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Conserved domains on  [gi|446647848|ref|WP_000725194|]
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MULTISPECIES: zinc dependent phospholipase C family protein [Bacillus]

Protein Classification

phospholipase C; zinc dependent phospholipase C family protein( domain architecture ID 10181125)

phospholipase C catayzes the hydroysis of a phosphatidylcholine to form 1,2-diacyl-sn-glycerol and phosphocholine| zinc dependent phospholipase C (PLC) family protein similar to the N-terminal domain PLC domain found in Clostridium perfringens alpha-toxin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Zn_dep_PLPC cd11009
Zinc dependent phospholipase C (alpha toxin); This domain conveys a zinc dependent ...
50-291 9.06e-53

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: 176.80  E-value: 9.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848  50 YHSDKSTHLWIAKQAIEIMKTESNIEAnkqaVDFLNypQYKDLFSKGLYDADYNAEFNDGgtgiggvfkggWKSHFYDPD 129
Cdd:cd11009    5 KITECSTHKFITYQAIKILGNDGKAEA----YQFLK--KYLYGLNQGLYWADQDWKSGDQ-----------YVNHFYDPD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848 130 TKEnyRGETNPTALTQGKKYFYESGEHLRNKDYEKAFYYLGVATHYFTDATQPMHAANFTAIDTraiKYHSYFENYVTTI 209
Cdd:cd11009   68 TGK--GLYGFPTALTEFRKYYDLALEYWRKGDYEKAMFYLGRALHYLQDLTVPHHAANATAVAL---NGHSAYENYVEDH 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848 210 QNQFAVNTGGNYNNS---LSTPEEWIDYVARVAKPEIQNITNDKTfkyynsgkaqLWQEMVTPAVQRSLGEAQRNTAGFL 286
Cdd:cd11009  143 KDDYKLNTAGIYANKpylSDSPEEYIKENAKYAKKYYPKIYNEKK----------GSEEAYDRAAGELLPEAQRTTAGFL 212

                 ....*
gi 446647848 287 NLWFK 291
Cdd:cd11009  213 LKFLK 217
beta-trefoil_STI super family cl11466
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold; The STI-like domain is found ...
307-363 5.11e-04

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold; The STI-like domain is found in the soybean trypsin inhibitor (Kunitz) family of protease inhibitors. They inhibit proteases by binding with high affinity to their active sites. Plant Kunitz-type inhibitors are thought to be important in defense, especially against insect pests. The STI-like domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


The actual alignment was detected with superfamily member pfam00197:

Pssm-ID: 472192  Cd Length: 174  Bit Score: 40.75  E-value: 5.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446647848  307 IYDIEGNVIEAGKNYYIVPSESPY--QGLTfewyLANRYD-----YVTLANKENNAlfGTPIEF 363
Cdd:pfam00197   1 VLDTDGNPLRAGVEYYILPAIGGGsgGGLT----LASRGNgtcplDVVQEPSEVSK--GLPVKF 58
 
Name Accession Description Interval E-value
Zn_dep_PLPC cd11009
Zinc dependent phospholipase C (alpha toxin); This domain conveys a zinc dependent ...
50-291 9.06e-53

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: 176.80  E-value: 9.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848  50 YHSDKSTHLWIAKQAIEIMKTESNIEAnkqaVDFLNypQYKDLFSKGLYDADYNAEFNDGgtgiggvfkggWKSHFYDPD 129
Cdd:cd11009    5 KITECSTHKFITYQAIKILGNDGKAEA----YQFLK--KYLYGLNQGLYWADQDWKSGDQ-----------YVNHFYDPD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848 130 TKEnyRGETNPTALTQGKKYFYESGEHLRNKDYEKAFYYLGVATHYFTDATQPMHAANFTAIDTraiKYHSYFENYVTTI 209
Cdd:cd11009   68 TGK--GLYGFPTALTEFRKYYDLALEYWRKGDYEKAMFYLGRALHYLQDLTVPHHAANATAVAL---NGHSAYENYVEDH 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848 210 QNQFAVNTGGNYNNS---LSTPEEWIDYVARVAKPEIQNITNDKTfkyynsgkaqLWQEMVTPAVQRSLGEAQRNTAGFL 286
Cdd:cd11009  143 KDDYKLNTAGIYANKpylSDSPEEYIKENAKYAKKYYPKIYNEKK----------GSEEAYDRAAGELLPEAQRTTAGFL 212

                 ....*
gi 446647848 287 NLWFK 291
Cdd:cd11009  213 LKFLK 217
Zn_dep_PLPC smart00770
Zinc dependent phospholipase C (alpha toxin); This domain conveys a zinc dependent ...
39-292 1.51e-38

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: 139.86  E-value: 1.51e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848    39 PITARWSAEAPYHSDKSTHLWIAKQAIEIMKtESNIEANKQAVDFLNypQYKDLFSKGLYDADYNAEFNDGgtgiggvfk 118
Cdd:smart00770  22 PTKKSPSWDGKLDGTCNTHLFIVNQALEILK-NDNNKNEYKLVEILK--KNYKELKLGSTYADYDNKYYDL--------- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848   119 ggWKSHFYDPDTKENYrGETNPTALTQGKKYFYESGEHLRNKDYEKAFYYLGVATHYFTDATQPMHAANFTAIDTRAiky 198
Cdd:smart00770  90 --SQDHFYDPDTGKNY-LPGFSNAKDTGRKYFKLALNEWKKGNYKKAFFYLGRACHYLGDLSTPYHANNVTAVDSPG--- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848   199 HSYFENYVTTIQNQFAVNTGGNYnnslstpeewidyvarvakpEIQNITNDKTFKYYNSG-KAQLWQEMVTPAVQRSLGE 277
Cdd:smart00770 164 HRKFENFVQTRKDNYSLNTEGEK--------------------KFLENVNKKAKKLYYSHaTMSKSEKDWDYAAGEALKN 223
                          250
                   ....*....|....*
gi 446647848   278 AQRNTAGFLNLWFKT 292
Cdd:smart00770 224 AQKTTAGFLYRFYNE 238
Zn_dep_PLPC pfam00882
Zinc dependent phospholipase C;
56-238 1.28e-06

Zinc dependent phospholipase C;


Pssm-ID: 425927  Cd Length: 173  Bit Score: 48.49  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848   56 THLWIAKQAIEIMKtesnieanKQAVDFLNYPQYKDLFSKGLYDADYnaefndggtgiggVFKGGWKSHFYDPDTkenyr 135
Cdd:pfam00882   1 THLTIASHALAVLP--------LLKKARKLLKLNKAALLLGSVAPDI-------------PYLFGFLPYSYLTHT----- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848  136 getnpTALTQGKKYFYESGEHLRNK---DYEKAFYYLGVATHYFTDATqpMHAANFTAIDTRAIKY----HSYFENYVTT 208
Cdd:pfam00882  55 -----HHWWETGDFILLLIKALRKRkkgNLKLAAFLLGVLSHYLADVF--THSYGVPLAGNGTFSGsllqHVSYELGLDF 127
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 446647848  209 IQ-----NQFAVNTGGNYNNSLSTPEEWIDYVARV 238
Cdd:pfam00882 128 LLlnyyrLEKEVDLLLLSVGDKDSNEALDELIKET 162
Kunitz_legume pfam00197
Trypsin and protease inhibitor;
307-363 5.11e-04

Trypsin and protease inhibitor;


Pssm-ID: 395144  Cd Length: 174  Bit Score: 40.75  E-value: 5.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446647848  307 IYDIEGNVIEAGKNYYIVPSESPY--QGLTfewyLANRYD-----YVTLANKENNAlfGTPIEF 363
Cdd:pfam00197   1 VLDTDGNPLRAGVEYYILPAIGGGsgGGLT----LASRGNgtcplDVVQEPSEVSK--GLPVKF 58
 
Name Accession Description Interval E-value
Zn_dep_PLPC cd11009
Zinc dependent phospholipase C (alpha toxin); This domain conveys a zinc dependent ...
50-291 9.06e-53

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: 176.80  E-value: 9.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848  50 YHSDKSTHLWIAKQAIEIMKTESNIEAnkqaVDFLNypQYKDLFSKGLYDADYNAEFNDGgtgiggvfkggWKSHFYDPD 129
Cdd:cd11009    5 KITECSTHKFITYQAIKILGNDGKAEA----YQFLK--KYLYGLNQGLYWADQDWKSGDQ-----------YVNHFYDPD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848 130 TKEnyRGETNPTALTQGKKYFYESGEHLRNKDYEKAFYYLGVATHYFTDATQPMHAANFTAIDTraiKYHSYFENYVTTI 209
Cdd:cd11009   68 TGK--GLYGFPTALTEFRKYYDLALEYWRKGDYEKAMFYLGRALHYLQDLTVPHHAANATAVAL---NGHSAYENYVEDH 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848 210 QNQFAVNTGGNYNNS---LSTPEEWIDYVARVAKPEIQNITNDKTfkyynsgkaqLWQEMVTPAVQRSLGEAQRNTAGFL 286
Cdd:cd11009  143 KDDYKLNTAGIYANKpylSDSPEEYIKENAKYAKKYYPKIYNEKK----------GSEEAYDRAAGELLPEAQRTTAGFL 212

                 ....*
gi 446647848 287 NLWFK 291
Cdd:cd11009  213 LKFLK 217
Zn_dep_PLPC smart00770
Zinc dependent phospholipase C (alpha toxin); This domain conveys a zinc dependent ...
39-292 1.51e-38

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: 139.86  E-value: 1.51e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848    39 PITARWSAEAPYHSDKSTHLWIAKQAIEIMKtESNIEANKQAVDFLNypQYKDLFSKGLYDADYNAEFNDGgtgiggvfk 118
Cdd:smart00770  22 PTKKSPSWDGKLDGTCNTHLFIVNQALEILK-NDNNKNEYKLVEILK--KNYKELKLGSTYADYDNKYYDL--------- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848   119 ggWKSHFYDPDTKENYrGETNPTALTQGKKYFYESGEHLRNKDYEKAFYYLGVATHYFTDATQPMHAANFTAIDTRAiky 198
Cdd:smart00770  90 --SQDHFYDPDTGKNY-LPGFSNAKDTGRKYFKLALNEWKKGNYKKAFFYLGRACHYLGDLSTPYHANNVTAVDSPG--- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848   199 HSYFENYVTTIQNQFAVNTGGNYnnslstpeewidyvarvakpEIQNITNDKTFKYYNSG-KAQLWQEMVTPAVQRSLGE 277
Cdd:smart00770 164 HRKFENFVQTRKDNYSLNTEGEK--------------------KFLENVNKKAKKLYYSHaTMSKSEKDWDYAAGEALKN 223
                          250
                   ....*....|....*
gi 446647848   278 AQRNTAGFLNLWFKT 292
Cdd:smart00770 224 AQKTTAGFLYRFYNE 238
ZnPC_S1P1 cd10981
Zinc dependent phospholipase C/S1-P1 nuclease; This model describes both the bacterial and ...
54-287 1.62e-09

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: 58.22  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848  54 KSTHLWIAKQAIEIMKTESNIEANKQAVdflnypQYKDLFSKGLYDADYnaEFNDggtgiggvFKGGWKSHFYDPDT--- 130
Cdd:cd10981    2 FGTHHKIARDAVFTLPPELAEFWSDLLK------RNIDELLEGAVAPDK--RRYD--------DDGEAQNHVLDVDDygd 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848 131 --KENYRGET---NPTALTQGKKYFYESGEHLRNKDYEKAFYYLGVATHYFTDATQPMH-AANFTAIDTRAIKYHSYFEN 204
Cdd:cd10981   66 saLDKYGEDTlgyWGGAPWQIQEWYQRLVDAFRRKDWKDIAFAAGVLSHYIGDAHVPLHtTQNYNGQLTGQDGIHRAWET 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848 205 YVTTIQNQFAVNTGGNYNNSLSTPeEWIDYVARVAKPEIQ--NITNDKTFKYYNSGKAQ-------LWQEMVTpAVQRSL 275
Cdd:cd10981  146 RIPELYAELYALTDAFGDPFVGKA-DYIKWPKEYIWDAAKhaNALYDTVLSHEKELAGSrkypyegRNDVVRK-TYSEAL 223
                        250
                 ....*....|..
gi 446647848 276 GEAQRNTAGFLN 287
Cdd:cd10981  224 AKAYHGLANGLV 235
Zn_dep_PLPC pfam00882
Zinc dependent phospholipase C;
56-238 1.28e-06

Zinc dependent phospholipase C;


Pssm-ID: 425927  Cd Length: 173  Bit Score: 48.49  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848   56 THLWIAKQAIEIMKtesnieanKQAVDFLNYPQYKDLFSKGLYDADYnaefndggtgiggVFKGGWKSHFYDPDTkenyr 135
Cdd:pfam00882   1 THLTIASHALAVLP--------LLKKARKLLKLNKAALLLGSVAPDI-------------PYLFGFLPYSYLTHT----- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446647848  136 getnpTALTQGKKYFYESGEHLRNK---DYEKAFYYLGVATHYFTDATqpMHAANFTAIDTRAIKY----HSYFENYVTT 208
Cdd:pfam00882  55 -----HHWWETGDFILLLIKALRKRkkgNLKLAAFLLGVLSHYLADVF--THSYGVPLAGNGTFSGsllqHVSYELGLDF 127
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 446647848  209 IQ-----NQFAVNTGGNYNNSLSTPEEWIDYVARV 238
Cdd:pfam00882 128 LLlnyyrLEKEVDLLLLSVGDKDSNEALDELIKET 162
Kunitz_legume pfam00197
Trypsin and protease inhibitor;
307-363 5.11e-04

Trypsin and protease inhibitor;


Pssm-ID: 395144  Cd Length: 174  Bit Score: 40.75  E-value: 5.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446647848  307 IYDIEGNVIEAGKNYYIVPSESPY--QGLTfewyLANRYD-----YVTLANKENNAlfGTPIEF 363
Cdd:pfam00197   1 VLDTDGNPLRAGVEYYILPAIGGGsgGGLT----LASRGNgtcplDVVQEPSEVSK--GLPVKF 58
 
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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