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. Author manuscript; available in PMC: 2024 Jun 5.
Published in final edited form as: Curr Biol. 2023 May 25;33(11):2270–2282.e2. doi: 10.1016/j.cub.2023.05.011

Figure 4. Multiple sequences alignment revealed the preserved residues of BEN domains.

Figure 4.

BEN domains from Drosophila (i.e. BEN domains from Drosophila Insv and Elba1), human (BEN domains from human NACC1, BANP, BEND3, BEND4, BEND5, BEND6 and BEND7), viruses (i.e. BEN domains from YB1 from Microplitis demolitor bracovirus, MC036R from Molluscum contagiosum virus, and PG067/E5R from Variola virus), C.elegans (i.e. BEN domains from LIN- 14 and SEL-7), DUF4806 factors (i.e. BEN domains from Drosophila CG12112 and CG42854 and zebrafish si:dkey-266f7.5) are used for multiple sequences alignment. The alignment reveals the conserved residues (marked with stars) and motifs (LhxxlF and LDP). The conserved hydrophobic resides are labeled with green, and the acidic residues with blue.