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Conserved domains on  [gi|2056392051|dbj|BCS83980|]
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truncated phosphplipase C, partial [Clostridium perfringens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnPC_S1P1 super family cl16915
Zinc dependent phospholipase C/S1-P1 nuclease; This model describes both the bacterial and ...
 1-52 3.89e-15

Zinc dependent phospholipase C/S1-P1 nuclease; This model describes both the bacterial and archeal zinc-dependent phospholipase C, a domain found in the alpha toxin of Clostridium perfringens, as well as S1/P1 nucleases, which predominantly act on single-stranded DNA and RNA.


The actual alignment was detected with superfamily member smart00770:

Pssm-ID: 450122  Cd Length: 241  Bit Score: 65.51  E-value: 3.89e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2056392051    1 GVSILENDLSKNEPESVrknlEILKENMHELQLGSTYPDYDKNAYDLYQDHF 52
Cdd:smart00770  47 ALEILKNDNNKNEYKLV----EILKKNYKELKLGSTYADYDNKYYDLSQDHF 94
 
Name Accession Description Interval E-value
Zn_dep_PLPC smart00770
Zinc dependent phospholipase C (alpha toxin); This domain conveys a zinc dependent ...
 1-52 3.89e-15

Zinc dependent phospholipase C (alpha toxin); This domain conveys a zinc dependent phospholipase C activity (EC 3.1.4.3). It is found in a monomeric phospholipase C of Bacillus cereus as well as in the alpha toxin of Clostridium perfringens and Clostridium bifermentans, which is involved in haemolysis and cell rupture. It is also found in a lecithinase of Listeria monocytogenes, which is involved in breaking the 2-membrane vacuoles that surround the bacterium. Structure information: PDB 1ca1.


Pssm-ID: 214813  Cd Length: 241  Bit Score: 65.51  E-value: 3.89e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2056392051    1 GVSILENDLSKNEPESVrknlEILKENMHELQLGSTYPDYDKNAYDLYQDHF 52
Cdd:smart00770  47 ALEILKNDNNKNEYKLV----EILKKNYKELKLGSTYADYDNKYYDLSQDHF 94
ZnPC_S1P1 cd10981
Zinc dependent phospholipase C/S1-P1 nuclease; This model describes both the bacterial and ...
 1-52 3.88e-07

Zinc dependent phospholipase C/S1-P1 nuclease; This model describes both the bacterial and archeal zinc-dependent phospholipase C, a domain found in the alpha toxin of Clostridium perfringens, as well as S1/P1 nucleases, which predominantly act on single-stranded DNA and RNA.


Pssm-ID: 211380  Cd Length: 238  Bit Score: 43.97  E-value: 3.88e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2056392051   1 GVSILENDLSKNEPEsvrknleILKENMHELQLGSTYPDYDKNAYD-LYQDHF 52
Cdd:cd10981    12 AVFTLPPELAEFWSD-------LLKRNIDELLEGAVAPDKRRYDDDgEAQNHV 57
 
Name Accession Description Interval E-value
Zn_dep_PLPC smart00770
Zinc dependent phospholipase C (alpha toxin); This domain conveys a zinc dependent ...
 1-52 3.89e-15

Zinc dependent phospholipase C (alpha toxin); This domain conveys a zinc dependent phospholipase C activity (EC 3.1.4.3). It is found in a monomeric phospholipase C of Bacillus cereus as well as in the alpha toxin of Clostridium perfringens and Clostridium bifermentans, which is involved in haemolysis and cell rupture. It is also found in a lecithinase of Listeria monocytogenes, which is involved in breaking the 2-membrane vacuoles that surround the bacterium. Structure information: PDB 1ca1.


Pssm-ID: 214813  Cd Length: 241  Bit Score: 65.51  E-value: 3.89e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2056392051    1 GVSILENDLSKNEPESVrknlEILKENMHELQLGSTYPDYDKNAYDLYQDHF 52
Cdd:smart00770  47 ALEILKNDNNKNEYKLV----EILKKNYKELKLGSTYADYDNKYYDLSQDHF 94
ZnPC_S1P1 cd10981
Zinc dependent phospholipase C/S1-P1 nuclease; This model describes both the bacterial and ...
 1-52 3.88e-07

Zinc dependent phospholipase C/S1-P1 nuclease; This model describes both the bacterial and archeal zinc-dependent phospholipase C, a domain found in the alpha toxin of Clostridium perfringens, as well as S1/P1 nucleases, which predominantly act on single-stranded DNA and RNA.


Pssm-ID: 211380  Cd Length: 238  Bit Score: 43.97  E-value: 3.88e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2056392051   1 GVSILENDLSKNEPEsvrknleILKENMHELQLGSTYPDYDKNAYD-LYQDHF 52
Cdd:cd10981    12 AVFTLPPELAEFWSD-------LLKRNIDELLEGAVAPDKRRYDDDgEAQNHV 57
Zn_dep_PLPC cd11009
Zinc dependent phospholipase C (alpha toxin); This domain conveys a zinc dependent ...
 1-52 7.39e-05

Zinc dependent phospholipase C (alpha toxin); This domain conveys a zinc dependent phospholipase C activity (EC 3.1.4.3). It is found in a monomeric phospholipase C of Bacillus cereus as well as in the alpha toxin of Clostridium perfringens and Clostridium bifermentans, which is involved in haemolysis and cell rupture. It is also found in a lecithinase of Listeria monocytogenes, which is involved in breaking the 2-membrane vacuoles that surround the bacterium.


Pssm-ID: 211381  Cd Length: 218  Bit Score: 37.36  E-value: 7.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2056392051   1 GVSILENDLsknepesVRKNLEILKENMHELQLGSTYPDYDKNAYDLYQDHF 52
Cdd:cd11009    19 AIKILGNDG-------KAEAYQFLKKYLYGLNQGLYWADQDWKSGDQYVNHF 63
 
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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