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Conserved domains on  [gi|768022751|ref|XP_011544421|]
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bcl-2-like protein 13 isoform X1 [Homo sapiens]

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;
128-224 1.29e-14

Apoptosis regulator proteins, Bcl-2 family;


:

Pssm-ID: 425690  Cd Length: 101  Bit Score: 69.60  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022751  128 LAHLGEKVSQELKEPLHKALQMLLSQPVT--YQAFRECTLEttVHASG---WNKILVPLVLLRQMLLELTRRGQ-EPLSA 201
Cdd:pfam00452   1 LRRLGDELERKHPEEFNRMLQQLLLTPEDtaYELFNEVADE--LFSDGvinWGRVVALFAFAGALAVKLVRQGHpELVRR 78
                          90       100
                  ....*....|....*....|...
gi 768022751  202 LLQFGVTYLEDYSAEYIIQQGGW 224
Cdd:pfam00452  79 LAEWLVDYLEERLADWIIQQGGW 101
 
Name Accession Description Interval E-value
Bcl-2 pfam00452
Apoptosis regulator proteins, Bcl-2 family;
128-224 1.29e-14

Apoptosis regulator proteins, Bcl-2 family;


Pssm-ID: 425690  Cd Length: 101  Bit Score: 69.60  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022751  128 LAHLGEKVSQELKEPLHKALQMLLSQPVT--YQAFRECTLEttVHASG---WNKILVPLVLLRQMLLELTRRGQ-EPLSA 201
Cdd:pfam00452   1 LRRLGDELERKHPEEFNRMLQQLLLTPEDtaYELFNEVADE--LFSDGvinWGRVVALFAFAGALAVKLVRQGHpELVRR 78
                          90       100
                  ....*....|....*....|...
gi 768022751  202 LLQFGVTYLEDYSAEYIIQQGGW 224
Cdd:pfam00452  79 LAEWLVDYLEERLADWIIQQGGW 101
Bcl-2_like cd06845
Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This ...
127-224 5.15e-03

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: 37.31  E-value: 5.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022751 127 CLAHLGEKVSQELKEPLHKALQML-LSQPVTYQAFREcTLETTVHASG--WNKILVPLVLLRQMLLELTRRGQEPL-SAL 202
Cdd:cd06845   38 TLRRVGDELEEKHRRLFENMCRQLnISPDNAYEVFQE-VARELFEDGGinWGRIVALFAFGGRLAVKCVEQGLPELvRSI 116
                         90       100
                 ....*....|....*....|..
gi 768022751 203 LQFGVTYLEDYSAEYIIQQGGW 224
Cdd:cd06845  117 AEWTSDFLEENLADWIQENGGW 138
 
Name Accession Description Interval E-value
Bcl-2 pfam00452
Apoptosis regulator proteins, Bcl-2 family;
128-224 1.29e-14

Apoptosis regulator proteins, Bcl-2 family;


Pssm-ID: 425690  Cd Length: 101  Bit Score: 69.60  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022751  128 LAHLGEKVSQELKEPLHKALQMLLSQPVT--YQAFRECTLEttVHASG---WNKILVPLVLLRQMLLELTRRGQ-EPLSA 201
Cdd:pfam00452   1 LRRLGDELERKHPEEFNRMLQQLLLTPEDtaYELFNEVADE--LFSDGvinWGRVVALFAFAGALAVKLVRQGHpELVRR 78
                          90       100
                  ....*....|....*....|...
gi 768022751  202 LLQFGVTYLEDYSAEYIIQQGGW 224
Cdd:pfam00452  79 LAEWLVDYLEERLADWIIQQGGW 101
Bcl-2_like cd06845
Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This ...
127-224 5.15e-03

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: 37.31  E-value: 5.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022751 127 CLAHLGEKVSQELKEPLHKALQML-LSQPVTYQAFREcTLETTVHASG--WNKILVPLVLLRQMLLELTRRGQEPL-SAL 202
Cdd:cd06845   38 TLRRVGDELEEKHRRLFENMCRQLnISPDNAYEVFQE-VARELFEDGGinWGRIVALFAFGGRLAVKCVEQGLPELvRSI 116
                         90       100
                 ....*....|....*....|..
gi 768022751 203 LQFGVTYLEDYSAEYIIQQGGW 224
Cdd:cd06845  117 AEWTSDFLEENLADWIQENGGW 138
 
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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