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PROSITE documentation PDOC51299APSES-type HTH DNA-binding domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51299
The APSES (ASM-1, Phd1, StuA, EFG1, and Sok2) domain is an ~110-residue sequence-specific DNA-binding domain found in a family of fungal transcription factors that regulate development or cell cycle progression. The APSES domain is found associated with ankyrin repeats (see <PDOC50088>) and a heterodimerization domain [1,2].
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 (see <PDB:1L3G>). The αA/αB helical pair corresponds to the HTH motif [3,4,5].
Some proteins known to contain an APSES domain are listed below:
- Saccharomyces cerevisiae Mlu-1 box binding protein (MBP1), a cell cycle transcription factor.
- Schizosaccharomyces pombe cell division cycle-related proteins res1/sct1 and res2/pct1, which are homologous to MBP1.
- Schizosaccharomyces 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.
- Saccharomyces cerevisiae transcription factor PHD1.
- Saccharomyces cerevisiae protein SOK2. It represses the transition from unicellular growth to pseudohyphae.
- Candida albicans enhanced filamentous growth protein (EFG1).
- Neurospora crassa ascospore maturation 1 protein (Asm-1). It has a role in spore maturation.
The profile we developed covers the entire APSES domain.
Last update:March 2007 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Aramayo R. Peleg Y. Addison R. Metzenberg R. |
| Title | Asm-1+, a Neurospora crassa gene related to transcriptional regulators of fungal development. | |
| Source | Genetics 144:991-1003(1996). | |
| PubMed ID | 8913744 |
| 2 | Authors | Dutton J.R. Johns S. Miller B.L. |
| Title | StuAp is a sequence-specific transcription factor that regulates developmental complexity in Aspergillus nidulans. | |
| Source | EMBO J. 16:5710-5721(1997). | |
| PubMed ID | 9312029 | |
| DOI | 10.1093/emboj/16.18.5710 |
| 3 | Authors | Xu R.-M. Koch C. Liu Y. Horton J.R. Knapp D. Nasmyth K. Cheng X. |
| Title | Crystal structure of the DNA-binding domain of Mbp1, a transcription factor important in cell-cycle control of DNA synthesis. | |
| Source | Structure 5:349-358(1997). | |
| PubMed ID | 9083114 |
| 4 | Authors | Taylor I.A. Treiber M.K. Olivi L. Smerdon S.J. |
| Title | The X-ray structure of the DNA-binding domain from the Saccharomyces cerevisiae cell-cycle transcription factor Mbp1 at 2.1 A resolution. | |
| Source | J. Mol. Biol. 272:1-8(1997). | |
| PubMed ID | 9299332 | |
| DOI | 10.1006/jmbi.1997.1229 |
| 5 | Authors | Nair M. McIntosh P.B. Frenkiel T.A. Kelly G. Taylor I.A. Smerdon S.J. Lane A.N. |
| Title | NMR structure of the DNA-binding domain of the cell cycle protein Mbp1 from Saccharomyces cerevisiae. | |
| Source | Biochemistry 42:1266-1273(2003). | |
| PubMed ID | 12564929 | |
| DOI | 10.1021/bi0205247 |
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