cd07849: STKc_ERK1_2_like (this model, PSSM-Id:143354 is obsolete and has been replaced by 270839)
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases
Serine/Threonine Kinases (STKs), Extracellular signal-regulated kinases 1 and 2 (ERK1/2) and Fus3 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion.
Comment:based on the structure of human CDK2 bound with ATP and substrate peptide, the structure of human ERK1 bound with inhibitor, the structure of rat ERK2 bound with MgATP, and the structure of yeast Fus3 bound with MgADP