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Conserved domains on  [gi|6671760|ref|NP_031735|]
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cbp/p300-interacting transactivator 1 isoform a [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CITED super family cl24024
CITED; CITED, CBP/p300-interacting transactivator with ED-rich tail, are characterized by a ...
 89-199 2.20e-29

CITED; CITED, CBP/p300-interacting transactivator with ED-rich tail, are characterized by a conserved 32-amino acid sequence at the C-terminus. CITED proteins do not bind DNA directly and are thought to function as transcriptional co-activators.


The actual alignment was detected with superfamily member pfam04487:

Pssm-ID: 461328  Cd Length: 211  Bit Score: 108.38  E-value: 2.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671760     89 PTPHLMASMQLQKLNSQYQGAAATaaaaltgaglPGEEEPMQNwvTAPLVVGGSPGSVSP---PAGAQSPALIDSDPVDE 165
Cdd:pfam04487  99 TSQQLMASMHLQKLNTQYHGHPLH----------PANGHHLGG--GGQYRDGPAQLSGMQphvPAPMLPPNVIDTDLIDE 166

                          90       100       110
                  ....*....|....*....|....*....|....
gi 6671760    166 EVLMSLVVELGLDRANELPELWLGQNEFDFTADF 199
Cdd:pfam04487 167 EVLTSLVLELGLDRIQELPELFLGQNEFDFMSDF 200
 
Name Accession Description Interval E-value
CITED pfam04487
CITED; CITED, CBP/p300-interacting transactivator with ED-rich tail, are characterized by a ...
 89-199 2.20e-29

CITED; CITED, CBP/p300-interacting transactivator with ED-rich tail, are characterized by a conserved 32-amino acid sequence at the C-terminus. CITED proteins do not bind DNA directly and are thought to function as transcriptional co-activators.


Pssm-ID: 461328  Cd Length: 211  Bit Score: 108.38  E-value: 2.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671760     89 PTPHLMASMQLQKLNSQYQGAAATaaaaltgaglPGEEEPMQNwvTAPLVVGGSPGSVSP---PAGAQSPALIDSDPVDE 165
Cdd:pfam04487  99 TSQQLMASMHLQKLNTQYHGHPLH----------PANGHHLGG--GGQYRDGPAQLSGMQphvPAPMLPPNVIDTDLIDE 166

                          90       100       110
                  ....*....|....*....|....*....|....
gi 6671760    166 EVLMSLVVELGLDRANELPELWLGQNEFDFTADF 199
Cdd:pfam04487 167 EVLTSLVLELGLDRIQELPELFLGQNEFDFMSDF 200
 
Name Accession Description Interval E-value
CITED pfam04487
CITED; CITED, CBP/p300-interacting transactivator with ED-rich tail, are characterized by a ...
 89-199 2.20e-29

CITED; CITED, CBP/p300-interacting transactivator with ED-rich tail, are characterized by a conserved 32-amino acid sequence at the C-terminus. CITED proteins do not bind DNA directly and are thought to function as transcriptional co-activators.


Pssm-ID: 461328  Cd Length: 211  Bit Score: 108.38  E-value: 2.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671760     89 PTPHLMASMQLQKLNSQYQGAAATaaaaltgaglPGEEEPMQNwvTAPLVVGGSPGSVSP---PAGAQSPALIDSDPVDE 165
Cdd:pfam04487  99 TSQQLMASMHLQKLNTQYHGHPLH----------PANGHHLGG--GGQYRDGPAQLSGMQphvPAPMLPPNVIDTDLIDE 166

                          90       100       110
                  ....*....|....*....|....*....|....
gi 6671760    166 EVLMSLVVELGLDRANELPELWLGQNEFDFTADF 199
Cdd:pfam04487 167 EVLTSLVLELGLDRIQELPELFLGQNEFDFMSDF 200
 
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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