Figure 3From: Rim15 and the crossroads of nutrient signalling pathways in Saccharomyces cerevisiae Schematic diagram illustrating the domain architecture of the S. cerevisiae Rim15 protein. All domains are drawn approximately to scale. Rim15 belongs to a group of conserved fungal proteins, which exhibit the same domain organization, including the N-terminal PAS and CCHC-type zinc finger domains, the central kinase catalytic domain (black ovals), with an insert of 188 amino acids between subdomains VII and VIII, that classifies Rim15 as a member of the conserved nuclear Dbf2-related (NDR) and large tumor suppressor (LATS) serine/threonine kinase subclasses of the protein kinase A, G, and C (AGC) class of kinases, and a C-terminal receiver (REC) domain. The PKA and the Pho85-Pho80 phosphorylation sites are indicated with open and closed arrows, respectively. The single high-stringency, putative 14-3-3 protein-binding site in Rim15 flanks amino acid T1075.Back to article page