| Description | The APSES (ASM-1, Phd1, StuA, EFG1, and Sok2) domain is a ~110-residue sequence-specific DNA-binding domain found in a family of fungal transcription factors and other DNA-binding proteins. The APSES domain is found associated with ankyrin repeats (see , ) and a heterodimerization domain [ , ].The APSES domain consists of a six-stranded β-sheet segment folded against two pairs of α-helices in the topology of the winged helix-turn-helix (HTH) family of proteins [ ]. The αA/αB helical pair corresponds to the HTH motif [, , ]. Some proteins known to contain an APSES domain are listed below:Saccharomyces cerevisiae (Baker's yeast) Mlu-1 box binding protein (MBP1, ); Mlu-1 and Swi6 together make up the transcription factor complex MBF (Mlu-1-binding factor), which binds to the Mlu1 cell-cycle box (MCB) elements found in the promoters of many DNA synthesis genes [ ].Schizosaccharomyces pombe (Fission yeast) cell division cycle-related proteins res1/sct1 ( ) and res2/pct1 ( ), which are homologous to MBP1. S. pombe start control protein cdc10 ( ). Emericella nidulans (Aspergillus nidulans) cell pattern formation-associated protein stuA ( ). It regulates the transformation of undifferentiated hyphal elements into a complex multicellular structure. S. cerevisiae transcription factor PHD1 ( ). S. cerevisiae protein SOK2 ( ). It represses the transition from unicellular growth to pseudohyphae. Candida albicans (Yeast) enhanced filamentous growth protein (EFG1, )). Neurospora crassa ascospore maturation 1 protein (Asm-1, ). It has a role in spore maturation.S. pombe bouquet formation protein 4 ( ), which is a nuclear membrane protein that connects telomeres to the nuclear envelop (NE) during both vegetative growth and meiosis. Bqt4 does not seem to bind DNA, but acts as an adaptor between Bqt3 and Rap1 [ ]. | Name | Transcription regulator HTH, APSES-type DNA-binding domain |
| Short Name | Tscrpt_reg_HTH_APSES-type | Type | Domain |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
