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The same sequence is found in many other mononucleotide\u2010binding proteins including elongation factors and oncogenic P21 proteins. Dinucleotide\u2010binding proteins display a pyrophosphate\u2010binding unit with a glycine pattern different from that of mononucleotide\u2010binding proteins. It has been found that P21 <jats:italic>ras<\/jats:italic> protein possesses a strand motif typical for (pyro)phosphate binding of a mononucleotide. A single mutation at position 12 can confer oncogenic activity on the protein. Based on the assumption that amino acid residues which are critical for function are preferentially conserved, we predict from the sequence that glycine residue 15 rather than residue 12 is important for (pyro)phosphate binding.<\/jats:p>","DOI":"10.1016\/0014-5793(85)81326-0","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T07:58:50Z","timestamp":1027583930000},"page":"1-7","source":"Crossref","is-referenced-by-count":226,"title":["Phosphate\u2010binding sequences in nucleotide\u2010binding proteins"],"prefix":"10.1002","volume":"186","author":[{"given":"W.","family":"M\u00f6ller","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R.","family":"Amons","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2001,11,5]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(83)80006-4"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0304-4173(78)90009-5"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/287686a0"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1038\/300143a0"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1038\/300149a0"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.76.10.5355"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.44.2.509-519.1982"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1038\/301262a0"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1038\/302842a0"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(77)90281-9"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1038\/310644a0"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.80.17.5253"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(84)90336-2"},{"key":"e_1_2_1_15_1","first-page":"1860","volume":"226","author":"Hurley J.B.","year":"1984","journal-title":"Science"},{"key":"e_1_2_1_16_1","first-page":"435","volume":"9","author":"Halliday K.R.","year":"1984","journal-title":"J. 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