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Figure 2.
Structure-based multiple sequence alignment of SelM and Sep15
homologs. Assigned secondary structure elements for SelM and
Sep15 are indicated above each sequence with α-helices colored
blue and β-strands colored orange. Strictly conserved residues
are shown in blue, and moderately conserved residues are shown
in red. The active-site redox motif, including the
selenocysteine residue (U), is colored green and is located
between the C terminus of strand β1 and the N terminus of helix
α1. The following accession numbers were used to generate this
alignment: human SelM (27805722); mouse SelM (23956246);
zebrafish SelM (29648551); human Sep15 (6094261); mouse Sep15
(20140242); zebrafish Sep15 (68053306); rat Sep15 (20139870);
mosquito (18389881); fruit fly Sep15 (24666045). This alignment
was produced with 3D-COFFEE (53).
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