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Conserved domains on  [gi|66529093|ref|NP_001018881|]
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ATP-binding cassette sub-family C member 5 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03232 super family cl33667
ABC transporter C family member; Provisional
 100-156 1.12e-06

ABC transporter C family member; Provisional


The actual alignment was detected with superfamily member PLN03232:

Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 48.43  E-value: 1.12e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 66529093   100 PVDNAGLFSCMTFSWLSSLARVAHKKgELSMEDVWSLSKHESSDVNCRRLERLWQEE 156
Cdd:PLN03232  228 PERYASIFSRIYFSWMTPLMQLGYRK-PITEKDVWQLDQWDQTETLIKRFQRCWTEE 283
 
Name Accession Description Interval E-value
PLN03232 PLN03232
ABC transporter C family member; Provisional
 100-156 1.12e-06

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 48.43  E-value: 1.12e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 66529093   100 PVDNAGLFSCMTFSWLSSLARVAHKKgELSMEDVWSLSKHESSDVNCRRLERLWQEE 156
Cdd:PLN03232  228 PERYASIFSRIYFSWMTPLMQLGYRK-PITEKDVWQLDQWDQTETLIKRFQRCWTEE 283
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 100-157 4.01e-04

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: 40.66  E-value: 4.01e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 66529093    100 PVDNAGLFSCMTFSWLSSLARVAHKKgELSMEDVWSLSKHESSDVNCRRLERLWQEEL 157
Cdd:TIGR01271    5 PVEKANFLSKLFFWWTRPILRKGYRQ-KLELSDIYQIPSFDSADNLSERLEREWDREL 61
 
Name Accession Description Interval E-value
PLN03232 PLN03232
ABC transporter C family member; Provisional
 100-156 1.12e-06

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 48.43  E-value: 1.12e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 66529093   100 PVDNAGLFSCMTFSWLSSLARVAHKKgELSMEDVWSLSKHESSDVNCRRLERLWQEE 156
Cdd:PLN03232  228 PERYASIFSRIYFSWMTPLMQLGYRK-PITEKDVWQLDQWDQTETLIKRFQRCWTEE 283
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 100-157 4.01e-04

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: 40.66  E-value: 4.01e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 66529093    100 PVDNAGLFSCMTFSWLSSLARVAHKKgELSMEDVWSLSKHESSDVNCRRLERLWQEEL 157
Cdd:TIGR01271    5 PVEKANFLSKLFFWWTRPILRKGYRQ-KLELSDIYQIPSFDSADNLSERLEREWDREL 61
PLN03130 PLN03130
ABC transporter C family member; Provisional
 100-162 5.82e-04

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 40.49  E-value: 5.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66529093   100 PVDNAGLFSCMTFSWLSSLARVAHKKgELSMEDVWSLSKHESSDVNCRRLERLWQEELNEVGP 162
Cdd:PLN03130  228 PERHANIFSRIFFGWMTPLMQLGYKR-PLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPKP 289
 
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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