UBA domain of yeast carbon catabolite-derepressing protein kinases (Snf1) and similar proteins found in fungi
Snf1, also called yeast adenosine monophosphate (AMP)-activated protein kinase (AMPK), is a global regulator of carbon metabolism in the yeast Saccharomyces cerevisiae. Its phosphorylation is essential for the regulation by carbon catabolite repression in eukaryotic cells. Snf1 is involved in the cellular responses to nutrient stress, as well as other environmental stresses, including sodium ion stress, heat shock, alkaline pH, oxidative stress, and genotoxic stress. It plays roles in various nutrient-responsive, cellular developmental processes, including meiosis and sporulation, aging, haploid invasive growth, and diploid pseudohyphal growth. It is required for transcription of glucose-repressed genes, glycogen storage, thermotolerance, and peroxisome biogenesis. The catalytic activity of Snf1 can be regulated by upstream kinases, Sak1, Elm1, and Tos3, by the Reg1-Glc7 protein phosphatase 1, and by autoinhibition. In addition to an N-terminal protein kinase domain and a C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK), Snf1 contains an ubiquitin-associated (UBA) domain, previously called SNF1 homology (SNH) domain, in the middle region.
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