NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|386277681|gb|AFJ04417|]
View 

Cry5B-like delta endotoxin [Bacillus thuringiensis]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Endotoxin_C pfam03944
delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of ...
 562-695 1.98e-28

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: 111.62  E-value: 1.98e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   562 KGFPFEKyGSEYNNRGISLVREWINGNNAVKLSNSQSVG----IQITNQTKQKYEIRCRYASKGDNNVYFNVDLSENpfr 637
Cdd:pfam03944    2 TQIPAVK-AYNLGSGASVVKGPGFTGGDLLKLRNSGGLLgrirVTVNAPLSQRYRIRIRYASTTDSQLSVNIGGSGG--- 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386277681   638 NSISFGSTESSVVGVQGENGKYILKSITTV----EIPAGSFYVHITNQGS-SDLFLDRIEFVP 695
Cdd:pfam03944   78 NQINFPSTMSGGDNLTLNYGSFQYVEFSTPftfsENPEITLTLSITNFSSnGELYIDRIEFIP 140
Cry1Ac_D5 super family cl39422
Insecticidal delta-endotoxin CryIA(c) domain 5; This domain is found in the protoxins portion ...
 827-986 9.37e-21

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: 90.90  E-value: 9.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   827 LIGGNFDNL-----DAWYRGRNVVNVSDHELFKSDHVLLPPP-----TLYSSYMFQKVEESKLKANTRYTVSGFIAHAED 896
Cdd:pfam17997    1 LQNGDFEELygfgkNGWTISNNITIQADNPIFKGHYLHMSGAkdidgTVFPTYIYQKIDESKLKPYTRYQVRGFVGSSKD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   897 LEIVVSRYGQEVKKVVQVPYGEAFP--LTSRGAICCPPRSTCNGKPADPHFFSYSIDVGTLDVEANPGIELGLRIVERTG 974
Cdd:pfam17997   81 LGLVVTRYGKEVNVVMNPEYNTPVTdgYTSDTCSCQPNLEKKHVVCHDYHQFKFHIDIGQLNMSENIGIWVLFKISSPDG 160

                          170
                   ....*....|..
gi 386277681   975 MARVSNLEIRED 986
Cdd:pfam17997  161 FATLDNLEVIEE 172
Endotoxin_N super family cl04339
delta endotoxin, N-terminal domain; This family contains insecticidal toxins produced by ...
 91-327 2.27e-10

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: 61.78  E-value: 2.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681    91 PFINMFVDFVWPKLFGANTEGKDqqLFNAIMDAVNKMVDNKFLRYNLSTLNKTIEGLQGNLGLFQNpiQVAICQGstper 170
Cdd:pfam03945    9 PVLSFIADLIWTHLIETDKSTPE--LFNSYRQMIQDLINNSLTQYDDNKLKALLQGCSLSLKDFRT--HVKNLKA----- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   171 vifdqnctpcNPNQpckddlDRVASRFDTANSQFTQHLPEF--KNPWSDENSTQEfkrtsveltLPLYTTVATLHLLLYK 248
Cdd:pfam03945   80 ----------DPKN------ATLKSTVNTIYLNLENDIPQKylKDCRKEGYEAYE---------LPLFVLMATMHLGLLK 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   249 GYIEFMTKWNFHNAQyLNNLKVELQQLIHSYSETVRTSFLQFLPTLNNRS---KSSV---NAYNGYVRNMTVNCLDIAAT 322
Cdd:pfam03945  135 EGISNGKDWGISDSD-VKIFIDKFNKWIVKYAEYCYTAYVKGLAKIQKESaniKDPVkqwNDLNDFRNFMILYVFDFVNL 213


                   ....*
gi 386277681   323 WPTFD 327
Cdd:pfam03945  214 WWAFD 218
Endotoxin_C2 super family cl39784
Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) ...
 758-820 3.73e-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: 36.96  E-value: 3.73e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386277681   758 TDLQNITTQVNALVASSEHDTLATDVSDYEIEEVVLKVDALsgeVFGKEKKALRKLVNHTKRL 820
Cdd:pfam18449    1 KQLQAATTAVNSLFTDDSHTALAAEVTQAEIDAAKKLVDKL---PSSKEKTKLLKDIKKAQAL 60
 
Name Accession Description Interval E-value
Endotoxin_C pfam03944
delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of ...
 562-695 1.98e-28

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: 111.62  E-value: 1.98e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   562 KGFPFEKyGSEYNNRGISLVREWINGNNAVKLSNSQSVG----IQITNQTKQKYEIRCRYASKGDNNVYFNVDLSENpfr 637
Cdd:pfam03944    2 TQIPAVK-AYNLGSGASVVKGPGFTGGDLLKLRNSGGLLgrirVTVNAPLSQRYRIRIRYASTTDSQLSVNIGGSGG--- 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386277681   638 NSISFGSTESSVVGVQGENGKYILKSITTV----EIPAGSFYVHITNQGS-SDLFLDRIEFVP 695
Cdd:pfam03944   78 NQINFPSTMSGGDNLTLNYGSFQYVEFSTPftfsENPEITLTLSITNFSSnGELYIDRIEFIP 140
delta_endotoxin_C cd04085
delta-endotoxin C-terminal domain may be associated with carbohydrate binding functionality; ...
 554-695 2.33e-23

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: 97.68  E-value: 2.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681  554 TKLPLT--------QLKGFPFEKyGSEYNNrGISLVREWI-NGNNAVKLSNS--QSVGIQITNQTKQKYEIRCRYASkgD 622
Cdd:cd04085     1 TKSELTrnntiypdKITQIPAVK-AYSLGN-GSSVIKGPGfTGGDLVKLTSNggGSLKVTVTNSLSQKYRIRIRYAS--N 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386277681  623 NNVYFNVDLSeNPFRNSISFGSTESSVVGVQGENGKYILkSITTVEIPAGSFYVHITNQ---GSSDLFLDRIEFVP 695
Cdd:cd04085    77 TNGTLSVSGG-GTTTNSFNFPSTMSSGDNLTYNSFKYVE-FPTTFTFNSSSSTIEITIQnssSGGEVYIDKIEFIP 150
Cry1Ac_D5 pfam17997
Insecticidal delta-endotoxin CryIA(c) domain 5; This domain is found in the protoxins portion ...
 827-986 9.37e-21

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: 90.90  E-value: 9.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   827 LIGGNFDNL-----DAWYRGRNVVNVSDHELFKSDHVLLPPP-----TLYSSYMFQKVEESKLKANTRYTVSGFIAHAED 896
Cdd:pfam17997    1 LQNGDFEELygfgkNGWTISNNITIQADNPIFKGHYLHMSGAkdidgTVFPTYIYQKIDESKLKPYTRYQVRGFVGSSKD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   897 LEIVVSRYGQEVKKVVQVPYGEAFP--LTSRGAICCPPRSTCNGKPADPHFFSYSIDVGTLDVEANPGIELGLRIVERTG 974
Cdd:pfam17997   81 LGLVVTRYGKEVNVVMNPEYNTPVTdgYTSDTCSCQPNLEKKHVVCHDYHQFKFHIDIGQLNMSENIGIWVLFKISSPDG 160

                          170
                   ....*....|..
gi 386277681   975 MARVSNLEIRED 986
Cdd:pfam17997  161 FATLDNLEVIEE 172
Endotoxin_N pfam03945
delta endotoxin, N-terminal domain; This family contains insecticidal toxins produced by ...
 91-327 2.27e-10

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: 61.78  E-value: 2.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681    91 PFINMFVDFVWPKLFGANTEGKDqqLFNAIMDAVNKMVDNKFLRYNLSTLNKTIEGLQGNLGLFQNpiQVAICQGstper 170
Cdd:pfam03945    9 PVLSFIADLIWTHLIETDKSTPE--LFNSYRQMIQDLINNSLTQYDDNKLKALLQGCSLSLKDFRT--HVKNLKA----- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   171 vifdqnctpcNPNQpckddlDRVASRFDTANSQFTQHLPEF--KNPWSDENSTQEfkrtsveltLPLYTTVATLHLLLYK 248
Cdd:pfam03945   80 ----------DPKN------ATLKSTVNTIYLNLENDIPQKylKDCRKEGYEAYE---------LPLFVLMATMHLGLLK 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   249 GYIEFMTKWNFHNAQyLNNLKVELQQLIHSYSETVRTSFLQFLPTLNNRS---KSSV---NAYNGYVRNMTVNCLDIAAT 322
Cdd:pfam03945  135 EGISNGKDWGISDSD-VKIFIDKFNKWIVKYAEYCYTAYVKGLAKIQKESaniKDPVkqwNDLNDFRNFMILYVFDFVNL 213


                   ....*
gi 386277681   323 WPTFD 327
Cdd:pfam03945  214 WWAFD 218
Endotoxin_C2 pfam18449
Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) ...
 758-820 3.73e-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: 36.96  E-value: 3.73e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386277681   758 TDLQNITTQVNALVASSEHDTLATDVSDYEIEEVVLKVDALsgeVFGKEKKALRKLVNHTKRL 820
Cdd:pfam18449    1 KQLQAATTAVNSLFTDDSHTALAAEVTQAEIDAAKKLVDKL---PSSKEKTKLLKDIKKAQAL 60
 
Name Accession Description Interval E-value
Endotoxin_C pfam03944
delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of ...
 562-695 1.98e-28

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: 111.62  E-value: 1.98e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   562 KGFPFEKyGSEYNNRGISLVREWINGNNAVKLSNSQSVG----IQITNQTKQKYEIRCRYASKGDNNVYFNVDLSENpfr 637
Cdd:pfam03944    2 TQIPAVK-AYNLGSGASVVKGPGFTGGDLLKLRNSGGLLgrirVTVNAPLSQRYRIRIRYASTTDSQLSVNIGGSGG--- 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386277681   638 NSISFGSTESSVVGVQGENGKYILKSITTV----EIPAGSFYVHITNQGS-SDLFLDRIEFVP 695
Cdd:pfam03944   78 NQINFPSTMSGGDNLTLNYGSFQYVEFSTPftfsENPEITLTLSITNFSSnGELYIDRIEFIP 140
delta_endotoxin_C cd04085
delta-endotoxin C-terminal domain may be associated with carbohydrate binding functionality; ...
 554-695 2.33e-23

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: 97.68  E-value: 2.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681  554 TKLPLT--------QLKGFPFEKyGSEYNNrGISLVREWI-NGNNAVKLSNS--QSVGIQITNQTKQKYEIRCRYASkgD 622
Cdd:cd04085     1 TKSELTrnntiypdKITQIPAVK-AYSLGN-GSSVIKGPGfTGGDLVKLTSNggGSLKVTVTNSLSQKYRIRIRYAS--N 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386277681  623 NNVYFNVDLSeNPFRNSISFGSTESSVVGVQGENGKYILkSITTVEIPAGSFYVHITNQ---GSSDLFLDRIEFVP 695
Cdd:cd04085    77 TNGTLSVSGG-GTTTNSFNFPSTMSSGDNLTYNSFKYVE-FPTTFTFNSSSSTIEITIQnssSGGEVYIDKIEFIP 150
Cry1Ac_D5 pfam17997
Insecticidal delta-endotoxin CryIA(c) domain 5; This domain is found in the protoxins portion ...
 827-986 9.37e-21

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: 90.90  E-value: 9.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   827 LIGGNFDNL-----DAWYRGRNVVNVSDHELFKSDHVLLPPP-----TLYSSYMFQKVEESKLKANTRYTVSGFIAHAED 896
Cdd:pfam17997    1 LQNGDFEELygfgkNGWTISNNITIQADNPIFKGHYLHMSGAkdidgTVFPTYIYQKIDESKLKPYTRYQVRGFVGSSKD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   897 LEIVVSRYGQEVKKVVQVPYGEAFP--LTSRGAICCPPRSTCNGKPADPHFFSYSIDVGTLDVEANPGIELGLRIVERTG 974
Cdd:pfam17997   81 LGLVVTRYGKEVNVVMNPEYNTPVTdgYTSDTCSCQPNLEKKHVVCHDYHQFKFHIDIGQLNMSENIGIWVLFKISSPDG 160

                          170
                   ....*....|..
gi 386277681   975 MARVSNLEIRED 986
Cdd:pfam17997  161 FATLDNLEVIEE 172
Endotoxin_N pfam03945
delta endotoxin, N-terminal domain; This family contains insecticidal toxins produced by ...
 91-327 2.27e-10

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: 61.78  E-value: 2.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681    91 PFINMFVDFVWPKLFGANTEGKDqqLFNAIMDAVNKMVDNKFLRYNLSTLNKTIEGLQGNLGLFQNpiQVAICQGstper 170
Cdd:pfam03945    9 PVLSFIADLIWTHLIETDKSTPE--LFNSYRQMIQDLINNSLTQYDDNKLKALLQGCSLSLKDFRT--HVKNLKA----- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   171 vifdqnctpcNPNQpckddlDRVASRFDTANSQFTQHLPEF--KNPWSDENSTQEfkrtsveltLPLYTTVATLHLLLYK 248
Cdd:pfam03945   80 ----------DPKN------ATLKSTVNTIYLNLENDIPQKylKDCRKEGYEAYE---------LPLFVLMATMHLGLLK 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386277681   249 GYIEFMTKWNFHNAQyLNNLKVELQQLIHSYSETVRTSFLQFLPTLNNRS---KSSV---NAYNGYVRNMTVNCLDIAAT 322
Cdd:pfam03945  135 EGISNGKDWGISDSD-VKIFIDKFNKWIVKYAEYCYTAYVKGLAKIQKESaniKDPVkqwNDLNDFRNFMILYVFDFVNL 213


                   ....*
gi 386277681   323 WPTFD 327
Cdd:pfam03945  214 WWAFD 218
Endotoxin_C2 pfam18449
Delta endotoxin; This is domain (D-VI) can be found in Bacillus thuringiensis (Bt) ...
 758-820 3.73e-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: 36.96  E-value: 3.73e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386277681   758 TDLQNITTQVNALVASSEHDTLATDVSDYEIEEVVLKVDALsgeVFGKEKKALRKLVNHTKRL 820
Cdd:pfam18449    1 KQLQAATTAVNSLFTDDSHTALAAEVTQAEIDAAKKLVDKL---PSSKEKTKLLKDIKKAQAL 60
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH