Mob-binding domain found in fungal Sid2p-like serine/threonine protein kinases
This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and ppk35p, as well as Saccharomyces cerevisiae Dbf2p and Dbf20p. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Ppk35p, also called meiotically up-regulated gene 27 protein (mug27p), has a role in meiosis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. Dbf20p may function in initiation of DNA synthesis and in late nuclear division. Kinases in this group belong to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. These proteins contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of Sid2p-like serine/threonine protein kinases.
Jiyao W et al.(2023). "The conserved domain database in 2023.",