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Conserved domains on  [gi|18875392|ref|NP_573494|]
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regulatory factor X-associated protein [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RFXA_RFXANK_bdg super family cl21137
Regulatory factor X-associated C-terminal binding domain; This C-terminal domain of Regulatory ...
 100-202 8.46e-46

Regulatory factor X-associated C-terminal binding domain; This C-terminal domain of Regulatory factor X-associated protein binds to RFXANK, the Ankyrin-repeat regulatory factor X proteins. RFXA is part of the RFX complex, Mutants of either RFXAP or RFXANK protein fail to bind to each other. RFX5 binds only to the RFXANK-RFXAP scaffold and not to either protein alone, and neither the scaffold nor RFX5 alone can bind DNA. The binding of the RFXANK-RFXAP scaffold to RFX5 leads to a conformational change in the latter that exposes the DNA-binding domain of RFX5. The DNA-binding domain of RFX5 anchors the RFX complex to MHC class II X and S promoter boxes.


The actual alignment was detected with superfamily member pfam15289:

Pssm-ID: 434600  Cd Length: 122  Bit Score: 148.64  E-value: 8.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18875392   100 TCTYEGCRETTSQVAKQRKPWMCKKHRNKMYKDKYKKKKSDQALGSGGpsaasTGNVKLEESTDNILSIVKQRTGSFGDR 179
Cdd:pfam15289   1 TCTYEGCNETTTQSAKQRKPWMCKKHRNKMYKDKYKKKKSDQALGNGG-----KGEEMFEDKEEGNVSKTKQRTGSPGDR 75

                          90       100
                  ....*....|....*....|...
gi 18875392   180 PARPTLLEQVLNQKRLSLLRSPE 202
Cdd:pfam15289  76 PARPTLLEQVLNQKRLSLLRSPA 98
 
Name Accession Description Interval E-value
RFXA_RFXANK_bdg pfam15289
Regulatory factor X-associated C-terminal binding domain; This C-terminal domain of Regulatory ...
 100-202 8.46e-46

Regulatory factor X-associated C-terminal binding domain; This C-terminal domain of Regulatory factor X-associated protein binds to RFXANK, the Ankyrin-repeat regulatory factor X proteins. RFXA is part of the RFX complex, Mutants of either RFXAP or RFXANK protein fail to bind to each other. RFX5 binds only to the RFXANK-RFXAP scaffold and not to either protein alone, and neither the scaffold nor RFX5 alone can bind DNA. The binding of the RFXANK-RFXAP scaffold to RFX5 leads to a conformational change in the latter that exposes the DNA-binding domain of RFX5. The DNA-binding domain of RFX5 anchors the RFX complex to MHC class II X and S promoter boxes.


Pssm-ID: 434600  Cd Length: 122  Bit Score: 148.64  E-value: 8.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18875392   100 TCTYEGCRETTSQVAKQRKPWMCKKHRNKMYKDKYKKKKSDQALGSGGpsaasTGNVKLEESTDNILSIVKQRTGSFGDR 179
Cdd:pfam15289   1 TCTYEGCNETTTQSAKQRKPWMCKKHRNKMYKDKYKKKKSDQALGNGG-----KGEEMFEDKEEGNVSKTKQRTGSPGDR 75

                          90       100
                  ....*....|....*....|...
gi 18875392   180 PARPTLLEQVLNQKRLSLLRSPE 202
Cdd:pfam15289  76 PARPTLLEQVLNQKRLSLLRSPA 98
 
Name Accession Description Interval E-value
RFXA_RFXANK_bdg pfam15289
Regulatory factor X-associated C-terminal binding domain; This C-terminal domain of Regulatory ...
 100-202 8.46e-46

Regulatory factor X-associated C-terminal binding domain; This C-terminal domain of Regulatory factor X-associated protein binds to RFXANK, the Ankyrin-repeat regulatory factor X proteins. RFXA is part of the RFX complex, Mutants of either RFXAP or RFXANK protein fail to bind to each other. RFX5 binds only to the RFXANK-RFXAP scaffold and not to either protein alone, and neither the scaffold nor RFX5 alone can bind DNA. The binding of the RFXANK-RFXAP scaffold to RFX5 leads to a conformational change in the latter that exposes the DNA-binding domain of RFX5. The DNA-binding domain of RFX5 anchors the RFX complex to MHC class II X and S promoter boxes.


Pssm-ID: 434600  Cd Length: 122  Bit Score: 148.64  E-value: 8.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18875392   100 TCTYEGCRETTSQVAKQRKPWMCKKHRNKMYKDKYKKKKSDQALGSGGpsaasTGNVKLEESTDNILSIVKQRTGSFGDR 179
Cdd:pfam15289   1 TCTYEGCNETTTQSAKQRKPWMCKKHRNKMYKDKYKKKKSDQALGNGG-----KGEEMFEDKEEGNVSKTKQRTGSPGDR 75

                          90       100
                  ....*....|....*....|...
gi 18875392   180 PARPTLLEQVLNQKRLSLLRSPE 202
Cdd:pfam15289  76 PARPTLLEQVLNQKRLSLLRSPA 98
 
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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