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Conserved domains on  [gi|1958649290|ref|XP_006230958|]
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bcl2-associated agonist of cell death isoform X1 [Rattus norvegicus]

Protein Classification

Bcl-2_BAD domain-containing protein( domain architecture ID 10565048)

Bcl-2_BAD domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bcl-2_BAD pfam10514
Pro-apoptotic Bcl-2 protein, BAD; BAD is a Bcl-2 homology domain 3 (BH3)-only pro-apoptotic ...
 73-195 8.08e-61

Pro-apoptotic Bcl-2 protein, BAD; BAD is a Bcl-2 homology domain 3 (BH3)-only pro-apoptotic member of the Bcl-2 protein family that is regulated by phosphorylation in response to survival factors. Binding of BAD to mitochondria is thought to be exclusively mediated by its BH3 domain. Membrane localization of BAD mediates membrane translocation of Bcl-XL. The C-terminal part of BAD is sufficient for membrane binding. There are two segments with differing lipid-binding preferences, LBD1 and LBD2, that are responsible for this binding: (i) LBD1 located in the proximity of the BH3 domain (amino acids 122-131) and (ii) LBD2, the putative C-terminal alpha-helix-5. Phosphorylation-regulated 14-3-3 protein binding may expose the cholesterol-preferring LBD1 and bury the LBD2, thereby mediating translocation of BAD to raft-like micro-domains.


:

Pssm-ID: 402236  Cd Length: 166  Bit Score: 189.06  E-value: 8.08e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649290  73 MFQIPEFEPSEQEDASTTDRGLGPSLTEDQPGP----YLAPGLLGSIVQQQpGQAANNSHHGGAGTMETRSRHSSYPAGT 148
Cdd:pfam10514   1 MFQIPEFEPSEQEDSSPADRGLGPSPTGDRPGPsgpsRAAPGLLGDISHQQ-GQPTSSSHHGGAGAVETRSRHSSYPAGT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958649290 149 EEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKG 195
Cdd:pfam10514  80 EEDEGMEEEPSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFHGSFKG 126
 
Name Accession Description Interval E-value
Bcl-2_BAD pfam10514
Pro-apoptotic Bcl-2 protein, BAD; BAD is a Bcl-2 homology domain 3 (BH3)-only pro-apoptotic ...
 73-195 8.08e-61

Pro-apoptotic Bcl-2 protein, BAD; BAD is a Bcl-2 homology domain 3 (BH3)-only pro-apoptotic member of the Bcl-2 protein family that is regulated by phosphorylation in response to survival factors. Binding of BAD to mitochondria is thought to be exclusively mediated by its BH3 domain. Membrane localization of BAD mediates membrane translocation of Bcl-XL. The C-terminal part of BAD is sufficient for membrane binding. There are two segments with differing lipid-binding preferences, LBD1 and LBD2, that are responsible for this binding: (i) LBD1 located in the proximity of the BH3 domain (amino acids 122-131) and (ii) LBD2, the putative C-terminal alpha-helix-5. Phosphorylation-regulated 14-3-3 protein binding may expose the cholesterol-preferring LBD1 and bury the LBD2, thereby mediating translocation of BAD to raft-like micro-domains.


Pssm-ID: 402236  Cd Length: 166  Bit Score: 189.06  E-value: 8.08e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649290  73 MFQIPEFEPSEQEDASTTDRGLGPSLTEDQPGP----YLAPGLLGSIVQQQpGQAANNSHHGGAGTMETRSRHSSYPAGT 148
Cdd:pfam10514   1 MFQIPEFEPSEQEDSSPADRGLGPSPTGDRPGPsgpsRAAPGLLGDISHQQ-GQPTSSSHHGGAGAVETRSRHSSYPAGT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958649290 149 EEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKG 195
Cdd:pfam10514  80 EEDEGMEEEPSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFHGSFKG 126
 
Name Accession Description Interval E-value
Bcl-2_BAD pfam10514
Pro-apoptotic Bcl-2 protein, BAD; BAD is a Bcl-2 homology domain 3 (BH3)-only pro-apoptotic ...
 73-195 8.08e-61

Pro-apoptotic Bcl-2 protein, BAD; BAD is a Bcl-2 homology domain 3 (BH3)-only pro-apoptotic member of the Bcl-2 protein family that is regulated by phosphorylation in response to survival factors. Binding of BAD to mitochondria is thought to be exclusively mediated by its BH3 domain. Membrane localization of BAD mediates membrane translocation of Bcl-XL. The C-terminal part of BAD is sufficient for membrane binding. There are two segments with differing lipid-binding preferences, LBD1 and LBD2, that are responsible for this binding: (i) LBD1 located in the proximity of the BH3 domain (amino acids 122-131) and (ii) LBD2, the putative C-terminal alpha-helix-5. Phosphorylation-regulated 14-3-3 protein binding may expose the cholesterol-preferring LBD1 and bury the LBD2, thereby mediating translocation of BAD to raft-like micro-domains.


Pssm-ID: 402236  Cd Length: 166  Bit Score: 189.06  E-value: 8.08e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649290  73 MFQIPEFEPSEQEDASTTDRGLGPSLTEDQPGP----YLAPGLLGSIVQQQpGQAANNSHHGGAGTMETRSRHSSYPAGT 148
Cdd:pfam10514   1 MFQIPEFEPSEQEDSSPADRGLGPSPTGDRPGPsgpsRAAPGLLGDISHQQ-GQPTSSSHHGGAGAVETRSRHSSYPAGT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958649290 149 EEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKG 195
Cdd:pfam10514  80 EEDEGMEEEPSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFHGSFKG 126
 
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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