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Conserved domains on  [gi|1278156095|gb|ATW01295|]
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cystic fibrosis transmembrane conductance regulating, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CFTR_protein super family cl36858
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 1-118 3.11e-55

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


The actual alignment was detected with superfamily member TIGR01271:

Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 184.34  E-value: 3.11e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278156095    1 IVQKTPLQMNGIEED--SDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSvNQGQNIHRKTTAS 78
Cdd:TIGR01271  717 FVQMGPQKAQATTIEdaVREPSERKFSLVPEDEQGEESLPRGNQYHHGLQHQAQRRQSVLQLMTHS-NRGENRREQLQTS 795

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1278156095   79 TRKVSLAPQAN--LTELDIYSRRLSQETGLEISEEINEEDLK 118
Cdd:TIGR01271  796 FRKKSSITQQNelASELDIYSRRLSKDSVYEISEEINEEDLK 837
 
Name Accession Description Interval E-value
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 1-118 3.11e-55

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 184.34  E-value: 3.11e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278156095    1 IVQKTPLQMNGIEED--SDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSvNQGQNIHRKTTAS 78
Cdd:TIGR01271  717 FVQMGPQKAQATTIEdaVREPSERKFSLVPEDEQGEESLPRGNQYHHGLQHQAQRRQSVLQLMTHS-NRGENRREQLQTS 795

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1278156095   79 TRKVSLAPQAN--LTELDIYSRRLSQETGLEISEEINEEDLK 118
Cdd:TIGR01271  796 FRKKSSITQQNelASELDIYSRRLSKDSVYEISEEINEEDLK 837
 
Name Accession Description Interval E-value
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 1-118 3.11e-55

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 184.34  E-value: 3.11e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278156095    1 IVQKTPLQMNGIEED--SDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSvNQGQNIHRKTTAS 78
Cdd:TIGR01271  717 FVQMGPQKAQATTIEdaVREPSERKFSLVPEDEQGEESLPRGNQYHHGLQHQAQRRQSVLQLMTHS-NRGENRREQLQTS 795

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1278156095   79 TRKVSLAPQAN--LTELDIYSRRLSQETGLEISEEINEEDLK 118
Cdd:TIGR01271  796 FRKKSSITQQNelASELDIYSRRLSKDSVYEISEEINEEDLK 837
 
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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