Razor: annotation of signal peptides from toxins

Abstract

ABSTRACTMotivationSignal peptides are responsible for protein transport and secretion and are ubiquitous to all forms of life. The annotation of signal peptides is important for understanding protein translocation and toxin secretion and evolution.ResultsHere we explore the features of these signal sequences from eukaryotic proteins. Strikingly, we find that the signal peptides from secretory toxins have common features across kingdoms, supporting the idea of horizontal gene transfer or convergence of toxin genes across kingdoms. We leverage these features to build Razor, a simple yet powerful tool specialised in identifying signal peptides from toxins using the first 23 N-terminal residues. We demonstrate the usability of Razor by analysing all the sequences reviewed by UniProt. Indeed, Razor is able to identify toxins using their N-terminal sequences only. Strikingly, we also discover that many defensive proteins across kingdoms harbour a toxin-like signal peptide; some of these defensive proteins have emerged through convergent evolution, e.g. defensin and defensin-like protein families, and phospholipase families. In sum, Razor uses an approach independent of homology search to identify novel and known toxin classes across species using N-terminal residues.Availability and implementationRazor is available as a web application (https://tisigner.com/razor) and a command-line tool (https://github.com/Gardner-BinfLab/Razor).