PROSITE documentation PDOC51895Alt a 1 (AA1)-like domain profile
Alt a 1 family proteins (AA1s) have only been observed in the Dothideomycetes and Sordariomycetes classes of fungi. AA1-like proteins are fungal toxins that can induce plant defense responses and cell death. They may contribute to virulence by protecting the cell wall, thus allowing fungal growth to be maintained and preventing the recognition of degraded β-1,3-glucan by the plant [1,2,3,4].
AA1 proteins comprise ~150 amino acids and contain two pairs of highly conserved disulfide bonds. They have a unique 11-stranded β-barrel fold with one 3-residue 3(10) helix (see <PDB:3V0R>). The Cys1-Cys2 bridge connects strand β3 and a fragment of the chain in the vicinity of strand β4. The Cys3-Cys4 bridge links two neighboring β-strands, β7b and β8a [1,2,3].
Some proteins known to contain an AA1-like domain are listed below:
- Alternaria alternata Alt a 1 (Aa1), involved in spore germination. It is a highly allergenic protein responsible for several respiratory diseases.
- Alternaria brassicicola Alt b 1 (Ab1), a homolog of Aa1.
- Verticillium dahliae effector protein PevD1, exhibits an elicitor-like activity by inducing denfense responses in tobacco plants.
The profile we developed covers the entire AA1-like domain.
Last update:May 2019 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Chruszcz M. Chapman M.D. Osinski T. Solberg R. Demas M. Porebski P.J. Majorek K.A. Pomes A. Minor W. |
| Title | Alternaria alternata allergen Alt a 1: a unique beta-barrel protein dimer found exclusively in fungi. | |
| Source | J. Allergy. Clin. Immunol. 130:241-7.e9(2012). | |
| PubMed ID | 22664167 | |
| DOI | 10.1016/j.jaci.2012.03.047 |
| 2 | Authors | Garrido-Arandia M. Bretones J. Gomez-Casado C. Cubells N. Diaz-Perales A. Pacios L.F. |
| Title | Computational study of pH-dependent oligomerization and ligand binding in Alt a 1, a highly allergenic protein with a unique fold. | |
| Source | J. Comput. Aided. Mol. Des. 30:365-379(2016). | |
| PubMed ID | 27090909 | |
| DOI | 10.1007/s10822-016-9911-6 |
| 3 | Authors | Zhou R. Zhu T. Han L. Liu M. Xu M. Liu Y. Han D. Qiu D. Gong Q. Liu X. |
| Title | The asparagine-rich protein NRP interacts with the Verticillium effector PevD1 and regulates the subcellular localization of cryptochrome 2. | |
| Source | J. Exp. Bot. 68:3427-3440(2017). | |
| PubMed ID | 28633330 | |
| DOI | 10.1093/jxb/erx192 |
| 4 | Authors | Zhang Y. Gao Y. Liang Y. Dong Y. Yang X. Qiu D. |
| Title | Verticillium dahliae PevD1, an Alt a 1-like protein, targets cotton PR5-like protein and promotes fungal infection. | |
| Source | J. Exp. Bot. 70:613-626(2019). | |
| PubMed ID | 30295911 | |
| DOI | 10.1093/jxb/ery351 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)