51.84  E-value: 9.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174229946  32 DWCTSSPDQP-GVDFRGPCARHDMCYdANPNAVPTVKSEGKMNCDEEFRSNLYANCnekYATDPDSALDCRRTADGYVFA 110
Cdd:pfam09056  23 DGCSSSPDNPfGFPFLPACQRHDFGY-RNYKAQGRFTEANRKRIDDNFKADLYRQC---ASYSSWKKPACRALADVYYEA 98


                  .
gi 1174229946 111 V 111
Cdd:pfam09056  99 V 99
 
Name Accession Description Interval E-value
Phospholip_A2_3 pfam09056
Prokaryotic phospholipase A2; The prokaryotic phospholipase A2 domain is predominantly found ...
 32-111 9.74e-10

Prokaryotic phospholipase A2; The prokaryotic phospholipase A2 domain is predominantly found in bacterial and fungal phospholipases, as well as various hypothetical and putative proteins. It enables the liberation of fatty acids and lysophospholipid by hydrolysing the 2-ester bond of 1,2-diacyl-3-sn-phosphoglycerides. The domain adopts an alpha-helical secondary structure, consisting of five alpha-helices and two helical segments.


Pssm-ID: 430387  Cd Length: 102  Bit Score: 51.84  E-value: 9.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174229946  32 DWCTSSPDQP-GVDFRGPCARHDMCYdANPNAVPTVKSEGKMNCDEEFRSNLYANCnekYATDPDSALDCRRTADGYVFA 110
Cdd:pfam09056  23 DGCSSSPDNPfGFPFLPACQRHDFGY-RNYKAQGRFTEANRKRIDDNFKADLYRQC---ASYSSWKKPACRALADVYYEA 98


                  .
gi 1174229946 111 V 111
Cdd:pfam09056  99 V 99
 
Name Accession Description Interval E-value
Phospholip_A2_3 pfam09056
Prokaryotic phospholipase A2; The prokaryotic phospholipase A2 domain is predominantly found ...
 32-111 9.74e-10

Prokaryotic phospholipase A2; The prokaryotic phospholipase A2 domain is predominantly found in bacterial and fungal phospholipases, as well as various hypothetical and putative proteins. It enables the liberation of fatty acids and lysophospholipid by hydrolysing the 2-ester bond of 1,2-diacyl-3-sn-phosphoglycerides. The domain adopts an alpha-helical secondary structure, consisting of five alpha-helices and two helical segments.


Pssm-ID: 430387  Cd Length: 102  Bit Score: 51.84  E-value: 9.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174229946  32 DWCTSSPDQP-GVDFRGPCARHDMCYdANPNAVPTVKSEGKMNCDEEFRSNLYANCnekYATDPDSALDCRRTADGYVFA 110
Cdd:pfam09056  23 DGCSSSPDNPfGFPFLPACQRHDFGY-RNYKAQGRFTEANRKRIDDNFKADLYRQC---ASYSSWKKPACRALADVYYEA 98


                  .
gi 1174229946 111 V 111
Cdd:pfam09056  99 V 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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