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Conserved domains on  [gi|388849893|gb|AFK79791|]
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delta-endotoxin, partial [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; ...
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893  463 NNIIPSSQITQIPLTKSTNLGSGTSVVKGPGFTGGDILRRTSPGQIsTLRVNITAPLSQRYRVGIRYASTTNLQFHTSID 542
Cdd:cd04085     8 NNTIYPDKITQIPAVKAYSLGNGSSVIKGPGFTGGDLVKLTSNGGG-SLKVTVTNSLSQKYRIRIRYASNTNGTLSVSGG 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388849893  543 GRPINQGNFSATMSSGSNLQSGSFRTVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYIDRIEFVP 606
Cdd:cd04085    87 GTTTNSFNFPSTMSSGDNLTYNSFKYVEFPTTFTFNSSSSTIEITIQNSSSGGEVYIDKIEFIP 150
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
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   259 TVSQLTREIYTNPVLENFDGSFRGSAQG---IEGSIRSPHLMDILNSITIYTDAHR---GEYYWSGHQIMASPVGFSgPE 332
Cdd:pfam00555    1 TKSELTREIYTDPVGFESPRGLNIYPTFsnlENALIRPPHLFDFLNSLTIYTNSSRnntGYNYWSGHRNRFSFTGGS-NI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   333 FTFPLYGTMGNAAPQQRIVAqLGQGVYRTLSSTLYRRPFNiginNQQLSVLDGTEFAY--GTSSNLPSAVYKKSG--TVD 408
Cdd:pfam00555   80 ISEPLYGNTTNAENPVTISF-TNRDIYRTLSNTINSIYGL----NNPINGVTKVDFYGynGTNSEISSQTYRNGGqyTID 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 388849893   409 SLDEIPPQNNNVPPRQGFSHRLSHVSMFRSGFSNSSvsiIRAPMFSWIHRSAE 461
Cdd:pfam00555  155 SIDELPPETNNEPIYESYSHRLSHVTFLSGKLGQLA---GSVPSFSWTHRSAD 204
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
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   684 LQDPNFRGINRQLDRGWRGSTDITIQGGDDVFKENCVTLLGTFD---ECYPTYLYQKIDESKLKAYTRYQLRGYIEDSQD 760
Cdd:pfam17997    1 LQNGDFEELYGFGKNGWTISNNITIQADNPIFKGHYLHMSGAKDidgTVFPTYIYQKIDESKLKPYTRYQVRGFVGSSKD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   761 LEIYLIRYNAKHETVNVPgtgslwplSAQSPI--GKCGEPNRCAPHLEwnpdldcscrDGEKCAHHSHHFSLDIDVGCTD 838
Cdd:pfam17997   81 LGLVVTRYGKEVNVVMNP--------EYNTPVtdGYTSDTCSCQPNLE----------KKHVVCHDYHQFKFHIDIGQLN 142
                          170       180       190
                   ....*....|....*....|....*....|
gi 388849893   839 LNEDLGVWVIFKIKTQDGHARLGNLEFLEE 868
Cdd:pfam17997  143 MSENIGIWVLFKISSPDGFATLDNLEVIEE 172
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
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893    48 SEFVPGAGFVL-GLVDIIWGIFG---PSQWDAFLV---QIEQLINQRIEEFARNQAISRLEGLSNLYQIYAESFREWEAD 120
Cdd:pfam03945    1 LSLIPFVGPVLsFIADLIWTHLIetdKSTPELFNSyrqMIQDLINNSLTQYDDNKLKALLQGCSLSLKDFRTHVKNLKAD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   121 PTNPALREEMRIQFNDM-NSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVLRDVSVFGQRWGFDAATINSRYNDLTRL 199
Cdd:pfam03945   81 PKNATLKSTVNTIYLNLeNDIPQKYLKDCRKEGYEAYELPLFVLMATMHLGLLKEGISNGKDWGISDSDVKIFIDKFNKW 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 388849893   200 IGNYTDHAVRWYNTGLERVWGPDS------RDWIRYNQFRRELTLTVLDIVSLFPNYD 251
Cdd:pfam03945  161 IVKYAEYCYTAYVKGLAKIQKESAnikdpvKQWNDLNDFRNFMILYVFDFVNLWWAFD 218
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
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388849893   616 DLERAQKAVNELFTSSNQIGLKTDVTDYHIDQVSNLVECLSDEfclDEKQELSEKVKHAKRLSDE 680
Cdd:pfam18449    2 QLQAATTAVNSLFTDDSHTALAAEVTQAEIDAAKKLVDKLPSS---KEKTKLLKDIKKAQALLDA 63
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
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 388849893   902 KEAKESVDALFVNSQYDQLQADTNIAMIHAADKRVHSI 939
Cdd:pfam18449    4 QAATTAVNSLFTDDSHTALAAEVTQAEIDAAKKLVDKL 41
 
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893  463 NNIIPSSQITQIPLTKSTNLGSGTSVVKGPGFTGGDILRRTSPGQIsTLRVNITAPLSQRYRVGIRYASTTNLQFHTSID 542
Cdd:cd04085     8 NNTIYPDKITQIPAVKAYSLGNGSSVIKGPGFTGGDLVKLTSNGGG-SLKVTVTNSLSQKYRIRIRYASNTNGTLSVSGG 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388849893  543 GRPINQGNFSATMSSGSNLQSGSFRTVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYIDRIEFVP 606
Cdd:cd04085    87 GTTTNSFNFPSTMSSGDNLTYNSFKYVEFPTTFTFNSSSSTIEITIQNSSSGGEVYIDKIEFIP 150
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
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   471 ITQIPLTKSTNLGSGTSVVKGPGFTGGDILR-RTSPGQISTLRVNITAPLSQRYRVGIRYASTTNLQFHTSIDGRPINQG 549
Cdd:pfam03944    1 ITQIPAVKAYNLGSGASVVKGPGFTGGDLLKlRNSGGLLGRIRVTVNAPLSQRYRIRIRYASTTDSQLSVNIGGSGGNQI 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388849893   550 NFSATMSSGSNLQ--SGSFRTVGFTTPFNFSNGSSV-FTLSAHVFNSGNEVYIDRIEFVPAE 608
Cdd:pfam03944   81 NFPSTMSGGDNLTlnYGSFQYVEFSTPFTFSENPEItLTLSITNFSSNGELYIDRIEFIPVN 142
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
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   259 TVSQLTREIYTNPVLENFDGSFRGSAQG---IEGSIRSPHLMDILNSITIYTDAHR---GEYYWSGHQIMASPVGFSgPE 332
Cdd:pfam00555    1 TKSELTREIYTDPVGFESPRGLNIYPTFsnlENALIRPPHLFDFLNSLTIYTNSSRnntGYNYWSGHRNRFSFTGGS-NI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   333 FTFPLYGTMGNAAPQQRIVAqLGQGVYRTLSSTLYRRPFNiginNQQLSVLDGTEFAY--GTSSNLPSAVYKKSG--TVD 408
Cdd:pfam00555   80 ISEPLYGNTTNAENPVTISF-TNRDIYRTLSNTINSIYGL----NNPINGVTKVDFYGynGTNSEISSQTYRNGGqyTID 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 388849893   409 SLDEIPPQNNNVPPRQGFSHRLSHVSMFRSGFSNSSvsiIRAPMFSWIHRSAE 461
Cdd:pfam00555  155 SIDELPPETNNEPIYESYSHRLSHVTFLSGKLGQLA---GSVPSFSWTHRSAD 204
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
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   684 LQDPNFRGINRQLDRGWRGSTDITIQGGDDVFKENCVTLLGTFD---ECYPTYLYQKIDESKLKAYTRYQLRGYIEDSQD 760
Cdd:pfam17997    1 LQNGDFEELYGFGKNGWTISNNITIQADNPIFKGHYLHMSGAKDidgTVFPTYIYQKIDESKLKPYTRYQVRGFVGSSKD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   761 LEIYLIRYNAKHETVNVPgtgslwplSAQSPI--GKCGEPNRCAPHLEwnpdldcscrDGEKCAHHSHHFSLDIDVGCTD 838
Cdd:pfam17997   81 LGLVVTRYGKEVNVVMNP--------EYNTPVtdGYTSDTCSCQPNLE----------KKHVVCHDYHQFKFHIDIGQLN 142
                          170       180       190
                   ....*....|....*....|....*....|
gi 388849893   839 LNEDLGVWVIFKIKTQDGHARLGNLEFLEE 868
Cdd:pfam17997  143 MSENIGIWVLFKISSPDGFATLDNLEVIEE 172
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
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893    48 SEFVPGAGFVL-GLVDIIWGIFG---PSQWDAFLV---QIEQLINQRIEEFARNQAISRLEGLSNLYQIYAESFREWEAD 120
Cdd:pfam03945    1 LSLIPFVGPVLsFIADLIWTHLIetdKSTPELFNSyrqMIQDLINNSLTQYDDNKLKALLQGCSLSLKDFRTHVKNLKAD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   121 PTNPALREEMRIQFNDM-NSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVLRDVSVFGQRWGFDAATINSRYNDLTRL 199
Cdd:pfam03945   81 PKNATLKSTVNTIYLNLeNDIPQKYLKDCRKEGYEAYELPLFVLMATMHLGLLKEGISNGKDWGISDSDVKIFIDKFNKW 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 388849893   200 IGNYTDHAVRWYNTGLERVWGPDS------RDWIRYNQFRRELTLTVLDIVSLFPNYD 251
Cdd:pfam03945  161 IVKYAEYCYTAYVKGLAKIQKESAnikdpvKQWNDLNDFRNFMILYVFDFVNLWWAFD 218
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
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388849893   616 DLERAQKAVNELFTSSNQIGLKTDVTDYHIDQVSNLVECLSDEfclDEKQELSEKVKHAKRLSDE 680
Cdd:pfam18449    2 QLQAATTAVNSLFTDDSHTALAAEVTQAEIDAAKKLVDKLPSS---KEKTKLLKDIKKAQALLDA 63
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
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 388849893   902 KEAKESVDALFVNSQYDQLQADTNIAMIHAADKRVHSI 939
Cdd:pfam18449    4 QAATTAVNSLFTDDSHTALAAEVTQAEIDAAKKLVDKL 41
 
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893  463 NNIIPSSQITQIPLTKSTNLGSGTSVVKGPGFTGGDILRRTSPGQIsTLRVNITAPLSQRYRVGIRYASTTNLQFHTSID 542
Cdd:cd04085     8 NNTIYPDKITQIPAVKAYSLGNGSSVIKGPGFTGGDLVKLTSNGGG-SLKVTVTNSLSQKYRIRIRYASNTNGTLSVSGG 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388849893  543 GRPINQGNFSATMSSGSNLQSGSFRTVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYIDRIEFVP 606
Cdd:cd04085    87 GTTTNSFNFPSTMSSGDNLTYNSFKYVEFPTTFTFNSSSSTIEITIQNSSSGGEVYIDKIEFIP 150
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
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   471 ITQIPLTKSTNLGSGTSVVKGPGFTGGDILR-RTSPGQISTLRVNITAPLSQRYRVGIRYASTTNLQFHTSIDGRPINQG 549
Cdd:pfam03944    1 ITQIPAVKAYNLGSGASVVKGPGFTGGDLLKlRNSGGLLGRIRVTVNAPLSQRYRIRIRYASTTDSQLSVNIGGSGGNQI 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388849893   550 NFSATMSSGSNLQ--SGSFRTVGFTTPFNFSNGSSV-FTLSAHVFNSGNEVYIDRIEFVPAE 608
Cdd:pfam03944   81 NFPSTMSGGDNLTlnYGSFQYVEFSTPFTFSENPEItLTLSITNFSSNGELYIDRIEFIPVN 142
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
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   259 TVSQLTREIYTNPVLENFDGSFRGSAQG---IEGSIRSPHLMDILNSITIYTDAHR---GEYYWSGHQIMASPVGFSgPE 332
Cdd:pfam00555    1 TKSELTREIYTDPVGFESPRGLNIYPTFsnlENALIRPPHLFDFLNSLTIYTNSSRnntGYNYWSGHRNRFSFTGGS-NI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   333 FTFPLYGTMGNAAPQQRIVAqLGQGVYRTLSSTLYRRPFNiginNQQLSVLDGTEFAY--GTSSNLPSAVYKKSG--TVD 408
Cdd:pfam00555   80 ISEPLYGNTTNAENPVTISF-TNRDIYRTLSNTINSIYGL----NNPINGVTKVDFYGynGTNSEISSQTYRNGGqyTID 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 388849893   409 SLDEIPPQNNNVPPRQGFSHRLSHVSMFRSGFSNSSvsiIRAPMFSWIHRSAE 461
Cdd:pfam00555  155 SIDELPPETNNEPIYESYSHRLSHVTFLSGKLGQLA---GSVPSFSWTHRSAD 204
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
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   684 LQDPNFRGINRQLDRGWRGSTDITIQGGDDVFKENCVTLLGTFD---ECYPTYLYQKIDESKLKAYTRYQLRGYIEDSQD 760
Cdd:pfam17997    1 LQNGDFEELYGFGKNGWTISNNITIQADNPIFKGHYLHMSGAKDidgTVFPTYIYQKIDESKLKPYTRYQVRGFVGSSKD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   761 LEIYLIRYNAKHETVNVPgtgslwplSAQSPI--GKCGEPNRCAPHLEwnpdldcscrDGEKCAHHSHHFSLDIDVGCTD 838
Cdd:pfam17997   81 LGLVVTRYGKEVNVVMNP--------EYNTPVtdGYTSDTCSCQPNLE----------KKHVVCHDYHQFKFHIDIGQLN 142
                          170       180       190
                   ....*....|....*....|....*....|
gi 388849893   839 LNEDLGVWVIFKIKTQDGHARLGNLEFLEE 868
Cdd:pfam17997  143 MSENIGIWVLFKISSPDGFATLDNLEVIEE 172
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
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893    48 SEFVPGAGFVL-GLVDIIWGIFG---PSQWDAFLV---QIEQLINQRIEEFARNQAISRLEGLSNLYQIYAESFREWEAD 120
Cdd:pfam03945    1 LSLIPFVGPVLsFIADLIWTHLIetdKSTPELFNSyrqMIQDLINNSLTQYDDNKLKALLQGCSLSLKDFRTHVKNLKAD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893   121 PTNPALREEMRIQFNDM-NSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVLRDVSVFGQRWGFDAATINSRYNDLTRL 199
Cdd:pfam03945   81 PKNATLKSTVNTIYLNLeNDIPQKYLKDCRKEGYEAYELPLFVLMATMHLGLLKEGISNGKDWGISDSDVKIFIDKFNKW 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 388849893   200 IGNYTDHAVRWYNTGLERVWGPDS------RDWIRYNQFRRELTLTVLDIVSLFPNYD 251
Cdd:pfam03945  161 IVKYAEYCYTAYVKGLAKIQKESAnikdpvKQWNDLNDFRNFMILYVFDFVNLWWAFD 218
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
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388849893   616 DLERAQKAVNELFTSSNQIGLKTDVTDYHIDQVSNLVECLSDEfclDEKQELSEKVKHAKRLSDE 680
Cdd:pfam18449    2 QLQAATTAVNSLFTDDSHTALAAEVTQAEIDAAKKLVDKLPSS---KEKTKLLKDIKKAQALLDA 63
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388849893  481 NLGSGTSVVKGPGFTGGDILRRTSPGQiSTLRVNITAPLSQRYRVGIRYAS-TTNLQFHTSIDGRPINQGNFSATmssgS 559
Cdd:cd02795     8 TLTGGTAVSTAAGASGGGYVIGFSSGG-DSVTFTVTVPKAGTYRLAVRYASpNGNGSRSVSLDGNGKLVGTITVP----S 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 388849893  560 NLQSGSFRTVGFTTPFNfSNGSSVFTLSAHVFNSGneVYIDRIEF 604
Cdd:cd02795    83 TGGWDTWGTASVSVNLP-DAGGHTLKIVGTGDNGG--ANIDYVVV 124
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
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 388849893   902 KEAKESVDALFVNSQYDQLQADTNIAMIHAADKRVHSI 939
Cdd:pfam18449    4 QAATTAVNSLFTDDSHTALAAEVTQAEIDAAKKLVDKL 41
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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