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Conserved domains on  [gi|296278219|ref|NP_001171611|]
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transcription factor Dp-2 isoform 3 [Homo sapiens]

Protein Classification

E2F/DP family transcription factor( domain architecture ID 11130207)

E2F/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'

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 ...
 187-325 8.55e-78

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: 237.11  E-value: 8.55e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278219  187 QECQNLEIEKQRRIERIKQKRAQLQELLLQQIAFKNLVQRNRQNEQQNqGPPALNSTIQLPFIIINTSRKTVIDCSISSD 266
Cdd:pfam08781   1 QECEELEKEKEKRLERIKKKKAQLQELILQQVAFKNLVQRNRELEQKG-GPPSPNSAIQLPFIIVNTSKKTVIDCSISND 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 296278219  267 KFEYLFNFDNTFEIHDDIEVLKRMGMSFGLESGKCSLEDLKLAKSLVPKALEGYITDIS 325
Cdd:pfam08781  80 KSEYLFNFDNTFEIHDDIEVLKRMGLALGLENGECTDEDLEKAKSLVPKALEPYVDEMA 138
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 100-180 5.56e-22

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: 88.64  E-value: 5.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278219  100 NGKGLRHFSMKVCEKVQR--KGTTSYNEVADELVseftnsnnhlaadsaydqkNIRRRVYDALNVLMAMNIISKE-KKEI 176
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLEspDGVIDLNEAAEELG-------------------VKKRRIYDITNVLEGLGLIEKKsKNKI 61


                  ....
gi 296278219  177 KWIG 180
Cdd:pfam02319  62 KWIG 65
 
Name Accession Description Interval E-value
DP pfam08781
Transcription factor DP; DP forms a heterodimer with E2F and regulates genes involved in cell ...
 187-325 8.55e-78

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: 237.11  E-value: 8.55e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278219  187 QECQNLEIEKQRRIERIKQKRAQLQELLLQQIAFKNLVQRNRQNEQQNqGPPALNSTIQLPFIIINTSRKTVIDCSISSD 266
Cdd:pfam08781   1 QECEELEKEKEKRLERIKKKKAQLQELILQQVAFKNLVQRNRELEQKG-GPPSPNSAIQLPFIIVNTSKKTVIDCSISND 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 296278219  267 KFEYLFNFDNTFEIHDDIEVLKRMGMSFGLESGKCSLEDLKLAKSLVPKALEGYITDIS 325
Cdd:pfam08781  80 KSEYLFNFDNTFEIHDDIEVLKRMGLALGLENGECTDEDLEKAKSLVPKALEPYVDEMA 138
DP_DD cd14458
Dimerization domain of DP; DP functions as a binding partner for E2F transcription factors. DP ...
 185-290 3.19e-51

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: 167.36  E-value: 3.19e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278219 185 SAQECQNLEIEKQRRIERIKQKRAQLQELLLQQIAFKNLVQRNRQNEQQNQGPPAlNSTIQLPFIIINTSRKTVIDCSIS 264
Cdd:cd14458    1 SLEECEQLEEEKERRRERIEKKKAQLQELILQQIALKNLVERNREREAQGEAPAP-NSKIQLPFIIVNTSKDAVIDCEIS 79

                         90       100
                 ....*....|....*....|....*.
gi 296278219 265 SDKFEYLFNFDNTFEIHDDIEVLKRM 290
Cdd:cd14458   80 EDRSEYLFNFNSPFEIHDDIEILKRM 105
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 100-180 5.56e-22

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: 88.64  E-value: 5.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278219  100 NGKGLRHFSMKVCEKVQR--KGTTSYNEVADELVseftnsnnhlaadsaydqkNIRRRVYDALNVLMAMNIISKE-KKEI 176
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLEspDGVIDLNEAAEELG-------------------VKKRRIYDITNVLEGLGLIEKKsKNKI 61


                  ....
gi 296278219  177 KWIG 180
Cdd:pfam02319  62 KWIG 65
 
Name Accession Description Interval E-value
DP pfam08781
Transcription factor DP; DP forms a heterodimer with E2F and regulates genes involved in cell ...
 187-325 8.55e-78

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: 237.11  E-value: 8.55e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278219  187 QECQNLEIEKQRRIERIKQKRAQLQELLLQQIAFKNLVQRNRQNEQQNqGPPALNSTIQLPFIIINTSRKTVIDCSISSD 266
Cdd:pfam08781   1 QECEELEKEKEKRLERIKKKKAQLQELILQQVAFKNLVQRNRELEQKG-GPPSPNSAIQLPFIIVNTSKKTVIDCSISND 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 296278219  267 KFEYLFNFDNTFEIHDDIEVLKRMGMSFGLESGKCSLEDLKLAKSLVPKALEGYITDIS 325
Cdd:pfam08781  80 KSEYLFNFDNTFEIHDDIEVLKRMGLALGLENGECTDEDLEKAKSLVPKALEPYVDEMA 138
DP_DD cd14458
Dimerization domain of DP; DP functions as a binding partner for E2F transcription factors. DP ...
 185-290 3.19e-51

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: 167.36  E-value: 3.19e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278219 185 SAQECQNLEIEKQRRIERIKQKRAQLQELLLQQIAFKNLVQRNRQNEQQNQGPPAlNSTIQLPFIIINTSRKTVIDCSIS 264
Cdd:cd14458    1 SLEECEQLEEEKERRRERIEKKKAQLQELILQQIALKNLVERNREREAQGEAPAP-NSKIQLPFIIVNTSKDAVIDCEIS 79

                         90       100
                 ....*....|....*....|....*.
gi 296278219 265 SDKFEYLFNFDNTFEIHDDIEVLKRM 290
Cdd:cd14458   80 EDRSEYLFNFNSPFEIHDDIEILKRM 105
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 100-180 5.56e-22

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: 88.64  E-value: 5.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278219  100 NGKGLRHFSMKVCEKVQR--KGTTSYNEVADELVseftnsnnhlaadsaydqkNIRRRVYDALNVLMAMNIISKE-KKEI 176
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLEspDGVIDLNEAAEELG-------------------VKKRRIYDITNVLEGLGLIEKKsKNKI 61


                  ....
gi 296278219  177 KWIG 180
Cdd:pfam02319  62 KWIG 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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