InterPro : IPR017919

Name  Transcription factor TFE/TFIIEalpha HTH domain Short Name  TFIIE/TFIIEa_HTH
Type  Domain Description  Initiation of eukaryotic mRNA transcription requires melting of promoter DNA with the help of the general transcription factors TFIIE and TFIIH. In higher eukaryotes, the general transcription factor TFIIE consists of two subunits: the large alpha subunit () and the small beta (). TFIIE beta has been found to bind to the region where the promoter starts to open to be single-stranded upon transcription initiation by RNA polymerase II. The approximately 120-residue central core domain of TFIIE beta plays a role in double-stranded DNA binding of TFIIE [].The TFIIE beta central core DNA-binding domain consists of three helices with a beta hairpin at the C terminus, resembling the winged helix proteins. It shows a novel double-stranded DNA-binding activity where the DNA-binding surface locates on the opposite side to the previously reported winged helix motif by forming a positively charged furrow [].Archaea contain a TFIIE homolog, called TFE, which corresponds to the N-terminal half of TFIIEalpha. It appears that archaeal TFE corresponds to the minimal essential region of eukaryotic TFIIEalpha. In archaea TFE contains an N-terminal, weakly conserved, helix-turn-helix (HTH) motif within a leucine-rich region and a C-terminal zinc ribbon [, , ]. It has been proposed that the TFE/IIEalpha-type HTH domain acts as a bridging factor or adapter between the TATA box-binding protein, the polymerase, and possibly promoter DNA [].The TFE/IIEalpha-type HTH domain adopts a winged HTH (winged helix) fold, comprising three alpha-helices and three beta-strands in the canonical order alpha1-beta1-alpha2-alpha3-beta2-beta3. Conserved residues within helices alpha1-alpha3 form the tightly packed hydrophobic core of the winged helix domain. A specific feature of the structure is the extension of the canonical winged helix fold at the N and C termini by the additional helices alpha0 and alpha4, respectively. Hydrophobic residues from the additional helix alpha0 extend the hydrophobic core of the winged helix domain, and helix alpha0 is tightly packed against the canonical winged helix fold. Helix alpha4 comprises only one turn [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

3 Found In

Id Name Short Name Type
IPR011991 Winged helix-turn-helix DNA-binding domain WHTH_DNA-bd_dom Domain
IPR002853 Transcription factor TFIIE, alpha subunit TFIIE_asu Family
IPR016481 Transcription factor TFE, archaea TF_E_archaea Family

1 Parent Features

Id Name Short Name Type
IPR024550 TFIIEalpha/SarR/Rpc3 HTH domain TFIIEa/SarR/Rpc3_HTH_dom Domain

6 Publications

First Author Title Year Journal Volume Pages
Okuda M Structure of the central core domain of TFIIEbeta with a novel double-stranded DNA-binding surface. 2000 EMBO J 19 1346-56
Kuldell NH Genetic analysis of the large subunit of yeast transcription factor IIE reveals two regions with distinct functions. 1997 Mol Cell Biol 17 5288-98
Bell SD The archaeal TFIIEalpha homologue facilitates transcription initiation by enhancing TATA-box recognition. 2001 EMBO Rep 2 133-8
Hanzelka BL TFE, an archaeal transcription factor in Methanobacterium thermoautotrophicum related to eucaryal transcription factor TFIIEalpha. 2001 J Bacteriol 183 1813-8
Pastorelli R Effect of butylated hydroxyanisole on the metabolism of N-nitrosodi-n-butylamine and N-nitrosobutyl(4-hydroxybutyl)amine by rat hepatic S9 preparations in vitro. 1987 IARC Sci Publ   183-4
Meinhart A An extended winged helix domain in general transcription factor E/IIE alpha. 2003 J Biol Chem 278 48267-74

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)