Multiple sequence alignment showing conserved regions of Mps1p homologs.

<p>(<b>A</b>) Alignment of N-terminal region of Mps1, showing conserved Leucine residue. (<b>B</b>) Sequence alignment to show C-terminal homology of CaMps1 (Orf19.7293/AY632356), Mps1 of <i>S. cerevisiae</i> (YDL028C/P54199), Mph1 of <i>S. pombe</i> (O94235), hMps1 of Human (Q9BW51) and mMps1 of Mouse (P35761): Where ORF numbers were not obtained, accession numbers are provided. Eleven subdomains are shown in Roman numerals (I–XI). Subdomains of the kinase domain are shown as described by <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0101517#pone.0101517-Hanks1" target="_blank">[30]</a>. The conserved amino acids in serine/threonine kinases (SER/THR) are shown as described by <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0101517#pone.0101517-Lindberg1" target="_blank">[31]</a>, conserved amino acids are shown in bold letters. The italicized <b><i>E</i></b> in the sub domain V is not part of the SER/THR consensus, but a feature of dual specificity kinases <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0101517#pone.0101517-Lindberg1" target="_blank">[31]</a>. Valine (<u>V</u>) at position 382 is the site of insertional inactivation. Well conserved aa are indicated with a double dot (:) and the perfectly conserved aa are indicated with an asterisk (*)