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The alignment of P-type ATPase-like domains of TgATPaseP-GC, PfGCα, and PfGCβ with the members of human P4-ATPases. The alignment of P-type ATPase-like.

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Presentation on theme: "The alignment of P-type ATPase-like domains of TgATPaseP-GC, PfGCα, and PfGCβ with the members of human P4-ATPases. The alignment of P-type ATPase-like."— Presentation transcript:

1 The alignment of P-type ATPase-like domains of TgATPaseP-GC, PfGCα, and PfGCβ with the members of human P4-ATPases. The alignment of P-type ATPase-like domains of TgATPaseP-GC, PfGCα, and PfGCβ with the members of human P4-ATPases. The human P4-ATPases were aligned by MAFFT alignment server (v7) (Katoh & Standley, 2013), and then merged with the aligned ATPase domains of TgATPaseP-GC, PfGCα, and PfGCβ using MAFFT merge. The alignment was trimmed, as indicated by horizontal lines, and signature residues were color-coded with the Clustal Omega program (>30% sequence conservation). Selected amino acids that are essential for ATP binding and phosphorylation, and transmembrane helices are boxed in black. Transmembrane topology of ATP8A1 retrieved from TMHMM Server (v2) (Sonnhammer et al, 1998) was used as a reference. Organism abbreviations and accession numbers: P-type ATPase-like domain of TgATPaseP-GC, T. gondii (EPR ); PfGCα, P. falciparum (AJ ); PfGCβ, P. falciparum (AJ ); and P4-ATPases of Homo sapiens: ATP8A1 (Q9Y2Q0.1), ATP8B4 (Q8TF62.3), ATP9A (O ), ATP10A (O ), and ATP11C (Q8NB49.3). Özlem Günay-Esiyok et al. LSA 2019;2:e © 2019 Günay-Esiyok et al.


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