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. 2023 Feb 12;9(2):244. doi: 10.3390/jof9020244

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© 2023 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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In silico analysis of Sterol 24-C-methyltransferase (EGR6) of Fusarium equiseti. (A) Multiple sequence alignments of EGR6 from F. oxysporum (FoEGR6; XP_031038350.1) and F. equiseti (FeEGR6; CAG7563035.1). Black shading denotes conserved amino acids, while white background denotes a low similarity score. Red and blue lines below the sequences indicate the conserved domains of Sterol methyltransferase and SAM−dependent methyltransferase, respectively. Whiskers suggest the beginning and the ending of each domain. (B) The predicted crystallographic three-dimensional (3D) modeling of 24-C-methyltransferase from F. equiseti (FeEGR6; CAG7563035.1). (C) Model–template alignment of FeEGR6 from F. equiseti. GMQE: Global model quality.