Difference between revisions of "Phosphatase Subfamily YNL217W"
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| − | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_PPPL|Fold PPPL]]: [[Phosphatase_Superfamily_PPPL|Superfamily PPPL]]: [[ | + | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_PPPL|Fold PPPL]]: [[Phosphatase_Superfamily_PPPL|Superfamily PPPL]]: [[Phosphatase_Family_PPP|Family PPP]]: [[Phosphatase_Subfamily_YNL217W|Subfamily YNL217W]] |
The subfamily is named after [http://www.yeastgenome.org/locus/S000005161/overview budding yeast YNL217W]. | The subfamily is named after [http://www.yeastgenome.org/locus/S000005161/overview budding yeast YNL217W]. | ||
Revision as of 17:34, 13 March 2017
Phosphatase Classification: Fold PPPL: Superfamily PPPL: Family PPP: Subfamily YNL217W
The subfamily is named after budding yeast YNL217W.
Evolution
The YNL217W subfamily is found in fungi and scattered metazoa, including sponge, molluscs, sea urchin, lancet, and ciona but is not present in any vertebrate, or in insects or nematodes. Related genes are also found in algae, but not higher plants, and an array of other basal or poorly-classified eukaryotes, and is similar to phosphatases found in several bacteria. This group has overlaps with the "Alphs" group of phosphatases previously described [1]
Domain
The YNL217W subfamily has a single known structural domain, PPPc domain.
Functions
The function is unknown. The yeast protein localizes to the vacuole, and the mutation shows a mild defect in vacuolar fragmentation [2].
This family is closest in sequence to bacterial diadenosine tetraphosphatases (adaH, prpA) that hydrolyze diadenosine tetraphosphate to yield ADP [3].
References
- Andreeva AV and Kutuzov MA. Widespread presence of "bacterial-like" PPP phosphatases in eukaryotes. BMC Evol Biol. 2004 Nov 19;4:47. DOI:10.1186/1471-2148-4-47 |
- Michaillat L and Mayer A. Identification of genes affecting vacuole membrane fragmentation in Saccharomyces cerevisiae. PLoS One. 2013;8(2):e54160. DOI:10.1371/journal.pone.0054160 |
- Sasaki M, Takegawa K, and Kimura Y. Enzymatic characteristics of an ApaH-like phosphatase, PrpA, and a diadenosine tetraphosphate hydrolase, ApaH, from Myxococcus xanthus. FEBS Lett. 2014 Sep 17;588(18):3395-402. DOI:10.1016/j.febslet.2014.07.031 |
