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Conserved domains on  [gi|17136994|ref|NP_477039|]
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DP transcription factor, isoform A [Drosophila melanogaster]

Protein Classification

DP family transcription factor( domain architecture ID 11130207)

DP family transcription factor can stimulate E2F-dependent transcription; it binds DNA cooperatively with E2F family members through the E2 recognition site, 5'-TTTC[CG]CGC-3'

CATH:  1.10.10.10|1.20.140.80
Gene Ontology:  GO:0006357|GO:0003700|GO:1990837
PubMed:  10090723|26632596|7917337|7880534|7739537|9670325
SCOP:  3000345|4000205

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DP pfam08781
Transcription factor DP; DP forms a heterodimer with E2F and regulates genes involved in cell ...
 255-386 6.88e-72

Transcription factor DP; DP forms a heterodimer with E2F and regulates genes involved in cell cycle progression. The transcriptional activity of E2F is inhibited by the retinoblastoma protein which binds to the E2F-DP heterodimer and negatively regulates the G1-S transition.


:

Pssm-ID: 462601  Cd Length: 138  Bit Score: 222.85  E-value: 6.88e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136994   255 LEEENCQRRERIKQKNEMLREMIMQHVAFKGLVERNKRNESQGVVPSPNASIQLPFIIVNTHKSTKINCSVTNDKSEYIF 334
Cdd:pfam08781   6 LEKEKEKRLERIKKKKAQLQELILQQVAFKNLVQRNRELEQKGGPPSPNSAIQLPFIIVNTSKKTVIDCSISNDKSEYLF 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17136994   335 KFDKTFEMHDDIEVLKRMGFLLGLDKGECTPENIERVKSWVPPNLAKYVEAY 386
Cdd:pfam08781  86 NFDNTFEIHDDIEVLKRMGLALGLENGECTDEDLEKAKSLVPKALEPYVDEM 137
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 167-243 2.52e-20

E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor E2F and its dimerization partners TDP1 and TDP2, which stimulate E2F-dependent transcription. E2F binds to DNA as a homodimer or as a heterodimer in association with TDP1/2, the heterodimer having increased binding efficiency. The crystal structure of an E2F4-DP2-DNA complex shows that the DNA-binding domains of the E2F and DP proteins both have a fold related to the winged-helix DNA-binding motif. Recognition of the central c/gGCGCg/c sequence of the consensus DNA-binding site is symmetric, and amino acids that contact these bases are conserved among all known E2F and DP proteins.


:

Pssm-ID: 460530  Cd Length: 65  Bit Score: 84.41  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136994   167 GKGLRHFSMKVCEKVE--EKGKTTYNEVADDLVseemknnaydnncdqkNIRRRVYDALNVLMAINVISKD-KKEIRWIG 243
Cdd:pfam02319   2 DKSLGLLTQKFLELLLesPDGVIDLNEAAEELG----------------VKKRRIYDITNVLEGLGLIEKKsKNKIKWIG 65
 
Name Accession Description Interval E-value
DP pfam08781
Transcription factor DP; DP forms a heterodimer with E2F and regulates genes involved in cell ...
 255-386 6.88e-72

Transcription factor DP; DP forms a heterodimer with E2F and regulates genes involved in cell cycle progression. The transcriptional activity of E2F is inhibited by the retinoblastoma protein which binds to the E2F-DP heterodimer and negatively regulates the G1-S transition.


Pssm-ID: 462601  Cd Length: 138  Bit Score: 222.85  E-value: 6.88e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136994   255 LEEENCQRRERIKQKNEMLREMIMQHVAFKGLVERNKRNESQGVVPSPNASIQLPFIIVNTHKSTKINCSVTNDKSEYIF 334
Cdd:pfam08781   6 LEKEKEKRLERIKKKKAQLQELILQQVAFKNLVQRNRELEQKGGPPSPNSAIQLPFIIVNTSKKTVIDCSISNDKSEYLF 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17136994   335 KFDKTFEMHDDIEVLKRMGFLLGLDKGECTPENIERVKSWVPPNLAKYVEAY 386
Cdd:pfam08781  86 NFDNTFEIHDDIEVLKRMGLALGLENGECTDEDLEKAKSLVPKALEPYVDEM 137
DP_DD cd14458
Dimerization domain of DP; DP functions as a binding partner for E2F transcription factors. DP ...
 248-352 1.16e-48

Dimerization domain of DP; DP functions as a binding partner for E2F transcription factors. DP and E2F form heterodimers and play important roles in regulating genes involved in DNA synthesis, cell cycle progression, proliferation and apoptosis. The transcriptional activity of E2F is inhibited by the retinoblastoma protein (Rb) which binds to the E2F-DP heterodimer, blocks the transactivation domain, and negatively regulates the G1-S transition. DP is distantly related to E2F. In humans, there are at least six closely related E2F and two DP family members, all containing a DNA binding domain, a coiled-coil (CC) region, and a marked-box domain. E2F1 to E2F5 also contain a C-terminal transactivation domain.


Pssm-ID: 271217  Cd Length: 105  Bit Score: 161.59  E-value: 1.16e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136994 248 STETFLALEEENCQRRERIKQKNEMLREMIMQHVAFKGLVERNKRNESQGVVPSPNASIQLPFIIVNTHKSTKINCSVTN 327
Cdd:cd14458   1 SLEECEQLEEEKERRRERIEKKKAQLQELILQQIALKNLVERNREREAQGEAPAPNSKIQLPFIIVNTSKDAVIDCEISE 80

                        90       100
                ....*....|....*....|....*
gi 17136994 328 DKSEYIFKFDKTFEMHDDIEVLKRM 352
Cdd:cd14458  81 DRSEYLFNFNSPFEIHDDIEILKRM 105
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 167-243 2.52e-20

E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor E2F and its dimerization partners TDP1 and TDP2, which stimulate E2F-dependent transcription. E2F binds to DNA as a homodimer or as a heterodimer in association with TDP1/2, the heterodimer having increased binding efficiency. The crystal structure of an E2F4-DP2-DNA complex shows that the DNA-binding domains of the E2F and DP proteins both have a fold related to the winged-helix DNA-binding motif. Recognition of the central c/gGCGCg/c sequence of the consensus DNA-binding site is symmetric, and amino acids that contact these bases are conserved among all known E2F and DP proteins.


Pssm-ID: 460530  Cd Length: 65  Bit Score: 84.41  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136994   167 GKGLRHFSMKVCEKVE--EKGKTTYNEVADDLVseemknnaydnncdqkNIRRRVYDALNVLMAINVISKD-KKEIRWIG 243
Cdd:pfam02319   2 DKSLGLLTQKFLELLLesPDGVIDLNEAAEELG----------------VKKRRIYDITNVLEGLGLIEKKsKNKIKWIG 65
 
Name Accession Description Interval E-value
DP pfam08781
Transcription factor DP; DP forms a heterodimer with E2F and regulates genes involved in cell ...
 255-386 6.88e-72

Transcription factor DP; DP forms a heterodimer with E2F and regulates genes involved in cell cycle progression. The transcriptional activity of E2F is inhibited by the retinoblastoma protein which binds to the E2F-DP heterodimer and negatively regulates the G1-S transition.


Pssm-ID: 462601  Cd Length: 138  Bit Score: 222.85  E-value: 6.88e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136994   255 LEEENCQRRERIKQKNEMLREMIMQHVAFKGLVERNKRNESQGVVPSPNASIQLPFIIVNTHKSTKINCSVTNDKSEYIF 334
Cdd:pfam08781   6 LEKEKEKRLERIKKKKAQLQELILQQVAFKNLVQRNRELEQKGGPPSPNSAIQLPFIIVNTSKKTVIDCSISNDKSEYLF 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17136994   335 KFDKTFEMHDDIEVLKRMGFLLGLDKGECTPENIERVKSWVPPNLAKYVEAY 386
Cdd:pfam08781  86 NFDNTFEIHDDIEVLKRMGLALGLENGECTDEDLEKAKSLVPKALEPYVDEM 137
DP_DD cd14458
Dimerization domain of DP; DP functions as a binding partner for E2F transcription factors. DP ...
 248-352 1.16e-48

Dimerization domain of DP; DP functions as a binding partner for E2F transcription factors. DP and E2F form heterodimers and play important roles in regulating genes involved in DNA synthesis, cell cycle progression, proliferation and apoptosis. The transcriptional activity of E2F is inhibited by the retinoblastoma protein (Rb) which binds to the E2F-DP heterodimer, blocks the transactivation domain, and negatively regulates the G1-S transition. DP is distantly related to E2F. In humans, there are at least six closely related E2F and two DP family members, all containing a DNA binding domain, a coiled-coil (CC) region, and a marked-box domain. E2F1 to E2F5 also contain a C-terminal transactivation domain.


Pssm-ID: 271217  Cd Length: 105  Bit Score: 161.59  E-value: 1.16e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136994 248 STETFLALEEENCQRRERIKQKNEMLREMIMQHVAFKGLVERNKRNESQGVVPSPNASIQLPFIIVNTHKSTKINCSVTN 327
Cdd:cd14458   1 SLEECEQLEEEKERRRERIEKKKAQLQELILQQIALKNLVERNREREAQGEAPAPNSKIQLPFIIVNTSKDAVIDCEISE 80

                        90       100
                ....*....|....*....|....*
gi 17136994 328 DKSEYIFKFDKTFEMHDDIEVLKRM 352
Cdd:cd14458  81 DRSEYLFNFNSPFEIHDDIEILKRM 105
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 167-243 2.52e-20

E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor E2F and its dimerization partners TDP1 and TDP2, which stimulate E2F-dependent transcription. E2F binds to DNA as a homodimer or as a heterodimer in association with TDP1/2, the heterodimer having increased binding efficiency. The crystal structure of an E2F4-DP2-DNA complex shows that the DNA-binding domains of the E2F and DP proteins both have a fold related to the winged-helix DNA-binding motif. Recognition of the central c/gGCGCg/c sequence of the consensus DNA-binding site is symmetric, and amino acids that contact these bases are conserved among all known E2F and DP proteins.


Pssm-ID: 460530  Cd Length: 65  Bit Score: 84.41  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136994   167 GKGLRHFSMKVCEKVE--EKGKTTYNEVADDLVseemknnaydnncdqkNIRRRVYDALNVLMAINVISKD-KKEIRWIG 243
Cdd:pfam02319   2 DKSLGLLTQKFLELLLesPDGVIDLNEAAEELG----------------VKKRRIYDITNVLEGLGLIEKKsKNKIKWIG 65
 
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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