Fig. 1: Structural and functional characterization of KERP2 through in silico analysis. | Nature Communications

Fig. 1: Structural and functional characterization of KERP2 through in silico analysis.

From: A multifaceted model of Entamoeba histolytica KERP2 regulating gene expression and host cell responses

Fig. 1: Structural and functional characterization of KERP2 through in silico analysis.The alternative text for this image may have been generated using AI.

a Maximum likelihood phylogenetic tree of KERP2 (EHI_065630) and homologous sequences across eukaryotic taxa, constructed using IQ-TREE and visualized with iTOL. The circular display represents bootstrap values with color gradients, while the rectangular display provides a simplified view for clarity, focusing on Entamoeba species. Bootstrap values are indicated at major branch points. b Multiple sequence alignment of the KERP2 SAP domain (amino acids 104–141) with representative SAP domains from other organisms, constructed as described in ref. 17. Conserved residues associated with DNA binding are highlighted by residue properties: hydrophobic (yellow), small (green), polar (purple), and bulky (gray). c Predicted secondary structures, shown schematically, feature two amphipathic helices characteristic of the SAP domain. Structural model of KERP2 generated by I-TASSER (white) showing conserved architecture resembling the N-terminal region of DEK proteins, including the embedded SAP domain (green; PDB ID: 2JX3). d Sequence analysis identifies a coiled-coil domain in the C-terminal region (amino acids 178–216) predicted by PCOILS and MARCOIL. Source data are provided as a Source Data file. e Schematic representation of the domain architecture of KERP2, highlighting the SAP domain (green), coiled-coil domain (purple), and nuclear localization signal (NLS, red line).

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