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Conserved domains on  [gi|145580626|ref|NP_976328|]
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transcription factor E2F7 [Homo sapiens]

Protein Classification

E2F family transcription factor( domain architecture ID 10491890)

E2F family transcription factor specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3' and plays a crucial role in the control of various processes such as the cell cycle; similar to human atypical E2F transcription factors E2F7 and E2F8

CATH:  1.10.10.10
Gene Ontology:  GO:0006357|GO:0003700|GO:1990837
PubMed:  19201609|26632596

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 143-211 9.79e-28

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: 106.36  E-value: 9.79e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145580626  143 KQKSLGLLCQKFLARYPSYPlsteKTTISLDEVAVSLGVERRRIYDIVNVLESLHLVSRVAKNQYGWHG 211
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLESP----DGVIDLNEAAEELGVKKRRIYDITNVLEGLGLIEKKSKNKIKWIG 65
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 283-367 5.91e-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: 89.80  E-value: 5.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580626  283 KDKSLRIMSQKFVMLFLVSKTKIVTLDVAAKILIeesqdapdhskfkTKVRRLYDIANVLTSLALIKKVHvteergrKPA 362
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLESPDGVIDLNEAAEELG-------------VKKRRIYDITNVLEGLGLIEKKS-------KNK 60


                  ....*
gi 145580626  363 FKWIG 367
Cdd:pfam02319  61 IKWIG 65
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 575-862 6.27e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580626  575 DRSSEAPATVELSSAPSAQKRlceERKPQEEDEPATKRQSREYEDGPLSLVMPKKPSDSTDLASPKTMGNRasiplkdih 654
Cdd:PHA03247 2565 DRSVPPPRPAPRPSEPAVTSR---ARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPS--------- 2632

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580626  655 vngqlPAAEEISGKATANSlvssewGNPSRNTDVEKPSKENESTKEPSLLQYLCVQSPaglngfnvllSGSQTPPTVGPS 734
Cdd:PHA03247 2633 -----PAANEPDPHPPPTV------PPPERPRDDPAPGRVSRPRRARRLGRAAQASSP----------PQRPRRRAARPT 2691

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580626  735 SGQLPSFSVPCMvlPSPPLGPFPVLYSPAMPGPV--SSTLGALPNTgPVNFSLPGLGSIAQLLVGPTAVVNPKS-----S 807
Cdd:PHA03247 2692 VGSLTSLADPPP--PPPTPEPAPHALVSATPLPPgpAAARQASPAL-PAAPAPPAVPAGPATPGGPARPARPPTtagppA 2768

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145580626  808 TLPSADPQLQSQPSLNLSPVMSRSHSVVQQP------ESPVYVGHPVSVVKLHQSPVPVTP 862
Cdd:PHA03247 2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPspwdpaDPPAAVLAPAAALPPAASPAGPLP 2829
 
Name Accession Description Interval E-value
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 143-211 9.79e-28

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: 106.36  E-value: 9.79e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145580626  143 KQKSLGLLCQKFLARYPSYPlsteKTTISLDEVAVSLGVERRRIYDIVNVLESLHLVSRVAKNQYGWHG 211
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLESP----DGVIDLNEAAEELGVKKRRIYDITNVLEGLGLIEKKSKNKIKWIG 65
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 283-367 5.91e-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: 89.80  E-value: 5.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580626  283 KDKSLRIMSQKFVMLFLVSKTKIVTLDVAAKILIeesqdapdhskfkTKVRRLYDIANVLTSLALIKKVHvteergrKPA 362
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLESPDGVIDLNEAAEELG-------------VKKRRIYDITNVLEGLGLIEKKS-------KNK 60


                  ....*
gi 145580626  363 FKWIG 367
Cdd:pfam02319  61 IKWIG 65
PHA03247 PHA03247
large tegument protein UL36; Provisional
 575-862 6.27e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580626  575 DRSSEAPATVELSSAPSAQKRlceERKPQEEDEPATKRQSREYEDGPLSLVMPKKPSDSTDLASPKTMGNRasiplkdih 654
Cdd:PHA03247 2565 DRSVPPPRPAPRPSEPAVTSR---ARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPS--------- 2632

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580626  655 vngqlPAAEEISGKATANSlvssewGNPSRNTDVEKPSKENESTKEPSLLQYLCVQSPaglngfnvllSGSQTPPTVGPS 734
Cdd:PHA03247 2633 -----PAANEPDPHPPPTV------PPPERPRDDPAPGRVSRPRRARRLGRAAQASSP----------PQRPRRRAARPT 2691

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580626  735 SGQLPSFSVPCMvlPSPPLGPFPVLYSPAMPGPV--SSTLGALPNTgPVNFSLPGLGSIAQLLVGPTAVVNPKS-----S 807
Cdd:PHA03247 2692 VGSLTSLADPPP--PPPTPEPAPHALVSATPLPPgpAAARQASPAL-PAAPAPPAVPAGPATPGGPARPARPPTtagppA 2768

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145580626  808 TLPSADPQLQSQPSLNLSPVMSRSHSVVQQP------ESPVYVGHPVSVVKLHQSPVPVTP 862
Cdd:PHA03247 2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPspwdpaDPPAAVLAPAAALPPAASPAGPLP 2829
 
Name Accession Description Interval E-value
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 143-211 9.79e-28

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: 106.36  E-value: 9.79e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145580626  143 KQKSLGLLCQKFLARYPSYPlsteKTTISLDEVAVSLGVERRRIYDIVNVLESLHLVSRVAKNQYGWHG 211
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLESP----DGVIDLNEAAEELGVKKRRIYDITNVLEGLGLIEKKSKNKIKWIG 65
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 283-367 5.91e-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: 89.80  E-value: 5.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580626  283 KDKSLRIMSQKFVMLFLVSKTKIVTLDVAAKILIeesqdapdhskfkTKVRRLYDIANVLTSLALIKKVHvteergrKPA 362
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLESPDGVIDLNEAAEELG-------------VKKRRIYDITNVLEGLGLIEKKS-------KNK 60


                  ....*
gi 145580626  363 FKWIG 367
Cdd:pfam02319  61 IKWIG 65
PHA03247 PHA03247
large tegument protein UL36; Provisional
 575-862 6.27e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580626  575 DRSSEAPATVELSSAPSAQKRlceERKPQEEDEPATKRQSREYEDGPLSLVMPKKPSDSTDLASPKTMGNRasiplkdih 654
Cdd:PHA03247 2565 DRSVPPPRPAPRPSEPAVTSR---ARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPS--------- 2632

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580626  655 vngqlPAAEEISGKATANSlvssewGNPSRNTDVEKPSKENESTKEPSLLQYLCVQSPaglngfnvllSGSQTPPTVGPS 734
Cdd:PHA03247 2633 -----PAANEPDPHPPPTV------PPPERPRDDPAPGRVSRPRRARRLGRAAQASSP----------PQRPRRRAARPT 2691

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580626  735 SGQLPSFSVPCMvlPSPPLGPFPVLYSPAMPGPV--SSTLGALPNTgPVNFSLPGLGSIAQLLVGPTAVVNPKS-----S 807
Cdd:PHA03247 2692 VGSLTSLADPPP--PPPTPEPAPHALVSATPLPPgpAAARQASPAL-PAAPAPPAVPAGPATPGGPARPARPPTtagppA 2768

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145580626  808 TLPSADPQLQSQPSLNLSPVMSRSHSVVQQP------ESPVYVGHPVSVVKLHQSPVPVTP 862
Cdd:PHA03247 2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPspwdpaDPPAAVLAPAAALPPAASPAGPLP 2829
 
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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