The experimentally confirmed O-glycosylated positions in this set of 30 proteins were analyzed with the macro XRR to identify highly O-glycosylated regions, with the parameters set to result in low stringency (%G = 15, W = 20, S = 5). A total of 13 hyper-O-glycosylated regions were found in 12 of the 30 protein sequences (one protein displayed two separate
regions), with an average length of 56 residues. Ser/Thr content in these regions resulted to be 38.5% ± 10.5, a value similar to that obtained for mucin domains in animal proteins [10]. Acknowledegments Support for this research was provided by grants from the Ministerio de Adriamycin Educación y Ciencia (AGL2010-22222) and Gobierno de Canarias (PI2007/009). M.G. was supported by Gobierno see more de Canarias. Electronic supplementary material Additional file 1: Comparison of experimental O -glycosylation sites found in fungal proteins with those predicted by NetOGlyc 3.1 ( http://www.cbs.dtu.dk/services/NetOGlyc/ ). (XLSX 18 KB) Additional file 2: List of SignalP-positive proteins for the eight fungal genomes with the O -glycosylation sites predicted by NetOGlyc. (ZIP 4 MB) Additional file 3: Results of the search for pHGRs (predicted Hyper- O -glycosylated Regions) in the SignalP-positive proteins coded by
the eight fungal genomes. (PDF 2 MB) Additional file 4: Microsoft Excel spreadsheet with the macro XRR used in the search for Ser/Thr-rich regions and pHGRs (predicted Hyper- O -glycosylated Regions). (XLSX 3 MB) References 1. Hanisch FG: O -glycosylation of the mucin type. Biol Chem 2001, 382:143–149.PubMedCrossRef 2. Goto M: Protein O -glycosylation in fungi: Staurosporine diverse structures and multiple functions. Biosci Biotechnol Biochem PIK-5 2007, 71:1415–1427.PubMedCrossRef 3. Lommel M, Strahl S: Protein O-mannosylation: conserved from bacteria to humans. Glycobiology 2009, 19:816.PubMedCrossRef 4. Lehle L, Strahl S, Tanner W: Protein glycosylation, conserved
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