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. 2024 May 9;33(6):e4999. doi: 10.1002/pro.4999

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© 2024 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.

This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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Sequence features of EVA‐ACA1001. (a) EVA‐ACA1001 sequence showing the conserved disulfide bonds in subclass A1 and A3 evasins (yellow), the additional disulfide pair unique to subclass A3 evasins (red), the N‐terminus (green), and the C‐terminus (blue). (b) Multiple sequence alignment (obtained using Clustal Omega) of the class A3 evasins EVA‐ACA1001 and EVA‐AAM1001 and the class A1 evasins EVA‐1 and EVA‐P974. Highlighted residues are conserved cysteines (yellow), additional cysteines in class A3 evasins (red), conserved glycines (green), putative tyrosine sulfation sites (magenta), and potential N‐linked glycosylation sites (cyan).