We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00952GDA1/CD39 family of nucleoside phosphatases signature
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00952
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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Technical section
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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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