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. 2022 Dec 22;12:22168. doi: 10.1038/s41598-022-26867-8

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Amino acid sequence alignments of the peptide toxins of X. aruana venom with homologues from other Apidae venoms. (a) XYTX₁-Xa1a alignment with Xac-1 (Uniprot: C0HKQ5), Xac-2 (Uniprot: C0HKQ6), melectin (Uniprot: P86170), bombolitin (Uniprot: D0VDZ4) and melittin (Uniprot: P01501). (b) XYTX₂-Xa2a alignment with apamin (Uniprot: P01500), Bombus MCD-peptide (Uniprot: P04567) and Apis MCD-peptide (Uniprot: P01499). Methionine, lysine/arginine, aspartate/glutamate, and cysteine residues and stop codons are highlighted in purple, blue, red, yellow and black, respectively. Signal peptides and mature peptides are underlined in purple and grey, respectively. Post-translational modifications are not shown.