Secreted effector that induces cell death when expressed in host plants (PubMed:19741609, PubMed:22927814, PubMed:20847293). Acts as a kinase and is able to autophosphorylate, however its cell death inducing-abiliy is not a direct result of its kinase activity, but rather a consequence of the phosphorylated state of the five identified serine residues in the CRN8 protein (PubMed:22927814). ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Dimerizes in host plants. The CRN proteins have modular architectures that include a signal peptide, a conserved N-terminus, and highly diverse C-terminal domains. The conserved CRN N-terminus harbors a distinct LXLFLAK motif, which is followed by the conserved DWL domain. A highly conserved HVLVXXP motif marks the end of the CRN N-terminal domains and forms a junction where diverse C-terminal effector domains are fused. The conserved CRN N-terminus mediates the translocation into the plant host cells. The whole D2 effector domain that contains a protein functional kinase domain, as well as the C-terminal NLS are required for cell death induction. Autophosphorylated at Ser-249, Ser-281, Ser-385, Ser-474 and Ser-587. Additional serines or threonines are also targeted for phosphorylation. In the N-terminal section; belongs to the Crinkler effector family. In the C-terminal section; belongs to the protein kinase superfamily.