{PDOC51895}
{PS51895; AA1}
{BEGIN}
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* Alt a 1 (AA1)-like domain profile *
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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 beta-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 beta-barrel fold
with one 3-residue 3(10) helix (see <PDB:3V0R>). The Cys1-Cys2 bridge connects
strand beta3  and a fragment of the chain in the vicinity of strand beta4. The
Cys3-Cys4 bridge   links  two  neighboring  beta-strands,  beta7b  and  beta8a
[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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: May 2019 / First entry.

[ 1] Chruszcz M., Chapman M.D., Osinski T., Solberg R., Demas M.,
     Porebski P.J., Majorek K.A., Pomes A., Minor W.
     "Alternaria alternata allergen Alt a 1: a unique beta-barrel protein
     dimer found exclusively in fungi."
     J. Allergy. Clin. Immunol. 130:241-7.e9(2012).
     PubMed=22664167; DOI=10.1016/j.jaci.2012.03.047
[ 2] Garrido-Arandia M., Bretones J., Gomez-Casado C., Cubells N.,
     Diaz-Perales A., Pacios L.F.
     "Computational study of pH-dependent oligomerization and ligand
     binding in Alt a 1, a highly allergenic protein with a unique fold."
     J. Comput. Aided. Mol. Des. 30:365-379(2016).
     PubMed=27090909; DOI=10.1007/s10822-016-9911-6
[ 3] Zhou R., Zhu T., Han L., Liu M., Xu M., Liu Y., Han D., Qiu D.,
     Gong Q., Liu X.
     "The asparagine-rich protein NRP interacts with the Verticillium
     effector PevD1 and regulates the subcellular localization of
     cryptochrome 2."
     J. Exp. Bot. 68:3427-3440(2017).
     PubMed=28633330; DOI=10.1093/jxb/erx192
[ 4] Zhang Y., Gao Y., Liang Y., Dong Y., Yang X., Qiu D.
     "Verticillium dahliae PevD1, an Alt a 1-like protein, targets cotton
     PR5-like protein and promotes fungal infection."
     J. Exp. Bot. 70:613-626(2019).
     PubMed=30295911; DOI=10.1093/jxb/ery351

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