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Conserved domains on  [gi|323362967|ref|NP_001191039|]
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bcl-2-like protein 11 isoform 15 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bim_N super family cl06026
Bim protein N-terminus; This family represents the N-terminal region of several mammal ...
 4-40 1.03e-10

Bim protein N-terminus; This family represents the N-terminal region of several mammal specific Bim proteins. The Bim protein is one of the BH3-only proteins, members of the Bcl-2 family that have only one of the Bcl-2 homology regions, BH3. BH3-only proteins are essential initiators of apoptotic cell death.


The actual alignment was detected with superfamily member pfam06773:

Pssm-ID: 429111  Cd Length: 40  Bit Score: 51.24  E-value: 1.03e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 323362967   4 QPSDVSSECDREGRQLQPAERPPQ---LRPGAPTSLQTEP 40
Cdd:pfam06773  1 QPSDLSSECDREGGQLQPTERPHQhrpLRPGAPTSLQTPF 40
Bclx_interact super family cl07517
Bcl-x interacting, BH3 domain; This domain is a long alpha helix, required for interaction ...
 46-76 8.37e-06

Bcl-x interacting, BH3 domain; This domain is a long alpha helix, required for interaction with Bcl-x. It is found in BAM, Bim and Bcl2-like protein 11. This domain is also known as the BH3 domain between residues 146 and 161.


The actual alignment was detected with superfamily member pfam08945:

Pssm-ID: 462643  Cd Length: 38  Bit Score: 38.70  E-value: 8.37e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 323362967  46 QAEPADMRPEIWIAQELRRIGDEFNAYYARR 76
Cdd:pfam08945  6 ASPPEDRPPEIWIAQELRRIGDEFNSSYNPR 36
 
Name Accession Description Interval E-value
Bim_N pfam06773
Bim protein N-terminus; This family represents the N-terminal region of several mammal ...
 4-40 1.03e-10

Bim protein N-terminus; This family represents the N-terminal region of several mammal specific Bim proteins. The Bim protein is one of the BH3-only proteins, members of the Bcl-2 family that have only one of the Bcl-2 homology regions, BH3. BH3-only proteins are essential initiators of apoptotic cell death.


Pssm-ID: 429111  Cd Length: 40  Bit Score: 51.24  E-value: 1.03e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 323362967   4 QPSDVSSECDREGRQLQPAERPPQ---LRPGAPTSLQTEP 40
Cdd:pfam06773  1 QPSDLSSECDREGGQLQPTERPHQhrpLRPGAPTSLQTPF 40
Bclx_interact pfam08945
Bcl-x interacting, BH3 domain; This domain is a long alpha helix, required for interaction ...
 46-76 8.37e-06

Bcl-x interacting, BH3 domain; This domain is a long alpha helix, required for interaction with Bcl-x. It is found in BAM, Bim and Bcl2-like protein 11. This domain is also known as the BH3 domain between residues 146 and 161.


Pssm-ID: 462643  Cd Length: 38  Bit Score: 38.70  E-value: 8.37e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 323362967  46 QAEPADMRPEIWIAQELRRIGDEFNAYYARR 76
Cdd:pfam08945  6 ASPPEDRPPEIWIAQELRRIGDEFNSSYNPR 36
bcl-2 TIGR00865
apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the ...
 22-75 1.32e-03

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: 35.18  E-value: 1.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 323362967   22 AERPPQLRPGAPTSLQTEPQASMRQAEPAdmrpeiwIAQELRRIGDEFNAYYAR 75
Cdd:TIGR00865  38 LHGFIQHRAGPMTGETPSEGPPQDPPPSA-------VHQALRRAGDEFERRYRR 84
 
Name Accession Description Interval E-value
Bim_N pfam06773
Bim protein N-terminus; This family represents the N-terminal region of several mammal ...
 4-40 1.03e-10

Bim protein N-terminus; This family represents the N-terminal region of several mammal specific Bim proteins. The Bim protein is one of the BH3-only proteins, members of the Bcl-2 family that have only one of the Bcl-2 homology regions, BH3. BH3-only proteins are essential initiators of apoptotic cell death.


Pssm-ID: 429111  Cd Length: 40  Bit Score: 51.24  E-value: 1.03e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 323362967   4 QPSDVSSECDREGRQLQPAERPPQ---LRPGAPTSLQTEP 40
Cdd:pfam06773  1 QPSDLSSECDREGGQLQPTERPHQhrpLRPGAPTSLQTPF 40
Bclx_interact pfam08945
Bcl-x interacting, BH3 domain; This domain is a long alpha helix, required for interaction ...
 46-76 8.37e-06

Bcl-x interacting, BH3 domain; This domain is a long alpha helix, required for interaction with Bcl-x. It is found in BAM, Bim and Bcl2-like protein 11. This domain is also known as the BH3 domain between residues 146 and 161.


Pssm-ID: 462643  Cd Length: 38  Bit Score: 38.70  E-value: 8.37e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 323362967  46 QAEPADMRPEIWIAQELRRIGDEFNAYYARR 76
Cdd:pfam08945  6 ASPPEDRPPEIWIAQELRRIGDEFNSSYNPR 36
bcl-2 TIGR00865
apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the ...
 22-75 1.32e-03

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: 35.18  E-value: 1.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 323362967   22 AERPPQLRPGAPTSLQTEPQASMRQAEPAdmrpeiwIAQELRRIGDEFNAYYAR 75
Cdd:TIGR00865  38 LHGFIQHRAGPMTGETPSEGPPQDPPPSA-------VHQALRRAGDEFERRYRR 84
 
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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