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. 2019 May 31;9:8120. doi: 10.1038/s41598-019-44542-3

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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In silico annotation of PfpTKL interaction motifs and domains. (a) Plasmodium PfpTKL homologs share common N-terminal features beside the MORN motif(s). The alignment was created with MAFFT⁸⁹ and residues 100% conserved over all of the sequences were shaded using BioEdit v7.2.5¹¹⁶. The putative N-myristoylation site is shown in red. (b) Plasmodium PfpTKL homologs possess one or two RVxF motifs. The alignment was created with MAFFT⁸⁹. RVxF motif consensus sequences used in silico to detect RVxF1 and RVxF2 are displayed below the alignment^86,87. (c) The PfpTKL SAM undergoes classic folding. Tertiary structure PfpTKL SAM predicted with Phyre2⁸¹ (75 residues (97%) modeled at >90% accuracy). Structure annotation and shading were achieved with Chimera v1.10.1¹¹⁷. (d) Plasmodium SAMs showing classic composition compared with SAM references. Sequence alignment created with MAFFT⁸⁹ between the four P. falciparum SAMs and reference SAMs (Sdiclina = Saprolegnia diclina, Scerevisiae = Saccharomyces cerevisiae, Spombe = Schizosaccharomyces pombe, Ddiscoideum = Dictyostelium discoideum). Conserved residues were shaded using BioEdit v7.2.5¹¹⁶. Arrows indicate residues conserved in SAMs. Below the alignment are delineated the five α-helices (H1-H5) of the SAM core¹¹⁸.