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Conserved domains on  [gi|674573794|emb|CDS40716|]
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EGFP:Bcl2 fusion protein [Echinococcus multilocularis]

Protein Classification

Bcl-2 domain-containing protein( domain architecture ID 10452259)

Bcl-2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bcl-2 pfam00452
Apoptosis regulator proteins, Bcl-2 family;
74-176 7.22e-21

Apoptosis regulator proteins, Bcl-2 family;


:

Pssm-ID: 459816  Cd Length: 101  Bit Score: 82.69  E-value: 7.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674573794   74 MRCLverATEFEKAFLPRFENRQALLLKRPENAELD-FKQTLEAIWSDGLVNWGRFLAYISFVGAYCLSALNAGMVYEIR 152
Cdd:pfam00452   1 LRRL---GDELERKHPELFQNMLNQLLLTPEDTAYElFREVADELFSDGVINWGRVVALFAFAGALAVKLVRQGHPELVR 77

                          90       100
                  ....*....|....*....|....
gi 674573794  153 FLVETAVDKLEKRIGGWIKRNGGW 176
Cdd:pfam00452  78 RLAEWLVDYLEERLADWIIQQGGW 101
 
Name Accession Description Interval E-value
Bcl-2 pfam00452
Apoptosis regulator proteins, Bcl-2 family;
74-176 7.22e-21

Apoptosis regulator proteins, Bcl-2 family;


Pssm-ID: 459816  Cd Length: 101  Bit Score: 82.69  E-value: 7.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674573794   74 MRCLverATEFEKAFLPRFENRQALLLKRPENAELD-FKQTLEAIWSDGLVNWGRFLAYISFVGAYCLSALNAGMVYEIR 152
Cdd:pfam00452   1 LRRL---GDELERKHPELFQNMLNQLLLTPEDTAYElFREVADELFSDGVINWGRVVALFAFAGALAVKLVRQGHPELVR 77

                          90       100
                  ....*....|....*....|....
gi 674573794  153 FLVETAVDKLEKRIGGWIKRNGGW 176
Cdd:pfam00452  78 RLAEWLVDYLEERLADWIIQQGGW 101
BCL smart00337
BCL (B-Cell lymphoma); contains BH1, BH2 regions; (BH1, BH2, (BH3 (one helix only)) and not ...
 81-176 4.62e-16

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: 70.04  E-value: 4.62e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674573794    81 ATEFEKAFLPRFENRQALLLKRPENAELDFKQTLEAIWSDGLVNWGRFLAYISFVGAYCLSALNAGMVYEIRFLVETAVD 160
Cdd:smart00337   5 GDELNKRYERAFSSFSAQLHVTPGTAIELFGEVATELFSDGNINWGRVVALLSFGGALAVKLVQKEDPDLVSRLASWLSE 84

                           90
                   ....*....|....*.
gi 674573794   161 KLEKRIGGWIKRNGGW 176
Cdd:smart00337  85 FLRETLRSWIRENGGW 100
bcl-2 TIGR00865
apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the ...
 76-176 1.04e-15

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: 72.16  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674573794   76 CLVERATEFEKAFLPRFENRQALLLKRPENAELDFKQTLEAIWSDGlVNWGRFLAYISFVGAYCLSALNAGMVYEIRFLV 155
Cdd:TIGR00865  70 ALRRAGDEFERRYRRAFSDMTSQLHITPFTARQSFFQVAAELFRDG-VNWGRIVAFFSFGGALCVESVNKEMSELVSRIA 148

                          90       100
                  ....*....|....*....|.
gi 674573794  156 ETAVDKLEKRIGGWIKRNGGW 176
Cdd:TIGR00865 149 GWMTEYLNEHLHPWIQENGGW 169
Bcl-2_like cd06845
Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This ...
 75-176 2.54e-14

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: 66.59  E-value: 2.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674573794  75 RCLVERATEFEKAFLPRFENRQALLLKRPENAELDFKQTLEAIWSDGLVNWGRFLAYISFVGAYCLSALNAGMVYEIRFL 154
Cdd:cd06845   37 ETLRRVGDELEEKHRRLFENMCRQLNISPDNAYEVFQEVARELFEDGGINWGRIVALFAFGGRLAVKCVEQGLPELVRSI 116

                         90       100
                 ....*....|....*....|..
gi 674573794 155 VETAVDKLEKRIGGWIKRNGGW 176
Cdd:cd06845  117 AEWTSDFLEENLADWIQENGGW 138
 
Name Accession Description Interval E-value
Bcl-2 pfam00452
Apoptosis regulator proteins, Bcl-2 family;
74-176 7.22e-21

Apoptosis regulator proteins, Bcl-2 family;


Pssm-ID: 459816  Cd Length: 101  Bit Score: 82.69  E-value: 7.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674573794   74 MRCLverATEFEKAFLPRFENRQALLLKRPENAELD-FKQTLEAIWSDGLVNWGRFLAYISFVGAYCLSALNAGMVYEIR 152
Cdd:pfam00452   1 LRRL---GDELERKHPELFQNMLNQLLLTPEDTAYElFREVADELFSDGVINWGRVVALFAFAGALAVKLVRQGHPELVR 77

                          90       100
                  ....*....|....*....|....
gi 674573794  153 FLVETAVDKLEKRIGGWIKRNGGW 176
Cdd:pfam00452  78 RLAEWLVDYLEERLADWIIQQGGW 101
BCL smart00337
BCL (B-Cell lymphoma); contains BH1, BH2 regions; (BH1, BH2, (BH3 (one helix only)) and not ...
 81-176 4.62e-16

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: 70.04  E-value: 4.62e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674573794    81 ATEFEKAFLPRFENRQALLLKRPENAELDFKQTLEAIWSDGLVNWGRFLAYISFVGAYCLSALNAGMVYEIRFLVETAVD 160
Cdd:smart00337   5 GDELNKRYERAFSSFSAQLHVTPGTAIELFGEVATELFSDGNINWGRVVALLSFGGALAVKLVQKEDPDLVSRLASWLSE 84

                           90
                   ....*....|....*.
gi 674573794   161 KLEKRIGGWIKRNGGW 176
Cdd:smart00337  85 FLRETLRSWIRENGGW 100
bcl-2 TIGR00865
apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the ...
 76-176 1.04e-15

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: 72.16  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674573794   76 CLVERATEFEKAFLPRFENRQALLLKRPENAELDFKQTLEAIWSDGlVNWGRFLAYISFVGAYCLSALNAGMVYEIRFLV 155
Cdd:TIGR00865  70 ALRRAGDEFERRYRRAFSDMTSQLHITPFTARQSFFQVAAELFRDG-VNWGRIVAFFSFGGALCVESVNKEMSELVSRIA 148

                          90       100
                  ....*....|....*....|.
gi 674573794  156 ETAVDKLEKRIGGWIKRNGGW 176
Cdd:TIGR00865 149 GWMTEYLNEHLHPWIQENGGW 169
Bcl-2_like cd06845
Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This ...
 75-176 2.54e-14

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: 66.59  E-value: 2.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674573794  75 RCLVERATEFEKAFLPRFENRQALLLKRPENAELDFKQTLEAIWSDGLVNWGRFLAYISFVGAYCLSALNAGMVYEIRFL 154
Cdd:cd06845   37 ETLRRVGDELEEKHRRLFENMCRQLNISPDNAYEVFQEVARELFEDGGINWGRIVALFAFGGRLAVKCVEQGLPELVRSI 116

                         90       100
                 ....*....|....*....|..
gi 674573794 155 VETAVDKLEKRIGGWIKRNGGW 176
Cdd:cd06845  117 AEWTSDFLEENLADWIQENGGW 138
 
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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