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Conserved domains on  [gi|52854790|gb|AAU88268|]
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cytolethal distending toxin A [Escherichia albertii]

Protein Classification

cytolethal distending toxin subunit A/C( domain architecture ID 10507426)

cytolethal distending toxin subunits A and C are components of cytolethal distending toxin (CDT), which is cytotoxin that induces host cell distension, growth arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in HeLa cells

Gene Ontology:  GO:0030246|GO:0090729
PubMed:  8844840|35536958
SCOP:  3000678

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_Ricin_CdtA cd23414
ricin B-type lectin domain, beta-trefoil fold, found in cytolethal distending toxin subunit A ...
 73-229 2.19e-60

ricin B-type lectin domain, beta-trefoil fold, found in cytolethal distending toxin subunit A (CdtA) and similar proteins; Cytolethal distending toxins (CDTs) are cytotoxins which induce host cell distension, growth arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in HeLa cells. CDT is a heterotrimer consisting of the three subunits, CdtA, CdtB, and CdtC. CdtA, along with CdtC, probably forms a heterodimeric subunit required for the delivery of nuclease CdtB. CdtA contains a ricin B-type lectin domain with 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. Each subdomain may harbor a sugar-binding pocket.


:

Pssm-ID: 469576  Cd Length: 147  Bit Score: 187.49  E-value: 2.19e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52854790  73 VPGTAPAVSLMNMDGSVLTMWSRGAGSSLWAYYISDSNSFGELRNWQIMPGTrPNTIQFRNVDVGTCMTSfpgFKGGVll 152
Cdd:cd23414   1 SPDTSDFVSIMNIGGALLTVWALAPGNWLWGYTPYDSGSFGNARNWQIIYNP-DGTVSFRNVYTGTCLTA---YGNGV-- 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52854790 153 STAPCQFGPQRFDFQPMATRNGNYQLKSLSTGLCIRANFLGRTpsspYATTLTMERCPSSGERNFEFMWSISEPLRP 229
Cdd:cd23414  75 IHNPCDSNNPAQKFELIPTDNGAVQIKNVSTGKCLQTPFGSRT----YAYSIYLTKCPTPGEVNLDQQWYIIPPLID 147
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_CdtA cd23414
ricin B-type lectin domain, beta-trefoil fold, found in cytolethal distending toxin subunit A ...
 73-229 2.19e-60

ricin B-type lectin domain, beta-trefoil fold, found in cytolethal distending toxin subunit A (CdtA) and similar proteins; Cytolethal distending toxins (CDTs) are cytotoxins which induce host cell distension, growth arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in HeLa cells. CDT is a heterotrimer consisting of the three subunits, CdtA, CdtB, and CdtC. CdtA, along with CdtC, probably forms a heterodimeric subunit required for the delivery of nuclease CdtB. CdtA contains a ricin B-type lectin domain with 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. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 469576  Cd Length: 147  Bit Score: 187.49  E-value: 2.19e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52854790  73 VPGTAPAVSLMNMDGSVLTMWSRGAGSSLWAYYISDSNSFGELRNWQIMPGTrPNTIQFRNVDVGTCMTSfpgFKGGVll 152
Cdd:cd23414   1 SPDTSDFVSIMNIGGALLTVWALAPGNWLWGYTPYDSGSFGNARNWQIIYNP-DGTVSFRNVYTGTCLTA---YGNGV-- 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52854790 153 STAPCQFGPQRFDFQPMATRNGNYQLKSLSTGLCIRANFLGRTpsspYATTLTMERCPSSGERNFEFMWSISEPLRP 229
Cdd:cd23414  75 IHNPCDSNNPAQKFELIPTDNGAVQIKNVSTGKCLQTPFGSRT----YAYSIYLTKCPTPGEVNLDQQWYIIPPLID 147
CDtoxinA pfam03498
Cytolethal distending toxin A/C domain;
79-232 6.00e-53

Cytolethal distending toxin A/C domain;


Pssm-ID: 397529  Cd Length: 149  Bit Score: 168.81  E-value: 6.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52854790    79 AVSLMN-MDGSVLTMWSRGAGSSL---WAYYISDSNSFGELRNwQIMPGTRPNTIQFRNVDVGTCMTSFpgfKGGVLLST 154
Cdd:pfam03498   1 LVSIRSlLTGALLTNWALDSRNWLstnWGYTPIDSNEFGLLRD-KIMDGKNGGTVQFKNPDTGTCLAAY---GNGVIHLK 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52854790   155 ApCQFGPQRFDFQPMATRNGNYQLKSLSTGLCIRANFLGRTpsspYATTLTMERCPSSGERNFEFMWSISEPLRPALA 232
Cdd:pfam03498  77 A-CDDDDLATLFSLIPTTTGAVQIKSLSSGLCITANFNSTT----FAFTITLEKCDLATTVNLDQLWMITPPLKTASP 149
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_CdtA cd23414
ricin B-type lectin domain, beta-trefoil fold, found in cytolethal distending toxin subunit A ...
 73-229 2.19e-60

ricin B-type lectin domain, beta-trefoil fold, found in cytolethal distending toxin subunit A (CdtA) and similar proteins; Cytolethal distending toxins (CDTs) are cytotoxins which induce host cell distension, growth arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in HeLa cells. CDT is a heterotrimer consisting of the three subunits, CdtA, CdtB, and CdtC. CdtA, along with CdtC, probably forms a heterodimeric subunit required for the delivery of nuclease CdtB. CdtA contains a ricin B-type lectin domain with 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. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 469576  Cd Length: 147  Bit Score: 187.49  E-value: 2.19e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52854790  73 VPGTAPAVSLMNMDGSVLTMWSRGAGSSLWAYYISDSNSFGELRNWQIMPGTrPNTIQFRNVDVGTCMTSfpgFKGGVll 152
Cdd:cd23414   1 SPDTSDFVSIMNIGGALLTVWALAPGNWLWGYTPYDSGSFGNARNWQIIYNP-DGTVSFRNVYTGTCLTA---YGNGV-- 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52854790 153 STAPCQFGPQRFDFQPMATRNGNYQLKSLSTGLCIRANFLGRTpsspYATTLTMERCPSSGERNFEFMWSISEPLRP 229
Cdd:cd23414  75 IHNPCDSNNPAQKFELIPTDNGAVQIKNVSTGKCLQTPFGSRT----YAYSIYLTKCPTPGEVNLDQQWYIIPPLID 147
CDtoxinA pfam03498
Cytolethal distending toxin A/C domain;
79-232 6.00e-53

Cytolethal distending toxin A/C domain;


Pssm-ID: 397529  Cd Length: 149  Bit Score: 168.81  E-value: 6.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52854790    79 AVSLMN-MDGSVLTMWSRGAGSSL---WAYYISDSNSFGELRNwQIMPGTRPNTIQFRNVDVGTCMTSFpgfKGGVLLST 154
Cdd:pfam03498   1 LVSIRSlLTGALLTNWALDSRNWLstnWGYTPIDSNEFGLLRD-KIMDGKNGGTVQFKNPDTGTCLAAY---GNGVIHLK 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52854790   155 ApCQFGPQRFDFQPMATRNGNYQLKSLSTGLCIRANFLGRTpsspYATTLTMERCPSSGERNFEFMWSISEPLRPALA 232
Cdd:pfam03498  77 A-CDDDDLATLFSLIPTTTGAVQIKSLSSGLCITANFNSTT----FAFTITLEKCDLATTVNLDQLWMITPPLKTASP 149
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 128-209 1.34e-05

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with 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. Each subdomain contains a sugar-binding pocket.


Pssm-ID: 467294 [Multi-domain]  Cd Length: 120  Bit Score: 43.58  E-value: 1.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52854790 128 TIQFRNVDVGTCMTSfpGFKGGVllSTAPCQFGP-QRFDFQPmaTRNGNYQLKSLSTGLCIRANflgrtpsspYATTLTM 206
Cdd:cd23415   2 TVRLRNVATGRCLDS--NAGGNV--YTGPCNGGPyQRWTWSG--VGDGTVTLRNAATGRCLDSN---------GNGGVYT 66


                ...
gi 52854790 207 ERC 209
Cdd:cd23415  67 LPC 69
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 108-194 3.02e-05

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with 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. Each subdomain contains a sugar-binding pocket.


Pssm-ID: 467294 [Multi-domain]  Cd Length: 120  Bit Score: 42.42  E-value: 3.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52854790 108 DSNSFGELR-------NWQ--IMPGTRPNTIQFRNVDVGTCMTSfpgfKGGVLLSTAPCQFGP-QRFDFQPmaTRNGNYQ 177
Cdd:cd23415  15 DSNAGGNVYtgpcnggPYQrwTWSGVGDGTVTLRNAATGRCLDS----NGNGGVYTLPCNGGSyQRWRVTS--TSGGGVT 88

                        90
                ....*....|....*..
gi 52854790 178 LKSLSTGLCIRANFLGR 194
Cdd:cd23415  89 LRNVATGRCLDSNGSGG 105
beta-trefoil_Ricin_CdtAC cd23387
ricin B-type lectin domain, beta-trefoil fold, found in cytolethal distending toxin subunit A ...
 77-226 1.17e-04

ricin B-type lectin domain, beta-trefoil fold, found in cytolethal distending toxin subunit A (CdtA), subunit C (CdtC), and similar proteins; Cytolethal distending toxins (CDTs) are cytotoxins which induce host cell distension, growth arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in HeLa cells. CDT is a heterotrimer consisting of the three subunits, CdtA, CdtB, and CdtC. CdtA, along with CdtC, probably forms a heterodimeric subunit required for the delivery of nuclease CdtB. Both CdtA and CdtC contain a ricin B-type lectin domain with 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. Each subdomain may harbor a sugar-binding pocket. The third beta strand is missing in CdtC.


Pssm-ID: 469574  Cd Length: 133  Bit Score: 40.89  E-value: 1.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52854790  77 APAVSLMN-MDGSVLTMWsrgagsslwaYYISDsnsFGELRNWQIMPGTRPNT---------IQFRNVDVGTCMtSFPGf 146
Cdd:cd23387   1 PPRISLRSlLTAQPLKND----------HYDSH---NYLSTHWELIDYKGKEYeklrdggtlVQFKVVGAAKCF-AFNG- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52854790 147 kggvlLSTAPCQF-GPQRFDFQPmaTRNGNYQLKSLSTGLCIRANflgrtpssPYaTTLTMERC---PSSGERNFEFMWS 222
Cdd:cd23387  66 -----LGTTDCKDkDHTVFNLIP--TNTGAFLIKDALLGFCVTSH--------DF-DDLTLEPCggsVSGRTFSLAYQWG 129


                ....
gi 52854790 223 ISEP 226
Cdd:cd23387 130 ILPP 133
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 118-187 1.10e-03

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold 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 ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 38.12  E-value: 1.10e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52854790 118 WQIMPgTRPNTIQFRNVDVGTCMTSFPGFKG-GVLLSTAPCQFGP-QRFDFQPmaTRNGNYQLKSLSTGLCI 187
Cdd:cd00161  40 WTLTP-VGDGYYTIRNVASGKCLDVAGGSTAnGANVQQWTCNGGDnQQWRLEP--VGDGYYRIVNKHSGKCL 108
 
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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