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Conserved domains on  [gi|158021540|gb|ABW08088|]
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insecticidal crystal protein [Bacillus thuringiensis]

Protein Classification

Graphical summary

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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; ...
 521-668 6.27e-53

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: 182.04  E-value: 6.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540  521 TNTIYPDKITQIPAVKGDQLWDGTSVVAGPGFTGGDIIRKTYGNTGYEIINVSlevPNPNQDYFIRIRYAATNDITLSVN 600
Cdd:cd04085     8 NNTIYPDKITQIPAVKAYSLGNGSSVIKGPGFTGGDLVKLTSNGGGSLKVTVT---NSLSQKYRIRIRYASNTNGTLSVS 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540  601 LF-PGFLTGNFQSTMNKGEPLTYGKFKYANFQST-KFNSSKQTIRLSVSGLTvpSGTEIYIDKIEFIPVD 668
Cdd:cd04085    85 GGgTTTNSFNFPSTMSSGDNLTYNSFKYVEFPTTfTFNSSSSTIEITIQNSS--SGGEVYIDKIEFIPVD 152
Cry1Ac_D5 super family cl39422
Insecticidal delta-endotoxin CryIA(c) domain 5; This domain is found in the protoxins portion ...
 743-926 1.64e-39

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: 144.44  E-value: 1.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   743 LQDPDFQEING--ENGWTASTGVEIIEGDAVFKGRYLRLPGAREMDTETYPTYVYQKIEEGVLKPYTRYRLRGFVGSSQG 820
Cdd:pfam17997    1 LQNGDFEELYGfgKNGWTISNNITIQADNPIFKGHYLHMSGAKDIDGTVFPTYIYQKIDESKLKPYTRYQVRGFVGSSKD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   821 LEIYTIRHQTNRIVKNVPDDLLPdvtsVNAGGGINRCSEQkyvnsrlegerglPNGNRS----AEAHEFSLPINIGELDY 896
Cdd:pfam17997   81 LGLVVTRYGKEVNVVMNPEYNTP----VTDGYTSDTCSCQ-------------PNLEKKhvvcHDYHQFKFHIDIGQLNM 143

                          170       180       190
                   ....*....|....*....|....*....|
gi 158021540   897 NENAGIWVGFKITDPEGYATLGNLGLVEEG 926
Cdd:pfam17997  144 SENIGIWVLFKISSPDGFATLDNLEVIEEG 173
Endotoxin_M pfam00555
delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of ...
 298-519 5.61e-37

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: 138.35  E-value: 5.61e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   298 TKAQLTREVYTDPIAFNLSGaagfcrpwsKYTGI-SFSEIENAVIRPPHLFNVLRSLEI--NTVRGTilgntkDYLNYWS 374
Cdd:pfam00555    1 TKSELTREIYTDPVGFESPR---------GLNIYpTFSNLENALIRPPHLFDFLNSLTIytNSSRNN------TGYNYWS 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   375 GHSLQYNF-IGNITVRESNYGYLT-SEKTR-IQLDTRDIFEINSTAA-SLANYYQETYGVPESRFHlvrwasPYDTSSHL 450
Cdd:pfam00555   66 GHRNRFSFtGGSNIISEPLYGNTTnAENPVtISFTNRDIYRTLSNTInSIYGLNNPINGVTKVDFY------GYNGTNSE 139

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   451 YSKTHTTGEGcTQVYESSEEIPVDRT-VPVNEGYGHRLSYVTALFFQKIINtfyrNGTLPVFVWTHRSAD 519
Cdd:pfam00555  140 ISSQTYRNGG-QYTIDSIDELPPETNnEPIYESYSHRLSHVTFLSGKLGQL----AGSVPSFSWTHRSAD 204
Endotoxin_N super family cl04339
delta endotoxin, N-terminal domain; This family contains insecticidal toxins produced by ...
 86-290 5.48e-24

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: 101.45  E-value: 5.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540    86 VPFASQIVSFynfILDQLW------PSNSVSVWEQIMTLVEELVDQKITEYARNKALAELKGLGDALGVYQQSLEAWLEN 159
Cdd:pfam03945    4 IPFVGPVLSF---IADLIWthlietDKSTPELFNSYRQMIQDLINNSLTQYDDNKLKALLQGCSLSLKDFRTHVKNLKAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   160 RNDTRARSVVSNQFIALELDfvgaIPSFAVS-----GQEVPLLAVYAQAVNMHLLLLRDASIFGEEWGFTSSEISTYYNR 234
Cdd:pfam03945   81 PKNATLKSTVNTIYLNLEND----IPQKYLKdcrkeGYEAYELPLFVLMATMHLGLLKEGISNGKDWGISDSDVKIFIDK 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158021540   235 QVQLTSQYSDYCVKWYDTGLQKLKGTSA------ESWLEYHQFRREMTFMVLDLVALFPNYD 290
Cdd:pfam03945  157 FNKWIVKYAEYCYTAYVKGLAKIQKESAnikdpvKQWNDLNDFRNFMILYVFDFVNLWWAFD 218
 
Name Accession Description Interval E-value
delta_endotoxin_C cd04085
delta-endotoxin C-terminal domain may be associated with carbohydrate binding functionality; ...
 521-668 6.27e-53

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: 182.04  E-value: 6.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540  521 TNTIYPDKITQIPAVKGDQLWDGTSVVAGPGFTGGDIIRKTYGNTGYEIINVSlevPNPNQDYFIRIRYAATNDITLSVN 600
Cdd:cd04085     8 NNTIYPDKITQIPAVKAYSLGNGSSVIKGPGFTGGDLVKLTSNGGGSLKVTVT---NSLSQKYRIRIRYASNTNGTLSVS 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540  601 LF-PGFLTGNFQSTMNKGEPLTYGKFKYANFQST-KFNSSKQTIRLSVSGLTvpSGTEIYIDKIEFIPVD 668
Cdd:cd04085    85 GGgTTTNSFNFPSTMSSGDNLTYNSFKYVEFPTTfTFNSSSSTIEITIQNSS--SGGEVYIDKIEFIPVD 152
Endotoxin_C pfam03944
delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of ...
 529-668 6.73e-41

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: 147.44  E-value: 6.73e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   529 ITQIPAVKGDQLWDGTSVVAGPGFTGGDIIRKTYGNTGYEIINVSLEvPNPNQDYFIRIRYAATNDITLSVNL-FPGFLT 607
Cdd:pfam03944    1 ITQIPAVKAYNLGSGASVVKGPGFTGGDLLKLRNSGGLLGRIRVTVN-APLSQRYRIRIRYASTTDSQLSVNIgGSGGNQ 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158021540   608 GNFQSTMNKGEPLT--YGKFKYANFQSTKFNSSKQTIRLSVSGLTVPSGTEIYIDKIEFIPVD 668
Cdd:pfam03944   80 INFPSTMSGGDNLTlnYGSFQYVEFSTPFTFSENPEITLTLSITNFSSNGELYIDRIEFIPVN 142
Cry1Ac_D5 pfam17997
Insecticidal delta-endotoxin CryIA(c) domain 5; This domain is found in the protoxins portion ...
 743-926 1.64e-39

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: 144.44  E-value: 1.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   743 LQDPDFQEING--ENGWTASTGVEIIEGDAVFKGRYLRLPGAREMDTETYPTYVYQKIEEGVLKPYTRYRLRGFVGSSQG 820
Cdd:pfam17997    1 LQNGDFEELYGfgKNGWTISNNITIQADNPIFKGHYLHMSGAKDIDGTVFPTYIYQKIDESKLKPYTRYQVRGFVGSSKD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   821 LEIYTIRHQTNRIVKNVPDDLLPdvtsVNAGGGINRCSEQkyvnsrlegerglPNGNRS----AEAHEFSLPINIGELDY 896
Cdd:pfam17997   81 LGLVVTRYGKEVNVVMNPEYNTP----VTDGYTSDTCSCQ-------------PNLEKKhvvcHDYHQFKFHIDIGQLNM 143

                          170       180       190
                   ....*....|....*....|....*....|
gi 158021540   897 NENAGIWVGFKITDPEGYATLGNLGLVEEG 926
Cdd:pfam17997  144 SENIGIWVLFKISSPDGFATLDNLEVIEEG 173
Endotoxin_M pfam00555
delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of ...
 298-519 5.61e-37

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: 138.35  E-value: 5.61e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   298 TKAQLTREVYTDPIAFNLSGaagfcrpwsKYTGI-SFSEIENAVIRPPHLFNVLRSLEI--NTVRGTilgntkDYLNYWS 374
Cdd:pfam00555    1 TKSELTREIYTDPVGFESPR---------GLNIYpTFSNLENALIRPPHLFDFLNSLTIytNSSRNN------TGYNYWS 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   375 GHSLQYNF-IGNITVRESNYGYLT-SEKTR-IQLDTRDIFEINSTAA-SLANYYQETYGVPESRFHlvrwasPYDTSSHL 450
Cdd:pfam00555   66 GHRNRFSFtGGSNIISEPLYGNTTnAENPVtISFTNRDIYRTLSNTInSIYGLNNPINGVTKVDFY------GYNGTNSE 139

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   451 YSKTHTTGEGcTQVYESSEEIPVDRT-VPVNEGYGHRLSYVTALFFQKIINtfyrNGTLPVFVWTHRSAD 519
Cdd:pfam00555  140 ISSQTYRNGG-QYTIDSIDELPPETNnEPIYESYSHRLSHVTFLSGKLGQL----AGSVPSFSWTHRSAD 204
Endotoxin_N pfam03945
delta endotoxin, N-terminal domain; This family contains insecticidal toxins produced by ...
 86-290 5.48e-24

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: 101.45  E-value: 5.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540    86 VPFASQIVSFynfILDQLW------PSNSVSVWEQIMTLVEELVDQKITEYARNKALAELKGLGDALGVYQQSLEAWLEN 159
Cdd:pfam03945    4 IPFVGPVLSF---IADLIWthlietDKSTPELFNSYRQMIQDLINNSLTQYDDNKLKALLQGCSLSLKDFRTHVKNLKAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   160 RNDTRARSVVSNQFIALELDfvgaIPSFAVS-----GQEVPLLAVYAQAVNMHLLLLRDASIFGEEWGFTSSEISTYYNR 234
Cdd:pfam03945   81 PKNATLKSTVNTIYLNLEND----IPQKYLKdcrkeGYEAYELPLFVLMATMHLGLLKEGISNGKDWGISDSDVKIFIDK 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158021540   235 QVQLTSQYSDYCVKWYDTGLQKLKGTSA------ESWLEYHQFRREMTFMVLDLVALFPNYD 290
Cdd:pfam03945  157 FNKWIVKYAEYCYTAYVKGLAKIQKESAnikdpvKQWNDLNDFRNFMILYVFDFVNLWWAFD 218
 
Name Accession Description Interval E-value
delta_endotoxin_C cd04085
delta-endotoxin C-terminal domain may be associated with carbohydrate binding functionality; ...
 521-668 6.27e-53

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: 182.04  E-value: 6.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540  521 TNTIYPDKITQIPAVKGDQLWDGTSVVAGPGFTGGDIIRKTYGNTGYEIINVSlevPNPNQDYFIRIRYAATNDITLSVN 600
Cdd:cd04085     8 NNTIYPDKITQIPAVKAYSLGNGSSVIKGPGFTGGDLVKLTSNGGGSLKVTVT---NSLSQKYRIRIRYASNTNGTLSVS 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540  601 LF-PGFLTGNFQSTMNKGEPLTYGKFKYANFQST-KFNSSKQTIRLSVSGLTvpSGTEIYIDKIEFIPVD 668
Cdd:cd04085    85 GGgTTTNSFNFPSTMSSGDNLTYNSFKYVEFPTTfTFNSSSSTIEITIQNSS--SGGEVYIDKIEFIPVD 152
Endotoxin_C pfam03944
delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of ...
 529-668 6.73e-41

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: 147.44  E-value: 6.73e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   529 ITQIPAVKGDQLWDGTSVVAGPGFTGGDIIRKTYGNTGYEIINVSLEvPNPNQDYFIRIRYAATNDITLSVNL-FPGFLT 607
Cdd:pfam03944    1 ITQIPAVKAYNLGSGASVVKGPGFTGGDLLKLRNSGGLLGRIRVTVN-APLSQRYRIRIRYASTTDSQLSVNIgGSGGNQ 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158021540   608 GNFQSTMNKGEPLT--YGKFKYANFQSTKFNSSKQTIRLSVSGLTVPSGTEIYIDKIEFIPVD 668
Cdd:pfam03944   80 INFPSTMSGGDNLTlnYGSFQYVEFSTPFTFSENPEITLTLSITNFSSNGELYIDRIEFIPVN 142
Cry1Ac_D5 pfam17997
Insecticidal delta-endotoxin CryIA(c) domain 5; This domain is found in the protoxins portion ...
 743-926 1.64e-39

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: 144.44  E-value: 1.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   743 LQDPDFQEING--ENGWTASTGVEIIEGDAVFKGRYLRLPGAREMDTETYPTYVYQKIEEGVLKPYTRYRLRGFVGSSQG 820
Cdd:pfam17997    1 LQNGDFEELYGfgKNGWTISNNITIQADNPIFKGHYLHMSGAKDIDGTVFPTYIYQKIDESKLKPYTRYQVRGFVGSSKD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   821 LEIYTIRHQTNRIVKNVPDDLLPdvtsVNAGGGINRCSEQkyvnsrlegerglPNGNRS----AEAHEFSLPINIGELDY 896
Cdd:pfam17997   81 LGLVVTRYGKEVNVVMNPEYNTP----VTDGYTSDTCSCQ-------------PNLEKKhvvcHDYHQFKFHIDIGQLNM 143

                          170       180       190
                   ....*....|....*....|....*....|
gi 158021540   897 NENAGIWVGFKITDPEGYATLGNLGLVEEG 926
Cdd:pfam17997  144 SENIGIWVLFKISSPDGFATLDNLEVIEEG 173
Endotoxin_M pfam00555
delta endotoxin; This family contains insecticidal toxins produced by Bacillus species of ...
 298-519 5.61e-37

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: 138.35  E-value: 5.61e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   298 TKAQLTREVYTDPIAFNLSGaagfcrpwsKYTGI-SFSEIENAVIRPPHLFNVLRSLEI--NTVRGTilgntkDYLNYWS 374
Cdd:pfam00555    1 TKSELTREIYTDPVGFESPR---------GLNIYpTFSNLENALIRPPHLFDFLNSLTIytNSSRNN------TGYNYWS 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   375 GHSLQYNF-IGNITVRESNYGYLT-SEKTR-IQLDTRDIFEINSTAA-SLANYYQETYGVPESRFHlvrwasPYDTSSHL 450
Cdd:pfam00555   66 GHRNRFSFtGGSNIISEPLYGNTTnAENPVtISFTNRDIYRTLSNTInSIYGLNNPINGVTKVDFY------GYNGTNSE 139

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   451 YSKTHTTGEGcTQVYESSEEIPVDRT-VPVNEGYGHRLSYVTALFFQKIINtfyrNGTLPVFVWTHRSAD 519
Cdd:pfam00555  140 ISSQTYRNGG-QYTIDSIDELPPETNnEPIYESYSHRLSHVTFLSGKLGQL----AGSVPSFSWTHRSAD 204
Endotoxin_N pfam03945
delta endotoxin, N-terminal domain; This family contains insecticidal toxins produced by ...
 86-290 5.48e-24

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: 101.45  E-value: 5.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540    86 VPFASQIVSFynfILDQLW------PSNSVSVWEQIMTLVEELVDQKITEYARNKALAELKGLGDALGVYQQSLEAWLEN 159
Cdd:pfam03945    4 IPFVGPVLSF---IADLIWthlietDKSTPELFNSYRQMIQDLINNSLTQYDDNKLKALLQGCSLSLKDFRTHVKNLKAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158021540   160 RNDTRARSVVSNQFIALELDfvgaIPSFAVS-----GQEVPLLAVYAQAVNMHLLLLRDASIFGEEWGFTSSEISTYYNR 234
Cdd:pfam03945   81 PKNATLKSTVNTIYLNLEND----IPQKYLKdcrkeGYEAYELPLFVLMATMHLGLLKEGISNGKDWGISDSDVKIFIDK 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158021540   235 QVQLTSQYSDYCVKWYDTGLQKLKGTSA------ESWLEYHQFRREMTFMVLDLVALFPNYD 290
Cdd:pfam03945  157 FNKWIVKYAEYCYTAYVKGLAKIQKESAnikdpvKQWNDLNDFRNFMILYVFDFVNLWWAFD 218
 
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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