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Conserved domains on  [gi|929048877|gb|ALF04647|]
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epsilon toxin, partial [Clostridium perfringens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ETX_MTX2 super family cl03107
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ...
 1-140 1.30e-27

Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be distantly related to pfam01117.


The actual alignment was detected with superfamily member pfam03318:

Pssm-ID: 446012 [Multi-domain]  Cd Length: 222  Bit Score: 102.48  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929048877    1 FTVPF-NETGVSLTTS--YSFANTNTNTNSKEITHNVPSQDILVPANTTVEVIAYLKKVNVKGNVKLVGQVSGSEWGEIP 77
Cdd:pfam03318  77 FGIPFvAEGGITLSVSgeYNFSSTTTNTTSVTTTYWVPSQKVTVPPHTTVRVTLVLYKTTYSVPVDLYTTLSGTFSIEGT 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 929048877   78 SYLAFPrdGYKFSLSDTVNKSD-----LNEDGTININGKGNYSAVMGDELIVKVRNLNTNNVQEYVIP 140
Cdd:pfam03318 157 RSGYVE--PASYPLTASWPLIDiifllINSDNSVNFNGSGYFELVYGLNFTIRVTETPLDNNSGETIT 222
 
Name Accession Description Interval E-value
ETX_MTX2 pfam03318
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ...
 1-140 1.30e-27

Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be distantly related to pfam01117.


Pssm-ID: 427241 [Multi-domain]  Cd Length: 222  Bit Score: 102.48  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929048877    1 FTVPF-NETGVSLTTS--YSFANTNTNTNSKEITHNVPSQDILVPANTTVEVIAYLKKVNVKGNVKLVGQVSGSEWGEIP 77
Cdd:pfam03318  77 FGIPFvAEGGITLSVSgeYNFSSTTTNTTSVTTTYWVPSQKVTVPPHTTVRVTLVLYKTTYSVPVDLYTTLSGTFSIEGT 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 929048877   78 SYLAFPrdGYKFSLSDTVNKSD-----LNEDGTININGKGNYSAVMGDELIVKVRNLNTNNVQEYVIP 140
Cdd:pfam03318 157 RSGYVE--PASYPLTASWPLIDiifllINSDNSVNFNGSGYFELVYGLNFTIRVTETPLDNNSGETIT 222
PFM_epsilon-toxin-like cd20223
pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type ...
 1-62 1.03e-13

pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type beta-barrel pore-forming proteins; Clostridium perfringens epsilon-toxin is responsible for fatal enterotoxemia in ungulates. It forms a heptamer in the lipid rafts of Madin-Darby Canine Kidney (MDCK) cells, leading to cell death; its oligomer formation is induced by activation of neutral sphingomyelinase. This group also includes an insecticidal crystal protein Cry14-4 (encoded on plasmid pBMBt1 of Bacillus thuringiensis serovar darmstadiensis). Also included is pXO2-60 (a protein from the pathogenic pXO2 plasmid of Bacillus anthracis) which harbors a unique ubiquitin-like fold domain at the C-terminus of the aerolysin-like domain, and is involved in virulence. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380793 [Multi-domain]  Cd Length: 144  Bit Score: 64.18  E-value: 1.03e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 929048877   1 FTVPFN-ETGVSLTTSYSFANTNTNTNSKEITHNVPSQDILVPANTTVEVIAYLKKVNVKGNV 62
Cdd:cd20223   63 FKIPFPgGGSTELSAEYNFSTTNTNTTSETKTYTAPSQTIKVPPGKTYKVTVYLKKVKFSGTV 125
 
Name Accession Description Interval E-value
ETX_MTX2 pfam03318
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ...
 1-140 1.30e-27

Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be distantly related to pfam01117.


Pssm-ID: 427241 [Multi-domain]  Cd Length: 222  Bit Score: 102.48  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929048877    1 FTVPF-NETGVSLTTS--YSFANTNTNTNSKEITHNVPSQDILVPANTTVEVIAYLKKVNVKGNVKLVGQVSGSEWGEIP 77
Cdd:pfam03318  77 FGIPFvAEGGITLSVSgeYNFSSTTTNTTSVTTTYWVPSQKVTVPPHTTVRVTLVLYKTTYSVPVDLYTTLSGTFSIEGT 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 929048877   78 SYLAFPrdGYKFSLSDTVNKSD-----LNEDGTININGKGNYSAVMGDELIVKVRNLNTNNVQEYVIP 140
Cdd:pfam03318 157 RSGYVE--PASYPLTASWPLIDiifllINSDNSVNFNGSGYFELVYGLNFTIRVTETPLDNNSGETIT 222
PFM_epsilon-toxin-like cd20223
pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type ...
 1-62 1.03e-13

pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type beta-barrel pore-forming proteins; Clostridium perfringens epsilon-toxin is responsible for fatal enterotoxemia in ungulates. It forms a heptamer in the lipid rafts of Madin-Darby Canine Kidney (MDCK) cells, leading to cell death; its oligomer formation is induced by activation of neutral sphingomyelinase. This group also includes an insecticidal crystal protein Cry14-4 (encoded on plasmid pBMBt1 of Bacillus thuringiensis serovar darmstadiensis). Also included is pXO2-60 (a protein from the pathogenic pXO2 plasmid of Bacillus anthracis) which harbors a unique ubiquitin-like fold domain at the C-terminus of the aerolysin-like domain, and is involved in virulence. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380793 [Multi-domain]  Cd Length: 144  Bit Score: 64.18  E-value: 1.03e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 929048877   1 FTVPFN-ETGVSLTTSYSFANTNTNTNSKEITHNVPSQDILVPANTTVEVIAYLKKVNVKGNV 62
Cdd:cd20223   63 FKIPFPgGGSTELSAEYNFSTTNTNTTSETKTYTAPSQTIKVPPGKTYKVTVYLKKVKFSGTV 125
PFM_natterin-3-like cd20220
pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar ...
 5-58 6.38e-04

pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar aerolysin-type beta-barrel pore-forming proteins; This group includes 4 of the 5 Thalassophryne nattereri fish venom natterins: natterin-1, -2, -3, and 4. Natterins have kininogenase activity, kallikrein activity, and are allodynic and edema inducing. They also cleave type I and type IV collagen, resulting in necrosis of the affected cells. Contradictory to their edematic activity, Natterins also have anti-inflammatory effects through inhibition of interactions between leukocytes and the endothelium, and reduction in neutrophil accumulation. Many proteins belonging to this group have an N-terminal DUF3421 domain. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380790 [Multi-domain]  Cd Length: 152  Bit Score: 37.99  E-value: 6.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 929048877   5 FNETGVSLTTSYSFANTNTNTNSKEITHNVpSQDILVPANT--TVEVIAYLKKVNV 58
Cdd:cd20220   59 IAGGGWEVSTETTFTWSGGTSVTESVTHSV-SVEVTVPPNHscTVKMVGYKYKADI 113
PFM_aerolysin-like cd20240
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 3-70 2.51e-03

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380810 [Multi-domain]  Cd Length: 145  Bit Score: 36.47  E-value: 2.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929048877   3 VPFNETGVSLTTSYSFANTNTNTNSKEITHNVPsqdILVPANTTV--EVIAYLKKVNVKGNVKLVGQVSG 70
Cdd:cd20240   58 IAGGEITTTTTTSQSWTYGKSETKTDTISYTFP---IVVPPNTTVtaTAVVTKYNMDVTYVATLRGINTG 124
 
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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