Disease resistance (R) protein that specifically recognizes the HopBA1 type III effector protein from P.syringae, and triggers cell death (PubMed:28137883). Acts as a NAD(+) hydrolase (NADase): in response to pathogen-recognition, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a defense system that promotes cell death (PubMed:31439793). In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed v-cADPR, for which the cyclizing bond is unknown (PubMed:31439793). Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules (PubMed:31439793). H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) + nicotinamide Homooligomer; homooligomerization is required for activity. Forms aggregate-like cyto-nucleoplasmic puncta. Accumulates during immune responses activated by a variety of NLR proteins. The TIR domain catalyzes the NAD(+) cleavage (NADase) activity (PubMed:31439793). In contrast to classical TIR-NB-LRR receptor-like proteins, only contains a TIR domain (Probable). The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.