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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335355168 456 TNTIESNIITQIPLVKAYQIGSGTTVRKGPGFTGGDILRRTgPGTFGDMRININAPLSQRYRVRIRYASTTDLQFVTSIN 535
Cdd:cd04085    8 NNTIYPDKITQIPAVKAYSLGNGSSVIKGPGFTGGDLVKLT-SNGGGSLKVTVTNSLSQKYRIRIRYASNTNGTLSVSGG 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 335355168 536 GTTINIGNFPKTINNLNTLGSEGYRTVSFSTPFSFSNAQSIFRLGIQAFSGVQEVYVDKIEFIPVE 601
Cdd:cd04085   87 GTTTNSFNFPSTMSSGDNLTYNSFKYVEFPTTFTFNSSSSTIEITIQNSSSGGEVYIDKIEFIPVD 152

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335355168   44 MIPG-GTALQFVFNQLWSRLGDSG------WNAFMEHVEELIDTKIEGYAKNKALSELAGIQRNLETYIQLRNEWENDIE 116
Cdd:pfam03945   3 LIPFvGPVLSFIADLIWTHLIETDkstpelFNSYRQMIQDLINNSLTQYDDNKLKALLQGCSLSLKDFRTHVKNLKADPK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335355168  117 NSKAQGKVANYYESLEQAVE-RSMPQFAVENFEVPLLTVYVQAANLHLLLLRDVSVYGKCWGWSEQKIKIYYDKQIKYTH 195
Cdd:pfam03945  83 NATLKSTVNTIYLNLENDIPqKYLKDCRKEGYEAYELPLFVLMATMHLGLLKEGISNGKDWGISDSDVKIFIDKFNKWIV 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 335355168  196 EYTNHCVNWYNKGLERLK----NKGSSYQDWYNYNRFRREMTLTVLDIVALFPHYD 247
Cdd:pfam03945 163 KYAEYCYTAYVKGLAKIQkesaNIKDPVKQWNDLNDFRNFMILYVFDFVNLWWAFD 218

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335355168 456 TNTIESNIITQIPLVKAYQIGSGTTVRKGPGFTGGDILRRTgPGTFGDMRININAPLSQRYRVRIRYASTTDLQFVTSIN 535
Cdd:cd04085    8 NNTIYPDKITQIPAVKAYSLGNGSSVIKGPGFTGGDLVKLT-SNGGGSLKVTVTNSLSQKYRIRIRYASNTNGTLSVSGG 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 335355168 536 GTTINIGNFPKTINNLNTLGSEGYRTVSFSTPFSFSNAQSIFRLGIQAFSGVQEVYVDKIEFIPVE 601
Cdd:cd04085   87 GTTTNSFNFPSTMSSGDNLTYNSFKYVEFPTTFTFNSSSSTIEITIQNSSSGGEVYIDKIEFIPVD 152

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335355168  255 TVAQLTREVYTDPLLNFNPKLHSVSqlPSFSDMENATIRTPHLMEFLRMLTIYTDWYSVG-RNYYWGGHRVTSYHVGGEN 333
Cdd:pfam00555   1 TKSELTREIYTDPVGFESPRGLNIY--PTFSNLENALIRPPHLFDFLNSLTIYTNSSRNNtGYNYWSGHRNRFSFTGGSN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335355168  334 -IRSPLYGREANQEVPRDFYFYG-PVFKTLSKPTLRPLQQPApappfNLRSLEGVEFHT------PTGSFMYRERG--SV 403
Cdd:pfam00555  79 iISEPLYGNTTNAENPVTISFTNrDIYRTLSNTINSIYGLNN-----PINGVTKVDFYGyngtnsEISSQTYRNGGqyTI 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 335355168  404 DSFNELPPFNPVGLPHKVYSHRLCHATFVRKSGTPYLTTGAIFSWTHRSAE 454
Cdd:pfam00555 154 DSIDELPPETNNEPIYESYSHRLSHVTFLSGKLGQLAGSVPSFSWTHRSAD 204

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335355168 456 TNTIESNIITQIPLVKAYQIGSGTTVRKGPGFTGGDILRRTgPGTFGDMRININAPLSQRYRVRIRYASTTDLQFVTSIN 535
Cdd:cd04085    8 NNTIYPDKITQIPAVKAYSLGNGSSVIKGPGFTGGDLVKLT-SNGGGSLKVTVTNSLSQKYRIRIRYASNTNGTLSVSGG 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 335355168 536 GTTINIGNFPKTINNLNTLGSEGYRTVSFSTPFSFSNAQSIFRLGIQAFSGVQEVYVDKIEFIPVE 601
Cdd:cd04085   87 GTTTNSFNFPSTMSSGDNLTYNSFKYVEFPTTFTFNSSSSTIEITIQNSSSGGEVYIDKIEFIPVD 152

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335355168  255 TVAQLTREVYTDPLLNFNPKLHSVSqlPSFSDMENATIRTPHLMEFLRMLTIYTDWYSVG-RNYYWGGHRVTSYHVGGEN 333
Cdd:pfam00555   1 TKSELTREIYTDPVGFESPRGLNIY--PTFSNLENALIRPPHLFDFLNSLTIYTNSSRNNtGYNYWSGHRNRFSFTGGSN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335355168  334 -IRSPLYGREANQEVPRDFYFYG-PVFKTLSKPTLRPLQQPApappfNLRSLEGVEFHT------PTGSFMYRERG--SV 403
Cdd:pfam00555  79 iISEPLYGNTTNAENPVTISFTNrDIYRTLSNTINSIYGLNN-----PINGVTKVDFYGyngtnsEISSQTYRNGGqyTI 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 335355168  404 DSFNELPPFNPVGLPHKVYSHRLCHATFVRKSGTPYLTTGAIFSWTHRSAE 454
Cdd:pfam00555 154 DSIDELPPETNNEPIYESYSHRLSHVTFLSGKLGQLAGSVPSFSWTHRSAD 204

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335355168 466 QIPLVKAYQIGSGTTVRKGPGFTGGDILRRTGPGtfGDMRININAPLSQRYRVRIRYASTTDL-QFVTSINGTTINIGNF 544
Cdd:cd02795    1 RIEAEDATLTGGTAVSTAAGASGGGYVIGFSSGG--DSVTFTVTVPKAGTYRLAVRYASPNGNgSRSVSLDGNGKLVGTI 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 335355168 545 PKTinnlNTLGSEGYRTVSFSTPFSFSNAQSIfrlGIQAFSGVQEVYVDKIEF 597
Cdd:cd02795   79 TVP----STGGWDTWGTASVSVNLPDAGGHTL---KIVGTGDNGGANIDYVVV 124