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Conserved domains on  [gi|1732262259|gb|QEJ80923|]
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protective antigen, partial [Bacillus anthracis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Binary_toxB_2 super family cl38748
Clostridial binary toxin B/anthrax toxin PA domain 2; This domain forms the middle beta ...
 73-195 2.07e-59

Clostridial binary toxin B/anthrax toxin PA domain 2; This domain forms the middle beta sandwish domain in anthrax toxin.


The actual alignment was detected with superfamily member pfam17475:

Pssm-ID: 435917  Cd Length: 198  Bit Score: 184.31  E-value: 2.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732262259  73 PIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEVHgnaevhasffdiggsvsagfSNSNSSTVAIDHSLS 152
Cdd:pfam17475   1 PIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEPG--------------------SNSNSSTVAIDHSLS 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1732262259 153 LAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTS 195
Cdd:pfam17475  61 LAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTS 103
Binary_toxB pfam03495
Clostridial binary toxin B/anthrax toxin PA Ca-binding domain; This domain is a calcium ...
 1-70 6.69e-36

Clostridial binary toxin B/anthrax toxin PA Ca-binding domain; This domain is a calcium binding domain in the anthrax toxin protective antigen.


:

Pssm-ID: 367526 [Multi-domain]  Cd Length: 78  Bit Score: 120.66  E-value: 6.69e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732262259   1 EVEGYTVDvknkRTFLSPWISNIHEKKGLTKYKSSPEKWSTASDPYSDFEKVTGRIDKNVSPEARHPLVA 70
Cdd:pfam03495  13 EINGYTVD----KTLLVPWIDKLHAKKGFTKYVSDPNEWSTAGDPYSDFEKVSGMIDRGIHKEARHPLVA 78
 
Name Accession Description Interval E-value
Binary_toxB_2 pfam17475
Clostridial binary toxin B/anthrax toxin PA domain 2; This domain forms the middle beta ...
 73-195 2.07e-59

Clostridial binary toxin B/anthrax toxin PA domain 2; This domain forms the middle beta sandwish domain in anthrax toxin.


Pssm-ID: 435917  Cd Length: 198  Bit Score: 184.31  E-value: 2.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732262259  73 PIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEVHgnaevhasffdiggsvsagfSNSNSSTVAIDHSLS 152
Cdd:pfam17475   1 PIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEPG--------------------SNSNSSTVAIDHSLS 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1732262259 153 LAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTS 195
Cdd:pfam17475  61 LAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTS 103
Binary_toxB pfam03495
Clostridial binary toxin B/anthrax toxin PA Ca-binding domain; This domain is a calcium ...
 1-70 6.69e-36

Clostridial binary toxin B/anthrax toxin PA Ca-binding domain; This domain is a calcium binding domain in the anthrax toxin protective antigen.


Pssm-ID: 367526 [Multi-domain]  Cd Length: 78  Bit Score: 120.66  E-value: 6.69e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732262259   1 EVEGYTVDvknkRTFLSPWISNIHEKKGLTKYKSSPEKWSTASDPYSDFEKVTGRIDKNVSPEARHPLVA 70
Cdd:pfam03495  13 EINGYTVD----KTLLVPWIDKLHAKKGFTKYVSDPNEWSTAGDPYSDFEKVSGMIDRGIHKEARHPLVA 78
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 87-175 9.15e-04

pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin domain, and similar aerolysin-type beta-barrel pore-forming proteins; Jacalin-like lectins are sugar-binding protein domains. Proteins having these lectin domains may bind mono- or oligosaccharides with high specificity. 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: 380801 [Multi-domain]  Cd Length: 150  Bit Score: 38.11  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732262259  87 NEDQSTQNTDSQTRTISKNTSTSRTHTSEVHGNAEVHASFFDIGGSVSAGFSNSNSSTVAIDHSLSLAGERTWAETMGLN 166
Cdd:cd20231    16 STDYTWTFSGSRTKTTSRTWSQSSTSGFELSVSVSVSAGIPEIGEAVTTSAGWSLSATSSESETETTTDELGWSVSGTLP 95


                  ....*....
gi 1732262259 167 TADTARLNA 175
Cdd:cd20231    96 PGEGVKCRA 104
 
Name Accession Description Interval E-value
Binary_toxB_2 pfam17475
Clostridial binary toxin B/anthrax toxin PA domain 2; This domain forms the middle beta ...
 73-195 2.07e-59

Clostridial binary toxin B/anthrax toxin PA domain 2; This domain forms the middle beta sandwish domain in anthrax toxin.


Pssm-ID: 435917  Cd Length: 198  Bit Score: 184.31  E-value: 2.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732262259  73 PIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEVHgnaevhasffdiggsvsagfSNSNSSTVAIDHSLS 152
Cdd:pfam17475   1 PIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEPG--------------------SNSNSSTVAIDHSLS 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1732262259 153 LAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTS 195
Cdd:pfam17475  61 LAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTS 103
Binary_toxB pfam03495
Clostridial binary toxin B/anthrax toxin PA Ca-binding domain; This domain is a calcium ...
 1-70 6.69e-36

Clostridial binary toxin B/anthrax toxin PA Ca-binding domain; This domain is a calcium binding domain in the anthrax toxin protective antigen.


Pssm-ID: 367526 [Multi-domain]  Cd Length: 78  Bit Score: 120.66  E-value: 6.69e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732262259   1 EVEGYTVDvknkRTFLSPWISNIHEKKGLTKYKSSPEKWSTASDPYSDFEKVTGRIDKNVSPEARHPLVA 70
Cdd:pfam03495  13 EINGYTVD----KTLLVPWIDKLHAKKGFTKYVSDPNEWSTAGDPYSDFEKVSGMIDRGIHKEARHPLVA 78
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 87-175 9.15e-04

pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin domain, and similar aerolysin-type beta-barrel pore-forming proteins; Jacalin-like lectins are sugar-binding protein domains. Proteins having these lectin domains may bind mono- or oligosaccharides with high specificity. 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: 380801 [Multi-domain]  Cd Length: 150  Bit Score: 38.11  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732262259  87 NEDQSTQNTDSQTRTISKNTSTSRTHTSEVHGNAEVHASFFDIGGSVSAGFSNSNSSTVAIDHSLSLAGERTWAETMGLN 166
Cdd:cd20231    16 STDYTWTFSGSRTKTTSRTWSQSSTSGFELSVSVSVSAGIPEIGEAVTTSAGWSLSATSSESETETTTDELGWSVSGTLP 95


                  ....*....
gi 1732262259 167 TADTARLNA 175
Cdd:cd20231    96 PGEGVKCRA 104
 
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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