All GTPases have the similar guanine nucleotide-binding (G) domain, which is responsible for binding and hydrolyzing guanine nucleotides. When vesicles are being formed via clathrin-mediated endocytosis or other vesicular processes, dynamin is the essential large GTPase for releasing the vesicles from the plasma membrane. By inducing membrane fission, extruding endocytic vesicles, and facilitating membrane fusion between virus and endosomes after endocytosis . Dynamin-regulated GTPase is a crucial endocytic pathway used by a wide variety of virus. Dynamin is an essential protein in the transport of vesicle bud formation and the division of various vesicles and organelles because of the guanylate-binding proteins/atlastins that make up its subunit. The N-terminal Dynamin N domain is present in dynamins (IPR045063). Table . GTPase domains of monkeypox virus E protein F13 Comparing dynamin-related sequences from the Uniprot database with the monkeypox virus protein F13 using the native MEME tool. The monkeypox virus F13 protein has Dynamin-type, Dynamin_N, and Dynamin_M domains, according to the search results (Table ). Dynamin_M A is situated at the center of the F13. F13 contains both Dynamin-type A-D and Dynamin_N A-D at its middle and C-terminus. This indicates that the GTPase active region of the F13 protein of the monkeypox virus is concentrated at the middle and C-terminus. Dynamin domains overlap with GAP and GEF domains. For viral membrane fusion with acidic endosomal membranes, F13 GTPase is utilized.