Currently, Dual Specificity YAK1-Related Kinases (MNB/DYRK) were found in slime molds, protista, fungi, and animals, but the existence of plant homologues is still unclear. In the present study, we have identified 14 potential plant homologues with the previously unknown functions, based on the strong sequence similarity. The results of bioinformatics analysis revealed their correspondence to DYRK1A, DYRK1B, DYRK3, and DYRK4. For two plant homologues of animal DYRK1A from Physcomitrella patens and Arabidopsis thaliana spatial structures of catalytic domains were predicted, as well as their complexes with ADP and selective inhibitor d15. Comparative analysis of 3D-structures of the human DYRK1A and plant homologues, their complexes with the specific inhibitors, and results of molecular dynamics confirm their structural and functional similarity with high probability. Preliminary data indicate the presence of potential MNB/DYRK specific phosphorylation sites in such proteins associated with plant cytoskeleton as plant microtubule-associated proteins WVD2 and WDL1, and FH5 and SCAR2 involved in the organization and polarity of the actin cytoskeleton and some kinesin-like microtubule motor proteins. 1. Introduction From the time of Yak1p kinase discovery in budding yeast more than two decades ago, DYRK (MNB/DYRK) family members have been identified in all eukaryotes. At present, different members of this family are regarded as key players in a number of cellular processes [1, 2]. The analysis of the genomic structure and the conservation degree within the kinase domain of the mammalian DYRK subfamily members (DYRK1A, DYRK1B (Mirk), DYRK2, DYRK3 (REDK), and DYRK4) reveal that all these kinases originated via gene duplication during the late periods in metazoan evolution [3, 4]. Mammalian Dual Specificity YAK1-Related Kinases (DYRKs) comprise a group of tyrosine-regulated kinases within the CMGC protein kinase family (MNB/DYRK subfamily) [5], homological yeast Yak1 [1, 6, 7], and Drosophila minibrain kinases [7]. Animal DYRK kinases participate in several signaling pathways involved in the development and support of cell homeostasis [3, 8]. One main feature of DYRKs is their dual ability to autophosphorylate tyrosine residues and to phosphorylate their substrates on serine and threonine residues within an RPx(S/T)P consensus sequence [9, 10]. At the same time, like many other protein kinases, mammalian DYRK1A prefers serine over threonine in substrate peptides and does not detectably phosphorylate tyrosine [10]. It was established that once
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