The domain within your query sequence starts at position 206 and ends at position 293; the E-value for the ETS domain shown below is 1.84e-52.



erythroblast transformation specific domain
SMART accession number:SM00413
Description: variation of the helix-turn-helix motif
Interpro abstract (IPR000418):

Transcription factors are protein molecules that bind to specific DNA sequences in the genome, resulting in the induction or inhibition of gene transcription [ (PUBMED:2163347) ]. The ets oncogene is such a factor, possessing a region of 85-90 amino acids known as the ETS (erythroblast transformation specific) domain [ (PUBMED:2163347) (PUBMED:2253872) (PUBMED:14693367) ]. This domain is rich in positively-charged and aromatic residues, and binds to purine-rich segments of DNA. The ETS domain has been identified in other transcription factors such as PU.1, human erg, human elf-1, human elk-1, GA binding protein, and a number of others [ (PUBMED:2163347) (PUBMED:2253872) (PUBMED:8425553) ]. It is generally localized at the C terminus of the protein, with the exception of ELF-1, ELK-1, ELK-3, ELK-4 and ERF where it is found at the N terminus.

NMR-analysis of the structure of the Ets domains revealed that it contains three alpha-helixes (1-3) and four-stranded beta-sheets (1-4) arranged in the order alpha1-beta1-beta2-alpha2-alpha3-beta3-beta4 forming a winged helix-turn-helix (wHTH) topology [ (PUBMED:12559563) ]. The third alpha-helix is responsive to contact to the major groove of the DNA. Different members of the Ets family proteins display distinct DNA binding specificities. The Ets domains and the flanking amino acid sequences of the proteins influence the binding affinity, and the alteration of a single amino acid in the Ets domain can change its DNA binding specificities.

GO process:regulation of transcription, DNA-templated (GO:0006355)
GO function:sequence-specific DNA binding (GO:0043565), DNA-binding transcription factor activity (GO:0003700)
Family alignment:
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There are 14302 ETS domains in 14280 proteins in SMART's nrdb database.

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