Comparative Analysis of SWIRM Domain-Containing Proteins in Plants
Figure 2
Structure-base sequence alignment of SWIRM domain subtypes. The sequence alignment was produced using Cluatal X. Resulting sequences were then adjusted manually using the GeneDoc software. The secondary structure was predicted by Jpred and PSIPRED. (a) Alignment of the SWIRM domain sequences in Oryza sativa. The coloring represents the conservation profile of amino acid residues distinguished by the following amino acid classes: hydrophobic residues are indicated by shaded black, charged residues (ED) by shaded blue, positive residues (RK) by shaded red, polar residues (YNRDTK) by shaded light green, amphoteric residues (RQ) by shaded green, small residues (NDSTPASV) by shaded yellow, aliphatic residues (LIAV) by shaded gray, and aromatic residues (YHWH) by shaded pink. (b) Alignment of the Swi3-type SWIRM domain sequences. The shaded blocks indicate several highly conserved residues by the alignment of SWIRM domain in Oryza sativa and Arabidopsis thaliana. (c) Alignment of the LSD1-type SWIRM domain sequences. The shaded blocks indicate several highly conserved residues by the alignment of SWIRM domains in Oryza sativa and Arabidopsis thaliana. (d) Alignment of the Ada2-type SWIRM domain sequences.
