Multiple sequence alignment of CIA proteins.

<p>(<b>A</b>-<b>B</b>) ClustalW alignment of <i>Pf</i>NBP35 (A) and <i>Pf</i>CFD1 (B) with their homologs. NBP35 homologs: TgNbp35 from <i>T</i>. <i>gondii</i>, AtNbp35 from <i>A</i>. <i>thaliana</i>, HsNbp35 from <i>H</i>. <i>sapiens</i>, ScNbp35 from <i>S</i>. <i>cerevisiae</i>, and C.alb Nbp35 from <i>Candida albicans</i>. CFD1 homologs: HsNubp2 from <i>H</i>. <i>sapiens</i>, ScCfd1 from <i>S</i>. <i>cerevisiae</i>, and Calbcfd1 from <i>C</i>. <i>albicans</i>. Arrows mark the start and end of recombinant <i>Pf</i>NBP35 and <i>Pf</i>CFD1. The predicted transmembrane domain of <i>Pf</i>NBP35 is indicated by a navy blue dashed box.</p> <p>(PDF)</p>

Publication Details

Journal
Figshare
Published
2024-09-30
DOI
https://doi.org/10.1371/journal.ppat.1012593.s008
Primary Topic
Cell Adhesion Molecules Research
Type
article
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article

Multiple sequence alignment of CIA proteins.

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Cell Adhesion Molecules Research
article

Multiple sequence alignment of CIA proteins.

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Abstract

<p>(<b>A</b>-<b>B</b>) ClustalW alignment of <i>Pf</i>NBP35 (A) and <i>Pf</i>CFD1 (B) with their homologs. NBP35 homologs: TgNbp35 from <i>T</i>. <i>gondii</i>, AtNbp35 from <i>A</i>. <i>thaliana</i>, HsNbp35 from <i>H</i>. <i>sapiens</i>, ScNbp35 from <i>S</i>. <i>cerevisiae</i>, and C.alb Nbp35 from <i>Candida albicans</i>. CFD1 homologs: HsNubp2 from <i>H</i>. <i>sapiens</i>, ScCfd1 from <i>S</i>. <i>cerevisiae</i>, and Calbcfd1 from <i>C</i>. <i>albicans</i>. Arrows mark the start and end of recombinant <i>Pf</i>NBP35 and <i>Pf</i>CFD1. The predicted transmembrane domain of <i>Pf</i>NBP35 is indicated by a navy blue dashed box.</p> <p>(PDF)</p>

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Cell Adhesion Molecules Research
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