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Conserved domains on  [gi|47078264|ref|NP_997705|]
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transcription factor E2F6 isoform 4 [Homo sapiens]

Protein Classification

E2F_DD domain-containing protein( domain architecture ID 10199752)

E2F_DD domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
E2F_DD cd14660
Dimerization domain of E2F transcription factors; E2F transcription factors are involved in ...
1-87 8.25e-42

Dimerization domain of E2F transcription factors; E2F transcription factors are involved in the regulation of DNA synthesis, cell cycle progression, proliferation and apoptosis. It associates with the retinoblastoma (Rb) protein, negatively regulating the G1-S transition until cyclin-dependent kinases phosphorylate Rb, which causes E2F release. E2F forms heterodimers with DP, a distantly related protein. Heterodimerization enhances the Rb binding, DNA binding, and transactivation activities of E2Fs. 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: 271137 [Multi-domain]  Cd Length: 104  Bit Score: 133.80  E-value: 8.25e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078264   1 MEDALDELIKDCAQQLFELTDDKENERLAYVTYQDIHSIQAFHEQIVIAVKAPAETRLDVPAPRED--SITVHIRSTNGP 78
Cdd:cd14660  16 EEKELDELIRWCQQSLKNLTEDPENQKLAYVTYEDIRSIPSFKEQTVIAIKAPPGTTLEVPDPEEGmrSYQIHLKSTKGP 95

                ....*....
gi 47078264  79 IDVYLCEVE 87
Cdd:cd14660  96 IDVYLCPKE 104
 
Name Accession Description Interval E-value
E2F_DD cd14660
Dimerization domain of E2F transcription factors; E2F transcription factors are involved in ...
1-87 8.25e-42

Dimerization domain of E2F transcription factors; E2F transcription factors are involved in the regulation of DNA synthesis, cell cycle progression, proliferation and apoptosis. It associates with the retinoblastoma (Rb) protein, negatively regulating the G1-S transition until cyclin-dependent kinases phosphorylate Rb, which causes E2F release. E2F forms heterodimers with DP, a distantly related protein. Heterodimerization enhances the Rb binding, DNA binding, and transactivation activities of E2Fs. 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: 271137 [Multi-domain]  Cd Length: 104  Bit Score: 133.80  E-value: 8.25e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078264   1 MEDALDELIKDCAQQLFELTDDKENERLAYVTYQDIHSIQAFHEQIVIAVKAPAETRLDVPAPRED--SITVHIRSTNGP 78
Cdd:cd14660  16 EEKELDELIRWCQQSLKNLTEDPENQKLAYVTYEDIRSIPSFKEQTVIAIKAPPGTTLEVPDPEEGmrSYQIHLKSTKGP 95

                ....*....
gi 47078264  79 IDVYLCEVE 87
Cdd:cd14660  96 IDVYLCPKE 104
E2F_CC-MB pfam16421
E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain ...
1-85 4.27e-39

E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain of E2F transcription factors. This domain forms a heterodimer with the corresponding domain of the DP transcription factor, the heterodimer binds the C-terminus of retinoblastoma protein.


Pssm-ID: 465115  Cd Length: 96  Bit Score: 126.54  E-value: 4.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078264     1 MEDALDELIKDCAQQLFELTDDKENERLAYVTYQDIHSIQAFHEQIVIAVKAPAETRLDVPAP-REDSITVHIRSTNGPI 79
Cdd:pfam16421  11 EEEELDQLIRWLQQSLKNLTEDEKNQKLAYVTYQDIRSIPCFQEQTVIAIKAPPGTQLEVPDPdEEEQYQIHLKSTNGPI 90

                  ....*.
gi 47078264    80 DVYLCE 85
Cdd:pfam16421  91 DVYLCS 96
 
Name Accession Description Interval E-value
E2F_DD cd14660
Dimerization domain of E2F transcription factors; E2F transcription factors are involved in ...
1-87 8.25e-42

Dimerization domain of E2F transcription factors; E2F transcription factors are involved in the regulation of DNA synthesis, cell cycle progression, proliferation and apoptosis. It associates with the retinoblastoma (Rb) protein, negatively regulating the G1-S transition until cyclin-dependent kinases phosphorylate Rb, which causes E2F release. E2F forms heterodimers with DP, a distantly related protein. Heterodimerization enhances the Rb binding, DNA binding, and transactivation activities of E2Fs. 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: 271137 [Multi-domain]  Cd Length: 104  Bit Score: 133.80  E-value: 8.25e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078264   1 MEDALDELIKDCAQQLFELTDDKENERLAYVTYQDIHSIQAFHEQIVIAVKAPAETRLDVPAPRED--SITVHIRSTNGP 78
Cdd:cd14660  16 EEKELDELIRWCQQSLKNLTEDPENQKLAYVTYEDIRSIPSFKEQTVIAIKAPPGTTLEVPDPEEGmrSYQIHLKSTKGP 95

                ....*....
gi 47078264  79 IDVYLCEVE 87
Cdd:cd14660  96 IDVYLCPKE 104
E2F_CC-MB pfam16421
E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain ...
1-85 4.27e-39

E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain of E2F transcription factors. This domain forms a heterodimer with the corresponding domain of the DP transcription factor, the heterodimer binds the C-terminus of retinoblastoma protein.


Pssm-ID: 465115  Cd Length: 96  Bit Score: 126.54  E-value: 4.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078264     1 MEDALDELIKDCAQQLFELTDDKENERLAYVTYQDIHSIQAFHEQIVIAVKAPAETRLDVPAP-REDSITVHIRSTNGPI 79
Cdd:pfam16421  11 EEEELDQLIRWLQQSLKNLTEDEKNQKLAYVTYQDIRSIPCFQEQTVIAIKAPPGTQLEVPDPdEEEQYQIHLKSTNGPI 90

                  ....*.
gi 47078264    80 DVYLCE 85
Cdd:pfam16421  91 DVYLCS 96
 
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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