ET-binding motif (EBM) of Saccharomyces cerevisiae ATP-dependent helicase STH1 and similar proteins
STH1/Sth1p (EC 3.6.4.12; also called nuclear protein STH1/NPS1, chromatin structure-remodeling complex protein STH1, or SNF2 homolog) is a Snf2p/Swi2p homolog that acts as a catalytic component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. STH1 is an essential ATPase in RSC and differs from Snf/Swi in its interactions with histones and chromatin-associated proteins. It is a DNA translocase capable of nucleosome remodeling and is required for full expression of early meiotic genes. STH1 plays an essential role for mitotic growth and repression of CHA1 expression. It is also involved in G2 phase control. This model corresponds to a conserved region of STH1, which is responsible for the binding of the extra-terminal (ET) domain of TBP associated factor 14 (Taf14), a transcriptional regulator that controls diverse physiological processes and that physically interacts with at least seven nuclear complexes in yeast.
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