<p>Conservation of the core architecture of EAG potassium channels.</p>

<p>Alignment of the protein sequences spanning the region from the PAS domain to the cyclic nucleotide-binding homology domain (CNBHD) of EAG channels from the following species: <i>Caenorhabditis elegans (EGL-2,</i> NP_503402.3)<i>, Mus musculus (mEag1,</i> NP_034730.1), <i>Rattus norvegicus (rEag1,</i> NP_113930.1), <i>Homo sapiens (hEAG1,</i> NP_758872.1), <i>Xenopus laevis (fEAG1,</i> XP_041418453.1), and <i>Drosophila melanogaster (dEAG,</i> NP_001036275.1).

Conserved residues are highlighted in black. Functional domains are indicated above the alignment, including the PAS domain, the voltage sensor domain (S1–S4), the pore-forming segments (S5–S6), the potassium ion selectivity filter (SF), the CNBHD, and the intrinsic ligand motif. Residue numbering at the top corresponds to EGL-2 isoform a.