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Conserved domains on  [gi|1149844967|ref|XP_020177970|]
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transcription factor E2FA isoform X1 [Aegilops tauschii subsp. strangulata]

Protein Classification

E2F_TDP and E2F_DD domain-containing protein( domain architecture ID 11130215)

E2F_TDP and E2F_DD domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
E2F_CC-MB pfam16421
E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain ...
 212-312 1.97e-50

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: 165.83  E-value: 1.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149844967 212 LQGDIEALTLQEHSLDGQISEMRDKLRELTEDENNQKWLYVTEDDIKSLPCFQNQTLIAIKAPHGTTLEVPDPDEvndyp 291
Cdd:pfam16421   1 LKAELEDLEEEEEELDQLIRWLQQSLKNLTEDEKNQKLAYVTYQDIRSIPCFQEQTVIAIKAPPGTQLEVPDPDE----- 75

                          90       100
                  ....*....|....*....|.
gi 1149844967 292 QRRYRIVLRSTMGPIDVYLVS 312
Cdd:pfam16421  76 EEQYQIHLKSTNGPIDVYLCS 96
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 132-196 1.49e-32

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: 117.53  E-value: 1.49e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149844967 132 YDSSLGLLTKKFLNLLKGAPGGMVDLNNAAETLEVQKRRIYDITNVLEGIGLIEKKLKNNIRWKG 196
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLESPDGVIDLNEAAEELGVKKRRIYDITNVLEGLGLIEKKSKNKIKWIG 65
 
Name Accession Description Interval E-value
E2F_CC-MB pfam16421
E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain ...
 212-312 1.97e-50

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: 165.83  E-value: 1.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149844967 212 LQGDIEALTLQEHSLDGQISEMRDKLRELTEDENNQKWLYVTEDDIKSLPCFQNQTLIAIKAPHGTTLEVPDPDEvndyp 291
Cdd:pfam16421   1 LKAELEDLEEEEEELDQLIRWLQQSLKNLTEDEKNQKLAYVTYQDIRSIPCFQEQTVIAIKAPPGTQLEVPDPDE----- 75

                          90       100
                  ....*....|....*....|.
gi 1149844967 292 QRRYRIVLRSTMGPIDVYLVS 312
Cdd:pfam16421  76 EEQYQIHLKSTNGPIDVYLCS 96
E2F_DD cd14660
Dimerization domain of E2F transcription factors; E2F transcription factors are involved in ...
 207-313 2.32e-50

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: 165.77  E-value: 2.32e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149844967 207 DDMSILQGDIEALTLQEHSLDGQISEMRDKLRELTEDENNQKWLYVTEDDIKSLPCFQNQTLIAIKAPHGTTLEVPDPDE 286
Cdd:cd14660     1 DRLSKLKEEIEELEAEEKELDELIRWCQQSLKNLTEDPENQKLAYVTYEDIRSIPSFKEQTVIAIKAPPGTTLEVPDPEE 80

                          90       100
                  ....*....|....*....|....*..
gi 1149844967 287 vndyPQRRYRIVLRSTMGPIDVYLVSQ 313
Cdd:cd14660    81 ----GMRSYQIHLKSTKGPIDVYLCPK 103
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 132-196 1.49e-32

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: 117.53  E-value: 1.49e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149844967 132 YDSSLGLLTKKFLNLLKGAPGGMVDLNNAAETLEVQKRRIYDITNVLEGIGLIEKKLKNNIRWKG 196
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLESPDGVIDLNEAAEELGVKKRRIYDITNVLEGLGLIEKKSKNKIKWIG 65
 
Name Accession Description Interval E-value
E2F_CC-MB pfam16421
E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain ...
 212-312 1.97e-50

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: 165.83  E-value: 1.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149844967 212 LQGDIEALTLQEHSLDGQISEMRDKLRELTEDENNQKWLYVTEDDIKSLPCFQNQTLIAIKAPHGTTLEVPDPDEvndyp 291
Cdd:pfam16421   1 LKAELEDLEEEEEELDQLIRWLQQSLKNLTEDEKNQKLAYVTYQDIRSIPCFQEQTVIAIKAPPGTQLEVPDPDE----- 75

                          90       100
                  ....*....|....*....|.
gi 1149844967 292 QRRYRIVLRSTMGPIDVYLVS 312
Cdd:pfam16421  76 EEQYQIHLKSTNGPIDVYLCS 96
E2F_DD cd14660
Dimerization domain of E2F transcription factors; E2F transcription factors are involved in ...
 207-313 2.32e-50

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: 165.77  E-value: 2.32e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149844967 207 DDMSILQGDIEALTLQEHSLDGQISEMRDKLRELTEDENNQKWLYVTEDDIKSLPCFQNQTLIAIKAPHGTTLEVPDPDE 286
Cdd:cd14660     1 DRLSKLKEEIEELEAEEKELDELIRWCQQSLKNLTEDPENQKLAYVTYEDIRSIPSFKEQTVIAIKAPPGTTLEVPDPEE 80

                          90       100
                  ....*....|....*....|....*..
gi 1149844967 287 vndyPQRRYRIVLRSTMGPIDVYLVSQ 313
Cdd:cd14660    81 ----GMRSYQIHLKSTKGPIDVYLCPK 103
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 132-196 1.49e-32

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: 117.53  E-value: 1.49e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149844967 132 YDSSLGLLTKKFLNLLKGAPGGMVDLNNAAETLEVQKRRIYDITNVLEGIGLIEKKLKNNIRWKG 196
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLESPDGVIDLNEAAEELGVKKRRIYDITNVLEGLGLIEKKSKNKIKWIG 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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