In rice, leucine-rich repeat nucleotide-binding site (NLR) proteins are pivotal immune receptors in combating -triggered rice blast. However, the precise molecular mechanism underlying how NLR proteins regulate downstream signalling remains elusive due to the lack of knowledge regarding their direct downstream targets. The NLR protein Pigm-1 was cloned from Shuangkang 77009 in our laboratory. This study shows that the nucleotide-binding site (NBS) domain of Pigm-1 facilitates its binding to and activation of OsRac1 while the coiled-coil (CC) domain enables its binding to and activation of RAI1, ultimately inducing cell death. At the same time, after knocking out in the background of Shuangkang 77009 containing , two knockout lines showed susceptibility to rice blast. This study reveals OsRac1, a GTPase, as a signalling molecule involved in Pigm-1-mediated blast resistance, suggesting its potential as a common downstream effector of rice NLR proteins. Additionally, a transcriptional activator, RAI1, acts as an essential Pigm-1 interactor for blast resistance. Furthermore, a novel material 9311() was prepared by using two-line restorer line 9311 as receptor and Shuangkang 77009 as donor with molecular marker-assisted technology, which improved blast resistance and yield. This research demonstrates that molecular marker-assisted selection technology enhances both resistance and yield in the crucial two-line restorer 9311(). This study offers crucial insights into how Pigm-1 protein activates downstream molecules and serves as a valuable reference for the molecular breeding of rice blast resistance genes, particularly .