NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|71989919|ref|NP_495771|]
View 

Transcription factor efl-3 [Caenorhabditis elegans]

Protein Classification

E2F family transcription factor( domain architecture ID 10491890)

atypical E2F family transcription factor acts as a transcription repressor that binds DNA independently of DP proteins, 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

CATH:  1.10.10.10
Gene Ontology:  GO:0006357|GO:0003700|GO:1990837
PubMed:  19201609|10090723|26632596|37592750|10521653
SCOP:  4000205

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 96-164 1.01e-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: 91.72  E-value: 1.01e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71989919    96 KEKSLGLLCQRFLIAINEetvgSSTREVHLETVARKMNVEKRRIYDIVNVMEALDAMQKTNKSYYQWQG 164
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLE----SPDGVIDLNEAAEELGVKKRRIYDITNVLEGLGLIEKKSKNKIKWIG 65
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 259-328 2.04e-13

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: 65.15  E-value: 2.04e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989919   259 NSLAQLCRRFLMVLLSNPKNIrkVSLDVASTVLIkdpetegfeppsrSRCRRLYDIANVLVALGLIKKVH 328
Cdd:pfam02319   3 KSLGLLTQKFLELLLESPDGV--IDLNEAAEELG-------------VKKRRIYDITNVLEGLGLIEKKS 57
 
Name Accession Description Interval E-value
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 96-164 1.01e-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: 91.72  E-value: 1.01e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71989919    96 KEKSLGLLCQRFLIAINEetvgSSTREVHLETVARKMNVEKRRIYDIVNVMEALDAMQKTNKSYYQWQG 164
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLE----SPDGVIDLNEAAEELGVKKRRIYDITNVLEGLGLIEKKSKNKIKWIG 65
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 259-328 2.04e-13

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: 65.15  E-value: 2.04e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989919   259 NSLAQLCRRFLMVLLSNPKNIrkVSLDVASTVLIkdpetegfeppsrSRCRRLYDIANVLVALGLIKKVH 328
Cdd:pfam02319   3 KSLGLLTQKFLELLLESPDGV--IDLNEAAEELG-------------VKKRRIYDITNVLEGLGLIEKKS 57
 
Name Accession Description Interval E-value
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 96-164 1.01e-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: 91.72  E-value: 1.01e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71989919    96 KEKSLGLLCQRFLIAINEetvgSSTREVHLETVARKMNVEKRRIYDIVNVMEALDAMQKTNKSYYQWQG 164
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLE----SPDGVIDLNEAAEELGVKKRRIYDITNVLEGLGLIEKKSKNKIKWIG 65
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 259-328 2.04e-13

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: 65.15  E-value: 2.04e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989919   259 NSLAQLCRRFLMVLLSNPKNIrkVSLDVASTVLIkdpetegfeppsrSRCRRLYDIANVLVALGLIKKVH 328
Cdd:pfam02319   3 KSLGLLTQKFLELLLESPDGV--IDLNEAAEELG-------------VKKRRIYDITNVLEGLGLIEKKS 57
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH