The FKS1_dom1 domain is likely to be the 'Class I' region just N-terminal to the first set of transmembrane helices that is involved in 1,3-beta-glucan synthesis itself. PMID:20124029 This family is found on proteins with family Glucan_synthase, Pfam: PF02364.
This domain is likely to be the 'Class I' region just N-terminal to the first set of transmembrane helices that is involved in 1,3-beta-glucan synthesis itself [ (PUBMED:20124029) ].
Family alignment:
There are 2975 FKS1_dom1 domains in 2972 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing FKS1_dom1 domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with FKS1_dom1 domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing FKS1_dom1 domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
Multiple functional domains of the yeast l,3-beta-glucan synthase subunit Fks1prevealed by quantitative phenotypic analysis of temperature-sensitive mutants.
Genetics. 2010; 184: 1013-24
Display abstract
The main filamentous structural component of the cell wall of the yeastSaccharomyces cerevisiae is 1,3-beta-glucan, which is synthesized by a plasmamembrane-localized enzyme called 1,3-beta-glucan synthase (GS). Here we analyzed the quantitative cell morphology and biochemical properties of 10 differenttemperature-sensitive mutants of FKS1, a putative catalytic subunit of GS. Tountangle their pleiotropic phenotypes, the mutants were classified into threefunctional groups. In the first group, mutants fail to synthesize 1,3-beta-glucanat the proper subcellular location, although GS activity is normal in vitro. Inthe second group, mutants have normal 1,3-beta-glucan content but are defectivein polarized growth and endocytosis. In the third group, mutations in theputative catalytic domain of Fks1p result in a loss of the catalytic activity of GS. The differences among the three groups suggest that Fks1p consists ofmultiple domains that are required for cell wall construction and cellularmorphogenesis.
Links (links to other resources describing this domain)
