protective antigen, partial [Bacillus anthracis]
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
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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
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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
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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
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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
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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
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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
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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
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Blast search parameters | ||||
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