<p>Amino acid residues conserved at the GTP binding site are shown in red. Amino acid residues perfectly and partially conserved across the isotype are highlighted with green or blue, respectively.</p
<p>Conserved amino acids in vertebrates excluding the five special species are indicated in the yell...
<p>Conserved residues are colored according to amino acid type following the Clustal X color scheme ...
Sequence logo of the multiple sequence alignment of amino acid sequence for the identification of no...
<p>Conserved GTP-binding amino acid residues are highlighted in red. Amino acid residues perfectly o...
<p>The degrees of conservation as well as the consensus between the amino acid sequences have been a...
<p>Sequence alignment of the SMIPP-S family highlighted a cluster of conserved surface exposed resid...
<p>Red dots indicate residues corresponding to the GTP/Mg<sup>2+</sup> binding site; arrows show Swi...
<p>Residues conserved in all lineages, three lineages, and two lineages are shaded black, dark gray,...
<p>The identical and conserved amino acid residues are highlighted in blue color. Five conserved dom...
The multiple sequence alignment of PargGR1 (red) with GRs from arthropods, Eaff (green), Dpul (pink)...
<p>The different Mx functional domains are represented in colored text (BSE = red, G-domain = or...
<p>Sequence alignments of representative members of the dynamin superfamily comparing conserved GTP ...
<p>Black and gray shading indicate the presence of identical and conserved amino acid residues, resp...
<p>“-” represents identical aa. The six key amino acids in the interaction are shown in yellow (Ala9...
<p>Sequence alignment around the catalytic triad including Cys (the active-site), His, and Asp was s...
<p>Conserved amino acids in vertebrates excluding the five special species are indicated in the yell...
<p>Conserved residues are colored according to amino acid type following the Clustal X color scheme ...
Sequence logo of the multiple sequence alignment of amino acid sequence for the identification of no...
<p>Conserved GTP-binding amino acid residues are highlighted in red. Amino acid residues perfectly o...
<p>The degrees of conservation as well as the consensus between the amino acid sequences have been a...
<p>Sequence alignment of the SMIPP-S family highlighted a cluster of conserved surface exposed resid...
<p>Red dots indicate residues corresponding to the GTP/Mg<sup>2+</sup> binding site; arrows show Swi...
<p>Residues conserved in all lineages, three lineages, and two lineages are shaded black, dark gray,...
<p>The identical and conserved amino acid residues are highlighted in blue color. Five conserved dom...
The multiple sequence alignment of PargGR1 (red) with GRs from arthropods, Eaff (green), Dpul (pink)...
<p>The different Mx functional domains are represented in colored text (BSE = red, G-domain = or...
<p>Sequence alignments of representative members of the dynamin superfamily comparing conserved GTP ...
<p>Black and gray shading indicate the presence of identical and conserved amino acid residues, resp...
<p>“-” represents identical aa. The six key amino acids in the interaction are shown in yellow (Ala9...
<p>Sequence alignment around the catalytic triad including Cys (the active-site), His, and Asp was s...
<p>Conserved amino acids in vertebrates excluding the five special species are indicated in the yell...
<p>Conserved residues are colored according to amino acid type following the Clustal X color scheme ...
Sequence logo of the multiple sequence alignment of amino acid sequence for the identification of no...