Improved detection and phylogenetic analysis of plant proteins containing LysM domains

Plants perceive N-acetyl-d-glucosamine-containing oligosaccharides that play a role in the interaction with bacteria and fungi, through cell-surface receptors containing a tight bundle of three LysM domains in their extracellular region. However, the identification of LysM domains of receptor-like kinases (RLK)/receptor-like proteins (RLP) using sequence based methods has led to some ambiguity, as some proteins have been annotated with only one or two LysM domains. This missing annotation was likely produced by the failure of the LysM hidden Markov model (HMM) from the Pfam database to correctly identify some LysM domains in proteins of plant origin. In this work, we provide improved HMMs for LysM domain detection in plants, that were built from the structural alignment of manually curated LysM domain structures from the Protein Data Bank and AlphaFold Protein Structure Database. Furthermore, we evaluated different sets of ligand-specific HMMs that were able to correctly classify a limited set of fully characterised RLK/Ps by their ligand specificity. In contrast, the phylogenetic analysis of the extracellular region of RLK/Ps, or of their individual LysM domains, was unable to discriminate these proteins by their ligand specificity. The HMMs reported here will allow a more sensitive detection of plant proteins containing LysM domains and help improve their characterisation. Plants perceive different signals from bacteria and fungi, both pathogenic and symbiotic, through a family of cell-surface receptor proteins. Oligosaccharides, particularly those structurally related to chitin, are sensed by protein modules of bacterial origin known as LysM domains. Plant proteins contain three LysM domains in their extracellular region, however, available tools are not always able to detect the three LysM domains. In this work, we provide improved tools for the detection of LysM domains in plant proteins, and for their classification by ligand specificity.