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Conserved domains on  [gi|470261059|ref|XP_004360286|]
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transcription factor Dp-2 [Cavenderia fasciculata]

Protein Classification

E2F_TDP and DP_DD domain-containing protein( domain architecture ID 10491891)

E2F_TDP and DP_DD domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DP_DD cd14458
Dimerization domain of DP; DP functions as a binding partner for E2F transcription factors. DP ...
 292-399 2.85e-34

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: 124.22  E-value: 2.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470261059 292 PSNSMAELERQKQDLQLRLKSKKQSLKELAHLELVYQELINRNKIIVQQQEQqsiRIENDRIHLPFIVVNTKYSTVINCE 371
Cdd:cd14458    1 SLEECEQLEEEKERRRERIEKKKAQLQELILQQIALKNLVERNREREAQGEA---PAPNSKIQLPFIIVNTSKDAVIDCE 77

                         90       100
                 ....*....|....*....|....*...
gi 470261059 372 VESDRSKYFFNFSQPFEIHDDSELIKKL 399
Cdd:cd14458   78 ISEDRSEYLFNFNSPFEIHDDIEILKRM 105
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 204-285 2.40e-17

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: 75.93  E-value: 2.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470261059  204 KSKGLSYLSQKVCQKVQS--KQTTSYVEVSNEIiaeyikenvangskesdlktNTMKRRIYDVLNVFQAMNIISKD-KQK 280
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLEspDGVIDLNEAAEEL--------------------GVKKRRIYDITNVLEGLGLIEKKsKNK 60


                  ....*
gi 470261059  281 ISWIG 285
Cdd:pfam02319  61 IKWIG 65
 
Name Accession Description Interval E-value
DP_DD cd14458
Dimerization domain of DP; DP functions as a binding partner for E2F transcription factors. DP ...
 292-399 2.85e-34

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: 124.22  E-value: 2.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470261059 292 PSNSMAELERQKQDLQLRLKSKKQSLKELAHLELVYQELINRNKIIVQQQEQqsiRIENDRIHLPFIVVNTKYSTVINCE 371
Cdd:cd14458    1 SLEECEQLEEEKERRRERIEKKKAQLQELILQQIALKNLVERNREREAQGEA---PAPNSKIQLPFIIVNTSKDAVIDCE 77

                         90       100
                 ....*....|....*....|....*...
gi 470261059 372 VESDRSKYFFNFSQPFEIHDDSELIKKL 399
Cdd:cd14458   78 ISEDRSEYLFNFNSPFEIHDDIEILKRM 105
DP pfam08781
Transcription factor DP; DP forms a heterodimer with E2F and regulates genes involved in cell ...
 298-401 1.41e-30

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: 115.38  E-value: 1.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470261059  298 ELERQKQDLQLRLKSKKQSLKELAHLELVYQELINRNKIIVQQQEQQSiriENDRIHLPFIVVNTKYSTVINCEVESDRS 377
Cdd:pfam08781   5 ELEKEKEKRLERIKKKKAQLQELILQQVAFKNLVQRNRELEQKGGPPS---PNSAIQLPFIIVNTSKKTVIDCSISNDKS 81

                          90       100
                  ....*....|....*....|....
gi 470261059  378 KYFFNFSQPFEIHDDSELIKKLSF 401
Cdd:pfam08781  82 EYLFNFDNTFEIHDDIEVLKRMGL 105
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 204-285 2.40e-17

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: 75.93  E-value: 2.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470261059  204 KSKGLSYLSQKVCQKVQS--KQTTSYVEVSNEIiaeyikenvangskesdlktNTMKRRIYDVLNVFQAMNIISKD-KQK 280
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLEspDGVIDLNEAAEEL--------------------GVKKRRIYDITNVLEGLGLIEKKsKNK 60


                  ....*
gi 470261059  281 ISWIG 285
Cdd:pfam02319  61 IKWIG 65
 
Name Accession Description Interval E-value
DP_DD cd14458
Dimerization domain of DP; DP functions as a binding partner for E2F transcription factors. DP ...
 292-399 2.85e-34

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: 124.22  E-value: 2.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470261059 292 PSNSMAELERQKQDLQLRLKSKKQSLKELAHLELVYQELINRNKIIVQQQEQqsiRIENDRIHLPFIVVNTKYSTVINCE 371
Cdd:cd14458    1 SLEECEQLEEEKERRRERIEKKKAQLQELILQQIALKNLVERNREREAQGEA---PAPNSKIQLPFIIVNTSKDAVIDCE 77

                         90       100
                 ....*....|....*....|....*...
gi 470261059 372 VESDRSKYFFNFSQPFEIHDDSELIKKL 399
Cdd:cd14458   78 ISEDRSEYLFNFNSPFEIHDDIEILKRM 105
DP pfam08781
Transcription factor DP; DP forms a heterodimer with E2F and regulates genes involved in cell ...
 298-401 1.41e-30

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: 115.38  E-value: 1.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470261059  298 ELERQKQDLQLRLKSKKQSLKELAHLELVYQELINRNKIIVQQQEQQSiriENDRIHLPFIVVNTKYSTVINCEVESDRS 377
Cdd:pfam08781   5 ELEKEKEKRLERIKKKKAQLQELILQQVAFKNLVQRNRELEQKGGPPS---PNSAIQLPFIIVNTSKKTVIDCSISNDKS 81

                          90       100
                  ....*....|....*....|....
gi 470261059  378 KYFFNFSQPFEIHDDSELIKKLSF 401
Cdd:pfam08781  82 EYLFNFDNTFEIHDDIEVLKRMGL 105
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 204-285 2.40e-17

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: 75.93  E-value: 2.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470261059  204 KSKGLSYLSQKVCQKVQS--KQTTSYVEVSNEIiaeyikenvangskesdlktNTMKRRIYDVLNVFQAMNIISKD-KQK 280
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLEspDGVIDLNEAAEEL--------------------GVKKRRIYDITNVLEGLGLIEKKsKNK 60


                  ....*
gi 470261059  281 ISWIG 285
Cdd:pfam02319  61 IKWIG 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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