Abstract
Intrinsically disordered proteins and regions typically lack a well-defined structure and thus fall outside the scope of the classic sequence–structure–function relationship. Hence, classic sequence- or structure-based bioinformatic approaches are often not well suited to identify homology or predict the function of unknown intrinsically disordered proteins. Here, we give selected examples of intrinsic disorder in plant proteins and present how protein function is shared, altered or distinct in evolutionary distant organisms. Furthermore, we explore how examining the specific role of disorder across different phyla can provide a better understanding of the common features that protein disorder contributes to the respective biological mechanism.
Highlights
Despite the progress made in recent decades, a large proportion of plant protein sequences still lacks useful functional annotation
The first plant Cyclin-dependent kinase inhibitors (CKIs) was identified by a yeast two-hybrid assay employing A. thaliana CDKA;1 as a bait protein and subsequent sequence analysis, in which the conserved inhibitory domain (CID) was found to be distantly homologous to that of mammalian p27kip1 [145]
Since protein disorder emerged as a systematically studied field some 20 years ago, the challenge of devising a scheme of classification and functional annotation for the disordered proteome has been widely discussed within the scientific community
Summary
Despite the progress made in recent decades, a large proportion of plant protein sequences still lacks useful functional annotation. Only approximately 1% of the protein sequences in the UniProt database have experimentally verified functions [4] To address this discrepancy, putative or hypothetical proteins are typically classified into protein families that may share evolutionary relationships or molecular function by sequence-based computational analysis. Putative or hypothetical proteins are typically classified into protein families that may share evolutionary relationships or molecular function by sequence-based computational analysis This approach works insufficiently for proteins lacking sequence conservation or experimentally verified, functional annotation in orthologous proteins
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