InterPro : IPR009072

Name  Histone-fold Short Name  Histone-fold
Type  Domain Description  Histones mediate DNA organisation and plays a dominant role in regulating eukaryotic transcription. The histone-fold consists of a core of three helices, where the long middle helix is flanked at each end by shorter ones. The histone fold is a structural element that facilitates heterodimerisation [, , ]. Proteins displaying this structure include the nucleosome core histones, which form octomers composed of two copies of each of the four histones, H2A, H2B, H3 and H4; archaeal histone, which possesses only the core domain part of eukaryotic histone; and the TATA-box binding protein (TBP)-associated factors (TAF), where the histone fold is a common motif for mediating TAF-TAF interactions. TAF proteins include TAF(II)18 and TAF(II)28, which form a heterodimer, TAF(II)42 and TAF(II)62, which form a heterotetramer similar to (H3-H4)2, and the negative cofactor 2 (NC2) alpha and beta chains, which form a heterodimer. The TAF proteins are a component of transcription factor IID (TFIID), along with the TBP protein. TFIID forms part of the pre-initiation complex on core promoter elements required for RNA polymerase II-dependent transcription. The TAF subunits of TFIID mediate transcriptional activation of subsets of eukaryotic genes. The NC2 complex mediates the inhibition of TATA-dependent transcription through interactions with TBP.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



4 Child Features

Id Name Short Name Type
IPR007125 Histone core Histone_core_D Domain
IPR003958 Transcription factor CBF/NF-Y/archaeal histone CBFA_NFYB_domain Domain
IPR003228 Transcription initiation factor TFIID TFIID_sub Domain
IPR004823 TATA box binding protein associated factor (TAF) TAF_TATA-bd Domain

2 Contains

Id Name Short Name Type
IPR019809 Histone H4, conserved site Histone_H4_CS Conserved_site
IPR003956 Transcription factor, NFYB/HAP3, conserved site Transcrpt_fac_NFYB/HAP3_CS Conserved_site

3 Found In

Id Name Short Name Type
IPR003195 Transcription initiation factor IID, 18kDa subunit TFIID-18 Family
IPR006809 TAFII28-like protein TAFII28 Family
IPR021171 Core histone macro-H2A Core_histone_macro-H2A Family

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Hartlepp KF The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions. 2005 Mol Cell Biol 25 9886-96
Goppelt A A mechanism for repression of class II gene transcription through specific binding of NC2 to TBP-promoter complexes via heterodimeric histone fold domains. 1996 EMBO J 15 3105-16
Kim IS Determination of functional domains in the C subunit of the CCAAT-binding factor (CBF) necessary for formation of a CBF-DNA complex: CBF-B interacts simultaneously with both the CBF-A and CBF-C subunits to form a heterotrimeric CBF molecule. 1996 Mol Cell Biol 16 4003-13

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)