Characterization of gene structure features of PMT protein family in Magnaporthe oryzae
To clarify the structure characteristics and the possible biological functions of the dolichyl- phosphate-mannose-protein mannosyltransferase encoding gene PMTs in Magnaporthe oryzae, the sequences of PMTs were analyzed. The results showed that the Mo PMTs are conservative in the structure of amino acid and highly homologous with the PMT protein from Botrytis cinerea, Neurospora crassa, Gibberella zeae, and Aspergillus nidulans. Further bioinformatics analysis indicated the protein of PMT is a nonsecreted protein without a signal peptide, contains transmembrane domains, and localices at the endoplasmic reticulum, and has conserved domain of PMT motif and MIR motif. These results will facilitate the further studies on the mechanism of PMTs in M. oryzae.