delta-endotoxin, partial [Bacillus thuringiensis]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
delta_endotoxin_C | cd04085 | delta-endotoxin C-terminal domain may be associated with carbohydrate binding functionality; ... |
463-606 | 1.03e-56 | ||||
delta-endotoxin C-terminal domain may be associated with carbohydrate binding functionality; Delta-endotoxin C-terminal domain (delta endotoxin domain III) is part of the activated region of delta endotoxins, which are insecticidal toxins produced during sporulation by Bacillus species of bacteria. The activated endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain (I) is involved in membrane insertion and pore formation, while the second and third domains (II and III) are involved in receptor binding. Domain III structurally resembles the carbohydrate binding domain 6 (CBM6) and it is possible that insect specificity is determined by protein-protein or protein-carbohydrate interactions mediated by both domains II and III of the toxin. Delta-endotoxins are of great interest for development of new bioinsecticides and in the control of mosquitoes. : Pssm-ID: 271151 Cd Length: 152 Bit Score: 192.83 E-value: 1.03e-56
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Endotoxin_M | pfam00555 | delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of ... |
259-461 | 2.30e-52 | ||||
delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of bacteria. During spore formation the bacteria produce crystals of this protein. When an insect ingests these proteins they are activated by proteolytic cleavage. The N-terminus is cleaved in all of the proteins and a C terminal extension is cleaved in some members. Once activated the endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain is involved in membrane insertion and pore formation. The second and third domains are involved in receptor binding. : Pssm-ID: 395440 Cd Length: 204 Bit Score: 182.64 E-value: 2.30e-52
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Cry1Ac_D5 super family | cl39422 | Insecticidal delta-endotoxin CryIA(c) domain 5; This domain is found in the protoxins portion ... |
684-868 | 2.68e-31 | ||||
Insecticidal delta-endotoxin CryIA(c) domain 5; This domain is found in the protoxins portion of insecticidal proteins (parasporins, or Cry proteins) such as those from Bacillus thuringiensis (Bt) Cry1Ac. The protoxin portion comprise a proteolytically labile C-terminal segment (sometimes referred to as the protoxin domain). This is domain V in Cry1Ac from B. thuringiensis. One of the four protoxin domains (D-IV through D-VII). Domains V and VII are beta-rolls (similar to D-II or D-III) that closely resemble carbohydrate-binding modules (CBM) found in sugar hydrolases, however, it is difficult to guess which particular carbohydrates (if any) may serve as their ligands because residues on the putative sugar-binding interfaces are conserved neither in sequence nor in local structure. Structural analysis indicate that there are putative disulfide crosslinking at the dimer interface mediated by cysteines within 783-823 region of this domain which together with other cysteines creates a three-dimensional network of cross-links across the crystal which may play a role in stabilizing mature Bt Cry1Ac. The actual alignment was detected with superfamily member pfam17997: Pssm-ID: 375474 Cd Length: 173 Bit Score: 120.95 E-value: 2.68e-31
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Endotoxin_N super family | cl04339 | delta endotoxin, N-terminal domain; This family contains insecticidal toxins produced by ... |
48-251 | 4.58e-28 | ||||
delta endotoxin, N-terminal domain; This family contains insecticidal toxins produced by Bacillus species of bacteria. During spore formation the bacteria produce crystals of this protein. When an insect ingests these proteins they are activated by proteolytic cleavage. The N-terminus is cleaved in all of the proteins and a C terminal extension is cleaved in some members. Once activated the endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain is involved in membrane insertion and pore formation. The second and third domains are involved in receptor binding. The actual alignment was detected with superfamily member pfam03945: Pssm-ID: 397850 Cd Length: 218 Bit Score: 113.39 E-value: 4.58e-28
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Endotoxin_C2 super family | cl39784 | Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) ... |
616-680 | 4.41e-06 | ||||
Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) insecticidal protein Cry1Ac. Full length structural analysis reveal that Cry1Ac contains seven distinct domains (DI-DVII): the three canonical toxin core domains (D-I through D-III) and four protoxin domains (D-IV through D-VII). Cry1Ac is sickle-shaped with the toxic core as handle and the protoxin domains as the blade. Domains IV and VI are alpha-bundles that resemble structural/interaction domains such as spectrin (PDB ID: 1CUN) or bacterial fibrinogen-binding complement inhibitor. The actual alignment was detected with superfamily member pfam18449: Pssm-ID: 436510 [Multi-domain] Cd Length: 63 Bit Score: 45.05 E-value: 4.41e-06
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Endotoxin_C2 super family | cl39784 | Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) ... |
902-939 | 1.04e-03 | ||||
Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) insecticidal protein Cry1Ac. Full length structural analysis reveal that Cry1Ac contains seven distinct domains (DI-DVII): the three canonical toxin core domains (D-I through D-III) and four protoxin domains (D-IV through D-VII). Cry1Ac is sickle-shaped with the toxic core as handle and the protoxin domains as the blade. Domains IV and VI are alpha-bundles that resemble structural/interaction domains such as spectrin (PDB ID: 1CUN) or bacterial fibrinogen-binding complement inhibitor. The actual alignment was detected with superfamily member pfam18449: Pssm-ID: 436510 [Multi-domain] Cd Length: 63 Bit Score: 38.50 E-value: 1.04e-03
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Name | Accession | Description | Interval | E-value | ||||
delta_endotoxin_C | cd04085 | delta-endotoxin C-terminal domain may be associated with carbohydrate binding functionality; ... |
463-606 | 1.03e-56 | ||||
delta-endotoxin C-terminal domain may be associated with carbohydrate binding functionality; Delta-endotoxin C-terminal domain (delta endotoxin domain III) is part of the activated region of delta endotoxins, which are insecticidal toxins produced during sporulation by Bacillus species of bacteria. The activated endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain (I) is involved in membrane insertion and pore formation, while the second and third domains (II and III) are involved in receptor binding. Domain III structurally resembles the carbohydrate binding domain 6 (CBM6) and it is possible that insect specificity is determined by protein-protein or protein-carbohydrate interactions mediated by both domains II and III of the toxin. Delta-endotoxins are of great interest for development of new bioinsecticides and in the control of mosquitoes. Pssm-ID: 271151 Cd Length: 152 Bit Score: 192.83 E-value: 1.03e-56
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Endotoxin_C | pfam03944 | delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of ... |
471-608 | 9.60e-54 | ||||
delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of bacteria. During spore formation the bacteria produce crystals of this protein. When an insect ingests these proteins they are activated by proteolytic cleavage. The N-terminus is cleaved in all of the proteins and a C terminal extension is cleaved in some members. Once activated the endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain is involved in membrane insertion and pore formation. The second and third domains are involved in receptor binding. Pssm-ID: 397849 Cd Length: 142 Bit Score: 184.04 E-value: 9.60e-54
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Endotoxin_M | pfam00555 | delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of ... |
259-461 | 2.30e-52 | ||||
delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of bacteria. During spore formation the bacteria produce crystals of this protein. When an insect ingests these proteins they are activated by proteolytic cleavage. The N-terminus is cleaved in all of the proteins and a C terminal extension is cleaved in some members. Once activated the endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain is involved in membrane insertion and pore formation. The second and third domains are involved in receptor binding. Pssm-ID: 395440 Cd Length: 204 Bit Score: 182.64 E-value: 2.30e-52
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Cry1Ac_D5 | pfam17997 | Insecticidal delta-endotoxin CryIA(c) domain 5; This domain is found in the protoxins portion ... |
684-868 | 2.68e-31 | ||||
Insecticidal delta-endotoxin CryIA(c) domain 5; This domain is found in the protoxins portion of insecticidal proteins (parasporins, or Cry proteins) such as those from Bacillus thuringiensis (Bt) Cry1Ac. The protoxin portion comprise a proteolytically labile C-terminal segment (sometimes referred to as the protoxin domain). This is domain V in Cry1Ac from B. thuringiensis. One of the four protoxin domains (D-IV through D-VII). Domains V and VII are beta-rolls (similar to D-II or D-III) that closely resemble carbohydrate-binding modules (CBM) found in sugar hydrolases, however, it is difficult to guess which particular carbohydrates (if any) may serve as their ligands because residues on the putative sugar-binding interfaces are conserved neither in sequence nor in local structure. Structural analysis indicate that there are putative disulfide crosslinking at the dimer interface mediated by cysteines within 783-823 region of this domain which together with other cysteines creates a three-dimensional network of cross-links across the crystal which may play a role in stabilizing mature Bt Cry1Ac. Pssm-ID: 375474 Cd Length: 173 Bit Score: 120.95 E-value: 2.68e-31
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Endotoxin_N | pfam03945 | delta endotoxin, N-terminal domain; This family contains insecticidal toxins produced by ... |
48-251 | 4.58e-28 | ||||
delta endotoxin, N-terminal domain; This family contains insecticidal toxins produced by Bacillus species of bacteria. During spore formation the bacteria produce crystals of this protein. When an insect ingests these proteins they are activated by proteolytic cleavage. The N-terminus is cleaved in all of the proteins and a C terminal extension is cleaved in some members. Once activated the endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain is involved in membrane insertion and pore formation. The second and third domains are involved in receptor binding. Pssm-ID: 397850 Cd Length: 218 Bit Score: 113.39 E-value: 4.58e-28
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Endotoxin_C2 | pfam18449 | Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) ... |
616-680 | 4.41e-06 | ||||
Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) insecticidal protein Cry1Ac. Full length structural analysis reveal that Cry1Ac contains seven distinct domains (DI-DVII): the three canonical toxin core domains (D-I through D-III) and four protoxin domains (D-IV through D-VII). Cry1Ac is sickle-shaped with the toxic core as handle and the protoxin domains as the blade. Domains IV and VI are alpha-bundles that resemble structural/interaction domains such as spectrin (PDB ID: 1CUN) or bacterial fibrinogen-binding complement inhibitor. Pssm-ID: 436510 [Multi-domain] Cd Length: 63 Bit Score: 45.05 E-value: 4.41e-06
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Endotoxin_C2 | pfam18449 | Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) ... |
902-939 | 1.04e-03 | ||||
Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) insecticidal protein Cry1Ac. Full length structural analysis reveal that Cry1Ac contains seven distinct domains (DI-DVII): the three canonical toxin core domains (D-I through D-III) and four protoxin domains (D-IV through D-VII). Cry1Ac is sickle-shaped with the toxic core as handle and the protoxin domains as the blade. Domains IV and VI are alpha-bundles that resemble structural/interaction domains such as spectrin (PDB ID: 1CUN) or bacterial fibrinogen-binding complement inhibitor. Pssm-ID: 436510 [Multi-domain] Cd Length: 63 Bit Score: 38.50 E-value: 1.04e-03
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Name | Accession | Description | Interval | E-value | ||||
delta_endotoxin_C | cd04085 | delta-endotoxin C-terminal domain may be associated with carbohydrate binding functionality; ... |
463-606 | 1.03e-56 | ||||
delta-endotoxin C-terminal domain may be associated with carbohydrate binding functionality; Delta-endotoxin C-terminal domain (delta endotoxin domain III) is part of the activated region of delta endotoxins, which are insecticidal toxins produced during sporulation by Bacillus species of bacteria. The activated endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain (I) is involved in membrane insertion and pore formation, while the second and third domains (II and III) are involved in receptor binding. Domain III structurally resembles the carbohydrate binding domain 6 (CBM6) and it is possible that insect specificity is determined by protein-protein or protein-carbohydrate interactions mediated by both domains II and III of the toxin. Delta-endotoxins are of great interest for development of new bioinsecticides and in the control of mosquitoes. Pssm-ID: 271151 Cd Length: 152 Bit Score: 192.83 E-value: 1.03e-56
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Endotoxin_C | pfam03944 | delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of ... |
471-608 | 9.60e-54 | ||||
delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of bacteria. During spore formation the bacteria produce crystals of this protein. When an insect ingests these proteins they are activated by proteolytic cleavage. The N-terminus is cleaved in all of the proteins and a C terminal extension is cleaved in some members. Once activated the endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain is involved in membrane insertion and pore formation. The second and third domains are involved in receptor binding. Pssm-ID: 397849 Cd Length: 142 Bit Score: 184.04 E-value: 9.60e-54
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Endotoxin_M | pfam00555 | delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of ... |
259-461 | 2.30e-52 | ||||
delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of bacteria. During spore formation the bacteria produce crystals of this protein. When an insect ingests these proteins they are activated by proteolytic cleavage. The N-terminus is cleaved in all of the proteins and a C terminal extension is cleaved in some members. Once activated the endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain is involved in membrane insertion and pore formation. The second and third domains are involved in receptor binding. Pssm-ID: 395440 Cd Length: 204 Bit Score: 182.64 E-value: 2.30e-52
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Cry1Ac_D5 | pfam17997 | Insecticidal delta-endotoxin CryIA(c) domain 5; This domain is found in the protoxins portion ... |
684-868 | 2.68e-31 | ||||
Insecticidal delta-endotoxin CryIA(c) domain 5; This domain is found in the protoxins portion of insecticidal proteins (parasporins, or Cry proteins) such as those from Bacillus thuringiensis (Bt) Cry1Ac. The protoxin portion comprise a proteolytically labile C-terminal segment (sometimes referred to as the protoxin domain). This is domain V in Cry1Ac from B. thuringiensis. One of the four protoxin domains (D-IV through D-VII). Domains V and VII are beta-rolls (similar to D-II or D-III) that closely resemble carbohydrate-binding modules (CBM) found in sugar hydrolases, however, it is difficult to guess which particular carbohydrates (if any) may serve as their ligands because residues on the putative sugar-binding interfaces are conserved neither in sequence nor in local structure. Structural analysis indicate that there are putative disulfide crosslinking at the dimer interface mediated by cysteines within 783-823 region of this domain which together with other cysteines creates a three-dimensional network of cross-links across the crystal which may play a role in stabilizing mature Bt Cry1Ac. Pssm-ID: 375474 Cd Length: 173 Bit Score: 120.95 E-value: 2.68e-31
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Endotoxin_N | pfam03945 | delta endotoxin, N-terminal domain; This family contains insecticidal toxins produced by ... |
48-251 | 4.58e-28 | ||||
delta endotoxin, N-terminal domain; This family contains insecticidal toxins produced by Bacillus species of bacteria. During spore formation the bacteria produce crystals of this protein. When an insect ingests these proteins they are activated by proteolytic cleavage. The N-terminus is cleaved in all of the proteins and a C terminal extension is cleaved in some members. Once activated the endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain is involved in membrane insertion and pore formation. The second and third domains are involved in receptor binding. Pssm-ID: 397850 Cd Length: 218 Bit Score: 113.39 E-value: 4.58e-28
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Endotoxin_C2 | pfam18449 | Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) ... |
616-680 | 4.41e-06 | ||||
Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) insecticidal protein Cry1Ac. Full length structural analysis reveal that Cry1Ac contains seven distinct domains (DI-DVII): the three canonical toxin core domains (D-I through D-III) and four protoxin domains (D-IV through D-VII). Cry1Ac is sickle-shaped with the toxic core as handle and the protoxin domains as the blade. Domains IV and VI are alpha-bundles that resemble structural/interaction domains such as spectrin (PDB ID: 1CUN) or bacterial fibrinogen-binding complement inhibitor. Pssm-ID: 436510 [Multi-domain] Cd Length: 63 Bit Score: 45.05 E-value: 4.41e-06
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CBM6-CBM35-CBM36_like | cd02795 | Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module ... |
481-604 | 7.45e-04 | ||||
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules. This alignment model also contains the C-terminal domains of bacterial insecticidal toxins, where they may be involved in determining insect specificity through carbohydrate binding functionality. Pssm-ID: 271143 Cd Length: 124 Bit Score: 40.63 E-value: 7.45e-04
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Endotoxin_C2 | pfam18449 | Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) ... |
902-939 | 1.04e-03 | ||||
Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) insecticidal protein Cry1Ac. Full length structural analysis reveal that Cry1Ac contains seven distinct domains (DI-DVII): the three canonical toxin core domains (D-I through D-III) and four protoxin domains (D-IV through D-VII). Cry1Ac is sickle-shaped with the toxic core as handle and the protoxin domains as the blade. Domains IV and VI are alpha-bundles that resemble structural/interaction domains such as spectrin (PDB ID: 1CUN) or bacterial fibrinogen-binding complement inhibitor. Pssm-ID: 436510 [Multi-domain] Cd Length: 63 Bit Score: 38.50 E-value: 1.04e-03
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Blast search parameters | ||||
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