<p>Sequence alignment of human desmoplakin I (DPI), human plectin (PL), human envoplakin (EP), and human periplakin (PP) in the region corresponding to the linker between PRDs B and C of desmoplakin. Secondary structures predicted with JPred4 are shown as arrows (β-strands) and thickened rectangles (α-helices). Ser/Thr residues in red and orange are predicted potential phosphorylation sites with scores higher than 0.9 and 0.6, respectively, by the NetPhos 2.0 server. The starting and ending residue numbers are indicated. A consensus sequence is shown at the bottom of each alignment. A consensus residue or class of residues, represented as a symbol, is indicated when more than 3/4 of the residues fall into this category.</p
<p>A. Disorder prediction of Rbm19 (human) and Mrd1 (<i>S. cerevisiae</i>). Grey areas indicate the ...
<p>A multiple sequence alignment of human rotatin and homologs in other species was produced and rep...
<p><b>(A)</b> Sequence alignments of the region surrounding amino acids 320, 321 and 353 from the hu...
<p>Secondary structure elements were obtained from the SR3-6 crystal structure <a href="http://www.p...
<p>(a) SMARCAD1, (b) GSG2, (c) NUP35, (d) NEK5, (e) KIF23 and (f) CEP170. MSA illustrates the conser...
<p><i>Left:</i> alignment of the kinase domain, covering the region 83–422 of FAM69A. The sequences ...
<p>Three domains of PgdS, the NlpC/P60 catalytic domains of LytF, LytE and CwlS from <i>B</i>. <i>su...
<p>Amino acid sequences were obtained from the Phytozome database. The numbers indicate the distance...
<p>A) Ribbon diagram of Ply with the domain 4 loop residues shown at the base. B) The bottom view of...
<p>Conserved residues in all sequences are highlighted: identical, similar and unrelated residues ar...
<p>Sequence alignment around the catalytic triad including Cys (the active-site), His, and Asp was s...
<p>The sequence alignment of PcFK1 (pdb: 1X5V) with the sequences recognized by PfSUB1 shows a compa...
<p>Numbering indicates the position of the first and last residue in each aligned sequence. Proteins...
<p>(<b>a</b>) The catalytic domain of CNA is highly conserved around the β12 and β13 connection in P...
<p>The EmPlk1 amino acid sequence was aligned to Plk1-like enzymes of <i>S. mansoni</i> (SmPlk1; Gen...
<p>A. Disorder prediction of Rbm19 (human) and Mrd1 (<i>S. cerevisiae</i>). Grey areas indicate the ...
<p>A multiple sequence alignment of human rotatin and homologs in other species was produced and rep...
<p><b>(A)</b> Sequence alignments of the region surrounding amino acids 320, 321 and 353 from the hu...
<p>Secondary structure elements were obtained from the SR3-6 crystal structure <a href="http://www.p...
<p>(a) SMARCAD1, (b) GSG2, (c) NUP35, (d) NEK5, (e) KIF23 and (f) CEP170. MSA illustrates the conser...
<p><i>Left:</i> alignment of the kinase domain, covering the region 83–422 of FAM69A. The sequences ...
<p>Three domains of PgdS, the NlpC/P60 catalytic domains of LytF, LytE and CwlS from <i>B</i>. <i>su...
<p>Amino acid sequences were obtained from the Phytozome database. The numbers indicate the distance...
<p>A) Ribbon diagram of Ply with the domain 4 loop residues shown at the base. B) The bottom view of...
<p>Conserved residues in all sequences are highlighted: identical, similar and unrelated residues ar...
<p>Sequence alignment around the catalytic triad including Cys (the active-site), His, and Asp was s...
<p>The sequence alignment of PcFK1 (pdb: 1X5V) with the sequences recognized by PfSUB1 shows a compa...
<p>Numbering indicates the position of the first and last residue in each aligned sequence. Proteins...
<p>(<b>a</b>) The catalytic domain of CNA is highly conserved around the β12 and β13 connection in P...
<p>The EmPlk1 amino acid sequence was aligned to Plk1-like enzymes of <i>S. mansoni</i> (SmPlk1; Gen...
<p>A. Disorder prediction of Rbm19 (human) and Mrd1 (<i>S. cerevisiae</i>). Grey areas indicate the ...
<p>A multiple sequence alignment of human rotatin and homologs in other species was produced and rep...
<p><b>(A)</b> Sequence alignments of the region surrounding amino acids 320, 321 and 353 from the hu...