The plant proteins called ERECTA family play important role in inflorescence architecture, stomatal patterning and phloem-xylem organization. ERECTA proteins belong to the moonlighting proteins family containing the guanylyl cyclase (GC) catalytic center embedded within the intracellular kinase domain. This characteristic architecture of ERECTA proteins prompted us to experimentally confirm of enzymatic activity of one of these, BdERL1 (ERECTA-like1 from Brachypodium distachyon). We have shown that BdERL1 is dual-function protein with both kinase and GC activity. Moreover, our mutagenesis studies also revealed the catalytic roles of key conserved amino acid residues at the GC center and importantly, probing of the kinase and GC with Ca{}^{2+} and/or cGMP, shed light on the intramolecular regulations of BdERL1.