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Conserved domains on  [gi|6323682|ref|NP_013753|]
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chromatin-binding transcription coactivator SUB1 [Saccharomyces cerevisiae S288C]

Protein Classification

transcriptional coactivator p15/PC4 family protein( domain architecture ID 10491384)

transcriptional coactivator p15/PC4 family protein is a general coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery

CATH:  2.30.31.10
Gene Ontology:  GO:0003713|GO:0005515|GO:0003697|GO:0003713|GO:0140297|GO:0060261
PubMed:  7628453|15692559|8062392
SCOP:  4001029

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PC4 pfam02229
Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an ...
 41-94 1.34e-20

Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an amino-terminal regulatory domain and a carboxy-terminal cryptic DNA-binding domain. The DNA-binding activity of the carboxy-terminal is disguised by the amino-terminal p15 domain. Activity is controlled by protein kinases that target the regulatory domain.


:

Pssm-ID: 460501  Cd Length: 52  Bit Score: 82.91  E-value: 1.34e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6323682     41 FDLGKNKRVTVRQFRNINLIDIREYYLDSstGEMKPGKKGISLTEDLYDELLKH 94
Cdd:pfam02229   1 WELSKKRRVTVREFKGKTLVDIREYYEKD--GELKPGKKGISLTLEQWKALKEA 52
 
Name Accession Description Interval E-value
PC4 pfam02229
Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an ...
 41-94 1.34e-20

Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an amino-terminal regulatory domain and a carboxy-terminal cryptic DNA-binding domain. The DNA-binding activity of the carboxy-terminal is disguised by the amino-terminal p15 domain. Activity is controlled by protein kinases that target the regulatory domain.


Pssm-ID: 460501  Cd Length: 52  Bit Score: 82.91  E-value: 1.34e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6323682     41 FDLGKNKRVTVRQFRNINLIDIREYYLDSstGEMKPGKKGISLTEDLYDELLKH 94
Cdd:pfam02229   1 WELSKKRRVTVREFKGKTLVDIREYYEKD--GELKPGKKGISLTLEQWKALKEA 52
 
Name Accession Description Interval E-value
PC4 pfam02229
Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an ...
 41-94 1.34e-20

Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an amino-terminal regulatory domain and a carboxy-terminal cryptic DNA-binding domain. The DNA-binding activity of the carboxy-terminal is disguised by the amino-terminal p15 domain. Activity is controlled by protein kinases that target the regulatory domain.


Pssm-ID: 460501  Cd Length: 52  Bit Score: 82.91  E-value: 1.34e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6323682     41 FDLGKNKRVTVRQFRNINLIDIREYYLDSstGEMKPGKKGISLTEDLYDELLKH 94
Cdd:pfam02229   1 WELSKKRRVTVREFKGKTLVDIREYYEKD--GELKPGKKGISLTLEQWKALKEA 52
 
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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