The TEA domain is a DNA-binding region of ~80 amino acids that has been named
after the two proteins that originally defined the domain: TEF-1 and AbaA. It
is also referred to as the ATTS domain because of the 4 proteins first found
to harbor this motif (AbaA and TEC1 in yeast, TEF1/TEAD1 in vertebrates and
Scalloped in fly). The TEA domain is located toward the amino terminus of
eukaryotic transcription factors of the TEA/ATTS family. The consensus DNA
sequence bound by an isolated TEA domain is N-[ATG]-G-[ATC]-A-T-N-T; where,
N=A, T, C. or G [1,2,3,4].
The TEA domain is composed of a three-helix bundle with a homeodomain fold
(see <PDB:2HZD>). It has a folded globular structure made of three α-helices, H1, H2, and H3. H1 and H2 are nearly anti-parallel and pack on either
side of the H3, which is the DNA-recognition helix of the TEA domain. Two
conserved serines are found on the DNA-binding surface. Phosphorylation of one
or both of these could interfere with DNA-binding activity, by introducing
electrostatic repulsion and/or steric hindrance, and help regulate TEA/ATTS
transcription factor activity [3,4].
Some of the proteins that contain a TEA domain are listed below:
Mammalian enhancer factor TEF-1. TEF-1 can bind to two distinct sequences
in the SV40 enhancer and is a transcriptional activator.
Mammalian TEF-3, TEF-4 and TEF-5 , putative transcriptional activators
highly similar to TEF-1.
Drosophila scalloped protein (gene sd), a probable transcription factor
that functions in the regulation of cell-specific gene expression during
Drosophila development, particularly in the differentiation of the nervous
Emericella nidulans regulatory protein abaA. AbaA is involved in the
regulation of conidiation (asexual spore); its expression leads to the
cessation of vegetative growth.
Yeast trans-acting factor TEC1. TEC1 is involved in the activation of the
Caenorhabditis elegans hypothetical protein F28B12.2.
We developed both a pattern and a profile. The pattern covers helices H2 and
H3, whereas the profile covers the whole domain.
January 2017 / Profile and text revised.
PROSITE methods (with tools and information) covered by this documentation:
The TEA domain: a novel, highly conserved DNA-binding motif.
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