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. 2018 May 4;9(1):866–878. doi: 10.1080/21505594.2018.1456228

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© 2018 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — The C. albicans Orf19.1725 protein potentially functions as an adhesin. (A) Analysis of Orf19.1725 reveals three conserved features, a putative signal peptide, four different tandem repeats (TR1, TR2, TR3 and TR4) and a hypothetical ω site. (B) Protein sequence of C. albicans orf19.1725. The arrow between the 26th (Gly) and 27th (Leu) amino acids indicates the likely cleavage site for the signal peptide (http://www.cbs.dtu.dk/services/SignalP/). The other, at the position of the 700th amino acid (Asp), was predicted to be an ω site with lower specificity (http://gpcr.biocomp.unibo.it/predgpi/). (C) Sequence motifs of four different tandem repeats of Orf19.1725 (http://weblogo.threeplusone.com/create.cgi).