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Conserved domains on  [gi|568940399|ref|XP_006505472|]
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BH3-interacting domain death agonist isoform X1 [Mus musculus]

Protein Classification

BID domain-containing protein( domain architecture ID 10533953)

BID domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BID pfam06393
BH3 interacting domain (BID); BID is a member of the BCL-2 superfamily of proteins are key ...
 3-192 3.43e-98

BH3 interacting domain (BID); BID is a member of the BCL-2 superfamily of proteins are key regulators of programmed cell death, hence this family is related to pfam00452. BID is a pro-apoptotic member of the Bcl-2 superfamily and as such posses the ability to target intracellular membranes and contains the BH3 death domain. The activity of BID is regulated by a Caspase 8-mediated cleavage event, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, which causes a change of cellular localization.


:

Pssm-ID: 428916  Cd Length: 191  Bit Score: 282.33  E-value: 3.43e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940399    3 SEVSNGSGLGAEHITDLLVFGFLQSS--GCTRQELEVLGRELPVQAYWEADLEDELQTDGSQASRSFNqGRIEPDSESQE 80
Cdd:pfam06393   1 EKVSNGSGLRDELITNLLVFGFLQSSnsCFFHEELELLGEELPVTALLEEDDDDELQTDGNRSSHFQE-GREEDDSESQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940399   81 EIIHNIARHLAQIGDEMDHNIQPTLVRQLAAQFMNGSLSEEDKRNCLAKALDEVKTAFPRDMENDKAMLIMTMLLAKKVA 160
Cdd:pfam06393  80 EIIRNIARQLAQIGDEMDSSIQPLVVNLLAQQFMNSLLSEEDRRHCLAAALEVLMTTYPDDMEQEKTMLVLTMLLAKKVA 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568940399  161 SHAPSLLRDVFHTTVNFINQNLFSYVRNLVRN 192
Cdd:pfam06393 160 DHTPSLLRDVFHTTVNFINQNLLTYVRNLVRN 191
 
Name Accession Description Interval E-value
BID pfam06393
BH3 interacting domain (BID); BID is a member of the BCL-2 superfamily of proteins are key ...
 3-192 3.43e-98

BH3 interacting domain (BID); BID is a member of the BCL-2 superfamily of proteins are key regulators of programmed cell death, hence this family is related to pfam00452. BID is a pro-apoptotic member of the Bcl-2 superfamily and as such posses the ability to target intracellular membranes and contains the BH3 death domain. The activity of BID is regulated by a Caspase 8-mediated cleavage event, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, which causes a change of cellular localization.


Pssm-ID: 428916  Cd Length: 191  Bit Score: 282.33  E-value: 3.43e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940399    3 SEVSNGSGLGAEHITDLLVFGFLQSS--GCTRQELEVLGRELPVQAYWEADLEDELQTDGSQASRSFNqGRIEPDSESQE 80
Cdd:pfam06393   1 EKVSNGSGLRDELITNLLVFGFLQSSnsCFFHEELELLGEELPVTALLEEDDDDELQTDGNRSSHFQE-GREEDDSESQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940399   81 EIIHNIARHLAQIGDEMDHNIQPTLVRQLAAQFMNGSLSEEDKRNCLAKALDEVKTAFPRDMENDKAMLIMTMLLAKKVA 160
Cdd:pfam06393  80 EIIRNIARQLAQIGDEMDSSIQPLVVNLLAQQFMNSLLSEEDRRHCLAAALEVLMTTYPDDMEQEKTMLVLTMLLAKKVA 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568940399  161 SHAPSLLRDVFHTTVNFINQNLFSYVRNLVRN 192
Cdd:pfam06393 160 DHTPSLLRDVFHTTVNFINQNLLTYVRNLVRN 191
 
Name Accession Description Interval E-value
BID pfam06393
BH3 interacting domain (BID); BID is a member of the BCL-2 superfamily of proteins are key ...
 3-192 3.43e-98

BH3 interacting domain (BID); BID is a member of the BCL-2 superfamily of proteins are key regulators of programmed cell death, hence this family is related to pfam00452. BID is a pro-apoptotic member of the Bcl-2 superfamily and as such posses the ability to target intracellular membranes and contains the BH3 death domain. The activity of BID is regulated by a Caspase 8-mediated cleavage event, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, which causes a change of cellular localization.


Pssm-ID: 428916  Cd Length: 191  Bit Score: 282.33  E-value: 3.43e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940399    3 SEVSNGSGLGAEHITDLLVFGFLQSS--GCTRQELEVLGRELPVQAYWEADLEDELQTDGSQASRSFNqGRIEPDSESQE 80
Cdd:pfam06393   1 EKVSNGSGLRDELITNLLVFGFLQSSnsCFFHEELELLGEELPVTALLEEDDDDELQTDGNRSSHFQE-GREEDDSESQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940399   81 EIIHNIARHLAQIGDEMDHNIQPTLVRQLAAQFMNGSLSEEDKRNCLAKALDEVKTAFPRDMENDKAMLIMTMLLAKKVA 160
Cdd:pfam06393  80 EIIRNIARQLAQIGDEMDSSIQPLVVNLLAQQFMNSLLSEEDRRHCLAAALEVLMTTYPDDMEQEKTMLVLTMLLAKKVA 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568940399  161 SHAPSLLRDVFHTTVNFINQNLFSYVRNLVRN 192
Cdd:pfam06393 160 DHTPSLLRDVFHTTVNFINQNLLTYVRNLVRN 191
 
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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