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Conserved domains on  [gi|347300410|ref|NP_001231496|]
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BH3-interacting domain death agonist isoform 2 [Homo sapiens]

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 5.65e-91

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: 264.23  E-value: 5.65e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347300410    3 CEVNNGSSLRDECITNLLVFGFLQSCSDNSFRRELDALGHELPVLAPQWEGY-DELQTDGNRSSHSRLGRIEADSESQED 81
Cdd:pfam06393   1 EKVSNGSGLRDELITNLLVFGFLQSSNSCFFHEELELLGEELPVTALLEEDDdDELQTDGNRSSHFQEGREEDDSESQEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347300410   82 IIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSRSEEDRNRDLATALEQLLQAYPRDMEKEKTMLVLALLLAKKVAS 161
Cdd:pfam06393  81 IIRNIARQLAQIGDEMDSSIQPLVVNLLAQQFMNSLLSEEDRRHCLAAALEVLMTTYPDDMEQEKTMLVLTMLLAKKVAD 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 347300410  162 HTPSLLRDVFHTTVNFINQNLRTYVRSLARN 192
Cdd:pfam06393 161 HTPSLLRDVFHTTVNFINQNLLTYVRNLVRN 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 5.65e-91

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: 264.23  E-value: 5.65e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347300410    3 CEVNNGSSLRDECITNLLVFGFLQSCSDNSFRRELDALGHELPVLAPQWEGY-DELQTDGNRSSHSRLGRIEADSESQED 81
Cdd:pfam06393   1 EKVSNGSGLRDELITNLLVFGFLQSSNSCFFHEELELLGEELPVTALLEEDDdDELQTDGNRSSHFQEGREEDDSESQEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347300410   82 IIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSRSEEDRNRDLATALEQLLQAYPRDMEKEKTMLVLALLLAKKVAS 161
Cdd:pfam06393  81 IIRNIARQLAQIGDEMDSSIQPLVVNLLAQQFMNSLLSEEDRRHCLAAALEVLMTTYPDDMEQEKTMLVLTMLLAKKVAD 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 347300410  162 HTPSLLRDVFHTTVNFINQNLRTYVRSLARN 192
Cdd:pfam06393 161 HTPSLLRDVFHTTVNFINQNLLTYVRNLVRN 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 5.65e-91

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: 264.23  E-value: 5.65e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347300410    3 CEVNNGSSLRDECITNLLVFGFLQSCSDNSFRRELDALGHELPVLAPQWEGY-DELQTDGNRSSHSRLGRIEADSESQED 81
Cdd:pfam06393   1 EKVSNGSGLRDELITNLLVFGFLQSSNSCFFHEELELLGEELPVTALLEEDDdDELQTDGNRSSHFQEGREEDDSESQEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347300410   82 IIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSRSEEDRNRDLATALEQLLQAYPRDMEKEKTMLVLALLLAKKVAS 161
Cdd:pfam06393  81 IIRNIARQLAQIGDEMDSSIQPLVVNLLAQQFMNSLLSEEDRRHCLAAALEVLMTTYPDDMEQEKTMLVLTMLLAKKVAD 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 347300410  162 HTPSLLRDVFHTTVNFINQNLRTYVRSLARN 192
Cdd:pfam06393 161 HTPSLLRDVFHTTVNFINQNLLTYVRNLVRN 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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