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Conserved domains on  [gi|13275532|emb|CAC34029|]
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unnamed protein product [synthetic construct]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bcl-2 TIGR00865
apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the ...
 21-253 1.21e-120

apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the apoptosis regulator, Bcl-X, and its homologues. Bcl-X is a dominant regulator of programmed cell death in mammalian cells. The long form (Bcl-X(L)) displays cell death repressor activity, but the short isoform (Bcl-X(S)) and the b-isoform (Bcl-Xb) promote cell death. Bcl-X(L), Bcl-X(S) and Bcl-Xb are three isoforms derived by alternative RNA splicing. Bcl-X(S) forms heterodimers with Bcl-2. Homologues of Bcl-X include the Bax (rat; 192 aas; spQ63690) and Bak (mouse; 208 aas; spO08734) proteins which also influence apoptosis. Using isolated mitochondria, recombinant Bax and Bak have been shown to induce Dy loss, swelling and cytochrome c release. All of these changes are dependent on Ca2+ and are prevented by cyclosporin A and bongkrekic acid, both of which are known to close permeability transition pores (megachannels). Coimmimoprecipitation studies revealed that Bax and Bak interact with VDAC to form permeability transition pores. Thus, even though they can form channels in artificial membranes at acidic pH, proapoptotic Bcl-2 family proteins (including Bax and Bak) probably induce the mitochondrial permeability transition and cytochrome c release by interacting with permeability transition pores, the most important component for pore fomation of which is VDAC. [Regulatory functions, Other]


:

Pssm-ID: 273308 [Multi-domain]  Cd Length: 213  Bit Score: 349.12  E-value: 1.21e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532    21 MSQSNRELVVDFLSYKLSQKGYSWSQFSDveenrteapegtesemetpSAINGNPSWHLADSPAVNGATAHSSSLDAREV 100
Cdd:TIGR00865   1 MAGSNRELVMKFISYKLSQRGGSWTAGEQ-------------------IMKNGAPLLHGFIQHRAGPMTGETPSEGPPQD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532   101 IPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQ 180
Cdd:TIGR00865  62 PPPSAVHQALRRAGDEFERRYRRAFSDMTSQLHITPFTARQSFFQVAAELFRDGVNWGRIVAFFSFGGALCVESVNKEMS 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13275532   181 VLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRwFLTGMTVAGVVLLGSLFSRK 253
Cdd:TIGR00865 142 ELVSRIAGWMTEYLNEHLHPWIQENGGWDGFVELYGNNAAQLFDFSWESFNT-LLTAGLVTAVLTLGAYMGRK 213
Diphtheria_R pfam01324
Diphtheria toxin, R domain; C-terminal receptor binding (R) domain - binds to cell surface ...
 257-410 7.59e-90

Diphtheria toxin, R domain; C-terminal receptor binding (R) domain - binds to cell surface receptor, permitting the toxin to enter the cell by receptor mediated endocytosis.


:

Pssm-ID: 396061  Cd Length: 167  Bit Score: 268.94  E-value: 7.59e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532   257 AAAHKTQPFLHDGYAVSWNTVEDSIIRTG------FQ-----GESGHDIKITAENTPLPIAGVLLPTIPGK-LDVNKSKT 324
Cdd:pfam01324   1 APGDKTQPALHDGLAAGWKTEEDAIIHIGspygmkFQrivlsAEEGHDIKITAENTPFPIAAVLLPAIDGKfLDINGPKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532   325 HISVNGRKIRMRCRAIDGDVTFCRPKSPVYVGNGVHANLHVAFHRSSSEKIHSNEISSDSIGVLGYQKTVDHTKVNS-KL 403
Cdd:pfam01324  81 FISQNGIKIPMACFAIDGDLAFCRPKRPIFLGNGSHANLHLAFHRNEHEKIHNGEIKNDSIDILGYQKIVDHKKINAnKL 160


                  ....*..
gi 13275532   404 SLFFEIK 410
Cdd:pfam01324 161 SLFFEID 167
 
Name Accession Description Interval E-value
bcl-2 TIGR00865
apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the ...
 21-253 1.21e-120

apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the apoptosis regulator, Bcl-X, and its homologues. Bcl-X is a dominant regulator of programmed cell death in mammalian cells. The long form (Bcl-X(L)) displays cell death repressor activity, but the short isoform (Bcl-X(S)) and the b-isoform (Bcl-Xb) promote cell death. Bcl-X(L), Bcl-X(S) and Bcl-Xb are three isoforms derived by alternative RNA splicing. Bcl-X(S) forms heterodimers with Bcl-2. Homologues of Bcl-X include the Bax (rat; 192 aas; spQ63690) and Bak (mouse; 208 aas; spO08734) proteins which also influence apoptosis. Using isolated mitochondria, recombinant Bax and Bak have been shown to induce Dy loss, swelling and cytochrome c release. All of these changes are dependent on Ca2+ and are prevented by cyclosporin A and bongkrekic acid, both of which are known to close permeability transition pores (megachannels). Coimmimoprecipitation studies revealed that Bax and Bak interact with VDAC to form permeability transition pores. Thus, even though they can form channels in artificial membranes at acidic pH, proapoptotic Bcl-2 family proteins (including Bax and Bak) probably induce the mitochondrial permeability transition and cytochrome c release by interacting with permeability transition pores, the most important component for pore fomation of which is VDAC. [Regulatory functions, Other]


Pssm-ID: 273308 [Multi-domain]  Cd Length: 213  Bit Score: 349.12  E-value: 1.21e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532    21 MSQSNRELVVDFLSYKLSQKGYSWSQFSDveenrteapegtesemetpSAINGNPSWHLADSPAVNGATAHSSSLDAREV 100
Cdd:TIGR00865   1 MAGSNRELVMKFISYKLSQRGGSWTAGEQ-------------------IMKNGAPLLHGFIQHRAGPMTGETPSEGPPQD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532   101 IPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQ 180
Cdd:TIGR00865  62 PPPSAVHQALRRAGDEFERRYRRAFSDMTSQLHITPFTARQSFFQVAAELFRDGVNWGRIVAFFSFGGALCVESVNKEMS 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13275532   181 VLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRwFLTGMTVAGVVLLGSLFSRK 253
Cdd:TIGR00865 142 ELVSRIAGWMTEYLNEHLHPWIQENGGWDGFVELYGNNAAQLFDFSWESFNT-LLTAGLVTAVLTLGAYMGRK 213
Diphtheria_R pfam01324
Diphtheria toxin, R domain; C-terminal receptor binding (R) domain - binds to cell surface ...
 257-410 7.59e-90

Diphtheria toxin, R domain; C-terminal receptor binding (R) domain - binds to cell surface receptor, permitting the toxin to enter the cell by receptor mediated endocytosis.


Pssm-ID: 396061  Cd Length: 167  Bit Score: 268.94  E-value: 7.59e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532   257 AAAHKTQPFLHDGYAVSWNTVEDSIIRTG------FQ-----GESGHDIKITAENTPLPIAGVLLPTIPGK-LDVNKSKT 324
Cdd:pfam01324   1 APGDKTQPALHDGLAAGWKTEEDAIIHIGspygmkFQrivlsAEEGHDIKITAENTPFPIAAVLLPAIDGKfLDINGPKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532   325 HISVNGRKIRMRCRAIDGDVTFCRPKSPVYVGNGVHANLHVAFHRSSSEKIHSNEISSDSIGVLGYQKTVDHTKVNS-KL 403
Cdd:pfam01324  81 FISQNGIKIPMACFAIDGDLAFCRPKRPIFLGNGSHANLHLAFHRNEHEKIHNGEIKNDSIDILGYQKIVDHKKINAnKL 160


                  ....*..
gi 13275532   404 SLFFEIK 410
Cdd:pfam01324 161 SLFFEID 167
Bcl-2_like cd06845
Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This ...
 101-214 1.10e-49

Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This alignment model spans what have been described as Bcl-2 homology regions BH1, BH2, BH3, and BH4. Many members of this family have an additional C-terminal transmembrane segment. Some homologous proteins, which are not included in this model, may miss either the BH4 (Bax, Bak) or the BH2 (Bcl-X(S)) region, and some appear to only share the BH3 region (Bik, Bim, Bad, Bid, Egl-1). This family is involved in the regulation of the outer mitochondrial membrane's permeability and in promoting or preventing the release of apoptogenic factors, which in turn may trigger apoptosis by activating caspases. Bcl-2 and the closely related Bcl-X(L) are anti-apoptotic key regulators of programmed cell death. They are assumed to function via heterodimeric protein-protein interactions, binding pro-apoptotic proteins such as Bad (BCL2-antagonist of cell death), Bid, and Bim, by specifically interacting with their BH3 regions. Interfering with this heterodimeric interaction via small-molecule inhibitors may prove effective in targeting various cancers. This family also includes the Caenorhabditis elegans Bcl-2 homolog CED-9, which binds to CED-4, the C. Elegans homolog of mammalian Apaf-1. Apaf-1, however, does not seem to be inhibited by Bcl-2 directly.


Pssm-ID: 132900 [Multi-domain]  Cd Length: 144  Bit Score: 164.81  E-value: 1.10e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532 101 IPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRD-GVNWGRIVAFFSFGGALCVESVDKEM 179
Cdd:cd06845  30 SPPSEVAETLRRVGDELEEKHRRLFENMCRQLNISPDNAYEVFQEVARELFEDgGINWGRIVALFAFGGRLAVKCVEQGL 109

                        90       100       110
                ....*....|....*....|....*....|....*
gi 13275532 180 QVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVEL 214
Cdd:cd06845 110 PELVRSIAEWTSDFLEENLADWIQENGGWDGFVEF 144
BCL smart00337
BCL (B-Cell lymphoma); contains BH1, BH2 regions; (BH1, BH2, (BH3 (one helix only)) and not ...
 110-208 1.76e-44

BCL (B-Cell lymphoma); contains BH1, BH2 regions; (BH1, BH2, (BH3 (one helix only)) and not BH4(one helix only)). Involved in apoptosis regulation


Pssm-ID: 214626  Cd Length: 100  Bit Score: 149.78  E-value: 1.76e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532    110 LREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDG-VNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAA 188
Cdd:smart00337   1 LRRVGDELNKRYERAFSSFSAQLHVTPGTAIELFGEVATELFSDGnINWGRVVALLSFGGALAVKLVQKEDPDLVSRLAS 80

                           90       100
                   ....*....|....*....|
gi 13275532    189 WMATYLNDHLEPWIQENGGW 208
Cdd:smart00337  81 WLSEFLRETLRSWIRENGGW 100
Bcl-2 pfam00452
Apoptosis regulator proteins, Bcl-2 family;
110-208 8.91e-39

Apoptosis regulator proteins, Bcl-2 family;


Pssm-ID: 459816  Cd Length: 101  Bit Score: 134.70  E-value: 8.91e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532   110 LREAGDEFELRYRRAFSDLTSQLHITPG-TAYQSFEQVVNELFRDG-VNWGRIVAFFSFGGALCVESVDKEMQVLVSRIA 187
Cdd:pfam00452   1 LRRLGDELERKHPELFQNMLNQLLLTPEdTAYELFREVADELFSDGvINWGRVVALFAFAGALAVKLVRQGHPELVRRLA 80

                          90       100
                  ....*....|....*....|.
gi 13275532   188 AWMATYLNDHLEPWIQENGGW 208
Cdd:pfam00452  81 EWLVDYLEERLADWIIQQGGW 101
PHA03159 PHA03159
hypothetical protein; Provisional
 156-250 1.18e-03

hypothetical protein; Provisional


Pssm-ID: 165430  Cd Length: 160  Bit Score: 39.22  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532  156 NWGRIVAFFSFGGALcVESVDKEMQ-VLVSRIAAWMATYLNDHlepWIQENGGWDTFVELygnnaaAESRKGQERFN-RW 233
Cdd:PHA03159  72 NWGKVVAMISFSAAA-LQTIDEDYKcVATSMLSSYIAKSVGAN---WFIDHGGEKGLVEF------CDSILPKNNFNfLN 141

                         90
                 ....*....|....*..
gi 13275532  234 FLTGMTVAGVVLLGSLF 250
Cdd:PHA03159 142 FLLPAILAGIILIGTLL 158
 
Name Accession Description Interval E-value
bcl-2 TIGR00865
apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the ...
 21-253 1.21e-120

apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the apoptosis regulator, Bcl-X, and its homologues. Bcl-X is a dominant regulator of programmed cell death in mammalian cells. The long form (Bcl-X(L)) displays cell death repressor activity, but the short isoform (Bcl-X(S)) and the b-isoform (Bcl-Xb) promote cell death. Bcl-X(L), Bcl-X(S) and Bcl-Xb are three isoforms derived by alternative RNA splicing. Bcl-X(S) forms heterodimers with Bcl-2. Homologues of Bcl-X include the Bax (rat; 192 aas; spQ63690) and Bak (mouse; 208 aas; spO08734) proteins which also influence apoptosis. Using isolated mitochondria, recombinant Bax and Bak have been shown to induce Dy loss, swelling and cytochrome c release. All of these changes are dependent on Ca2+ and are prevented by cyclosporin A and bongkrekic acid, both of which are known to close permeability transition pores (megachannels). Coimmimoprecipitation studies revealed that Bax and Bak interact with VDAC to form permeability transition pores. Thus, even though they can form channels in artificial membranes at acidic pH, proapoptotic Bcl-2 family proteins (including Bax and Bak) probably induce the mitochondrial permeability transition and cytochrome c release by interacting with permeability transition pores, the most important component for pore fomation of which is VDAC. [Regulatory functions, Other]


Pssm-ID: 273308 [Multi-domain]  Cd Length: 213  Bit Score: 349.12  E-value: 1.21e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532    21 MSQSNRELVVDFLSYKLSQKGYSWSQFSDveenrteapegtesemetpSAINGNPSWHLADSPAVNGATAHSSSLDAREV 100
Cdd:TIGR00865   1 MAGSNRELVMKFISYKLSQRGGSWTAGEQ-------------------IMKNGAPLLHGFIQHRAGPMTGETPSEGPPQD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532   101 IPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQ 180
Cdd:TIGR00865  62 PPPSAVHQALRRAGDEFERRYRRAFSDMTSQLHITPFTARQSFFQVAAELFRDGVNWGRIVAFFSFGGALCVESVNKEMS 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13275532   181 VLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRwFLTGMTVAGVVLLGSLFSRK 253
Cdd:TIGR00865 142 ELVSRIAGWMTEYLNEHLHPWIQENGGWDGFVELYGNNAAQLFDFSWESFNT-LLTAGLVTAVLTLGAYMGRK 213
Diphtheria_R pfam01324
Diphtheria toxin, R domain; C-terminal receptor binding (R) domain - binds to cell surface ...
 257-410 7.59e-90

Diphtheria toxin, R domain; C-terminal receptor binding (R) domain - binds to cell surface receptor, permitting the toxin to enter the cell by receptor mediated endocytosis.


Pssm-ID: 396061  Cd Length: 167  Bit Score: 268.94  E-value: 7.59e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532   257 AAAHKTQPFLHDGYAVSWNTVEDSIIRTG------FQ-----GESGHDIKITAENTPLPIAGVLLPTIPGK-LDVNKSKT 324
Cdd:pfam01324   1 APGDKTQPALHDGLAAGWKTEEDAIIHIGspygmkFQrivlsAEEGHDIKITAENTPFPIAAVLLPAIDGKfLDINGPKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532   325 HISVNGRKIRMRCRAIDGDVTFCRPKSPVYVGNGVHANLHVAFHRSSSEKIHSNEISSDSIGVLGYQKTVDHTKVNS-KL 403
Cdd:pfam01324  81 FISQNGIKIPMACFAIDGDLAFCRPKRPIFLGNGSHANLHLAFHRNEHEKIHNGEIKNDSIDILGYQKIVDHKKINAnKL 160


                  ....*..
gi 13275532   404 SLFFEIK 410
Cdd:pfam01324 161 SLFFEID 167
Bcl-2_like cd06845
Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This ...
 101-214 1.10e-49

Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This alignment model spans what have been described as Bcl-2 homology regions BH1, BH2, BH3, and BH4. Many members of this family have an additional C-terminal transmembrane segment. Some homologous proteins, which are not included in this model, may miss either the BH4 (Bax, Bak) or the BH2 (Bcl-X(S)) region, and some appear to only share the BH3 region (Bik, Bim, Bad, Bid, Egl-1). This family is involved in the regulation of the outer mitochondrial membrane's permeability and in promoting or preventing the release of apoptogenic factors, which in turn may trigger apoptosis by activating caspases. Bcl-2 and the closely related Bcl-X(L) are anti-apoptotic key regulators of programmed cell death. They are assumed to function via heterodimeric protein-protein interactions, binding pro-apoptotic proteins such as Bad (BCL2-antagonist of cell death), Bid, and Bim, by specifically interacting with their BH3 regions. Interfering with this heterodimeric interaction via small-molecule inhibitors may prove effective in targeting various cancers. This family also includes the Caenorhabditis elegans Bcl-2 homolog CED-9, which binds to CED-4, the C. Elegans homolog of mammalian Apaf-1. Apaf-1, however, does not seem to be inhibited by Bcl-2 directly.


Pssm-ID: 132900 [Multi-domain]  Cd Length: 144  Bit Score: 164.81  E-value: 1.10e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532 101 IPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRD-GVNWGRIVAFFSFGGALCVESVDKEM 179
Cdd:cd06845  30 SPPSEVAETLRRVGDELEEKHRRLFENMCRQLNISPDNAYEVFQEVARELFEDgGINWGRIVALFAFGGRLAVKCVEQGL 109

                        90       100       110
                ....*....|....*....|....*....|....*
gi 13275532 180 QVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVEL 214
Cdd:cd06845 110 PELVRSIAEWTSDFLEENLADWIQENGGWDGFVEF 144
BCL smart00337
BCL (B-Cell lymphoma); contains BH1, BH2 regions; (BH1, BH2, (BH3 (one helix only)) and not ...
 110-208 1.76e-44

BCL (B-Cell lymphoma); contains BH1, BH2 regions; (BH1, BH2, (BH3 (one helix only)) and not BH4(one helix only)). Involved in apoptosis regulation


Pssm-ID: 214626  Cd Length: 100  Bit Score: 149.78  E-value: 1.76e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532    110 LREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDG-VNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAA 188
Cdd:smart00337   1 LRRVGDELNKRYERAFSSFSAQLHVTPGTAIELFGEVATELFSDGnINWGRVVALLSFGGALAVKLVQKEDPDLVSRLAS 80

                           90       100
                   ....*....|....*....|
gi 13275532    189 WMATYLNDHLEPWIQENGGW 208
Cdd:smart00337  81 WLSEFLRETLRSWIRENGGW 100
Bcl-2 pfam00452
Apoptosis regulator proteins, Bcl-2 family;
110-208 8.91e-39

Apoptosis regulator proteins, Bcl-2 family;


Pssm-ID: 459816  Cd Length: 101  Bit Score: 134.70  E-value: 8.91e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532   110 LREAGDEFELRYRRAFSDLTSQLHITPG-TAYQSFEQVVNELFRDG-VNWGRIVAFFSFGGALCVESVDKEMQVLVSRIA 187
Cdd:pfam00452   1 LRRLGDELERKHPELFQNMLNQLLLTPEdTAYELFREVADELFSDGvINWGRVVALFAFAGALAVKLVRQGHPELVRRLA 80

                          90       100
                  ....*....|....*....|.
gi 13275532   188 AWMATYLNDHLEPWIQENGGW 208
Cdd:pfam00452  81 EWLVDYLEERLADWIIQQGGW 101
BH4 smart00265
BH4 Bcl-2 homology region 4;
21-47 9.94e-10

BH4 Bcl-2 homology region 4;


Pssm-ID: 128561  Cd Length: 27  Bit Score: 53.43  E-value: 9.94e-10
                           10        20
                   ....*....|....*....|....*..
gi 13275532     21 MSQSNRELVVDFLSYKLSQKGYSWSQF 47
Cdd:smart00265   1 SRLDNRELVVDYVTYKLSQNGYEWDAG 27
BH4 pfam02180
Bcl-2 homology region 4;
22-46 3.60e-09

Bcl-2 homology region 4;


Pssm-ID: 426639  Cd Length: 25  Bit Score: 51.80  E-value: 3.60e-09
                          10        20
                  ....*....|....*....|....*
gi 13275532    22 SQSNRELVVDFLSYKLSQKGYSWSQ 46
Cdd:pfam02180   1 RLDNRELVVDYVSYKLSQRGYEWEH 25
PHA03159 PHA03159
hypothetical protein; Provisional
 156-250 1.18e-03

hypothetical protein; Provisional


Pssm-ID: 165430  Cd Length: 160  Bit Score: 39.22  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13275532  156 NWGRIVAFFSFGGALcVESVDKEMQ-VLVSRIAAWMATYLNDHlepWIQENGGWDTFVELygnnaaAESRKGQERFN-RW 233
Cdd:PHA03159  72 NWGKVVAMISFSAAA-LQTIDEDYKcVATSMLSSYIAKSVGAN---WFIDHGGEKGLVEF------CDSILPKNNFNfLN 141

                         90
                 ....*....|....*..
gi 13275532  234 FLTGMTVAGVVLLGSLF 250
Cdd:PHA03159 142 FLLPAILAGIILIGTLL 158
 
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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