Multiple sequence alignment of amino acid sequences of UPRTs from <i>M. tuberculosis</i>, <i>B. caldolyticus</i>, <i>T. gondii</i>, <i>E. coli</i> and <i>S. solfataricus</i>.
- Anne Drumond Villela (284136)
- Rodrigo Gay Ducati (284138)
- Leonardo Astolfi Rosado (284140)
- Carlos Junior Bloch (284142)
- Maura Vianna Prates (284144)
- Danieli Cristina Gonçalves (284146)
- Carlos Henrique Inacio Ramos (284148)
- Luiz Augusto Basso (284150)
- Diogenes Santiago Santos (284152)
Publication date
February 2013
DOIAbstract
<p>Amino acids for each polypeptide sequence were independently numbered. Identical conserved residues are indicated by stars below the alignment. Residues proposed to be involved in catalysis (ARg102 and Asp198), PRPP substrate binding (ARg77 and Arg102), and (or not) C-terminal glycine (Gly205) are highlighted (<i>Mt</i>UPRT numbering). Multiple sequence alignment was carried out using Clustal W2 software (<a href="http://www.ebi.ac.uk/Tools/msa/clustalw2/" target="_blank">http://www.ebi.ac.uk/Tools/msa/clustalw2/</a>).</p
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