PROSITE documentation PDOC00952GDA1/CD39 family of nucleoside phosphatases signature
Description
A number of nucleoside diphosphate and triphosphate hydrolases as well as some yet uncharacterized proteins have been found to belong to the same family [1,2]. This family currently consist of:
- Yeast guanosine-diphosphatase (EC 3.6.1.42) (GDPase) (gene GDA1). GDA1 is a golgi integral membrane enzyme that catalyzes the hydrolysis of GDP to GMP.
- Potato apyrase (EC 3.6.1.5) (adenosine diphosphatase) (ADPase). Apyrase acts on both ATP and ADP to produce AMP.
- Mammalian vascular ATP-diphosphohydrolase (EC 3.6.1.5) (also known as lymphoid cell activation antigen CD39).
- Toxoplasma gondii nucleoside-triphosphatases (EC 3.6.1.15) (NTPase). NTPase hydrolyses various nucleoside triphosphates to produce the corresponding nucleoside mono- and diphosphates. This enzyme is secreted into the invaded host cell into the parasitophorous vacuole, a specialized compartment where the parasite intracellulary resides.
- Pea nucleoside-triphosphatases (EC 3.6.1.15) (NTPase).
- Caenorhabditis elegans hypothetical protein C33H5.14.
- Caenorhabditis elegans hypothetical protein R07E4.4.
- Yeast chromosome V hypothetical protein YER005w.
The above uncharacterized proteins all seem to be membrane-bound.
All these proteins share a number of conserved domains. We have selected the best conserved of these domains. It is located in the central section of the proteins.
Last update:December 2004 / Pattern and text revised.
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References
1 | Authors | Handa M. Guidotti G. |
Title | Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum). | |
Source | Biochem. Biophys. Res. Commun. 218:916-923(1996). | |
PubMed ID | 8579614 |
2 | Authors | Vasconcelos E.G. Ferreira S.T. de Carvalho T.M.U. de Souza W. Kettlun A.M. Mancilla M. Valenzuela M.A. Verjovski-Almeida S. |
Title | Partial purification and immunohistochemical localization of ATP diphosphohydrolase from Schistosoma mansoni. Immunological cross-reactivities with potato apyrase and Toxoplasma gondii nucleoside triphosphate hydrolase. | |
Source | J. Biol. Chem. 271:22139-22145(1996). | |
PubMed ID | 8703025 |
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