Protein phosphatases are enzymes that dephosphorylate proteins, including those that play crucial roles in eukaryotic and bacterial signal transduction pathways. Phosphoprotein (PPP) and Mg2+/Mn2+-dependent protein phosphatase (PPM) families are subclasses of protein phosphatases that dephosphorylate Ser and Thr residues, respectively. Serine/threonine phosphatase (PPM, IPR001932) catalyzes Mg2+/Mn2+-dependent dephosphorylation of Ser and Thr residues. PPM's central structure is a PPM-type phosphatase domain, which is responsible for the dephosphorylation of proteins containing phosphoserine and phosphothreonine. PPM1H phosphatases share a conserved Mg2+/Mn2+-dependent catalytic domain with other PPM (PP2C) enzymes. As a result of dephosphorylating specific Rab GTPases, PPM1H inhibits the LRRK2 kinase pathway . Downloaded sequences related to Mg+ serinethreonine kinase' and PPM were compared independently with the Monkeypox virus protein F13 using the local MEME tool. The N-and C-termini of the F13 protein are where the PPM-type domains are located, as shown in Table . The F13 protein of the monkeypox virus has five protein kinase motifs. The 279-296 region of the protein F13 of the monkeypox virus also contains a PK_Tyr Ser-Thr domain. This domain, PK Tyr Ser-Thr, contains three Ser but no Thr. That's why we can classify F13 as a serine protein kinase. Table reveals that the protein kinase C and PPM-type A regions contain the Mg2+ binding site Asn132. Both protein kinase and GTPase require Mg2+, but protein kinase requires Mg2+-ATP, and GTPase requires Mg2+-GTP. Therefore, the PI3K catalytic activity and phosphoinositide phosphorylation capability of Monkeypox virus protein F13 are activated when Mg2+-ATP binds to Asn132. Following this, serine phosphatase (PPM) activity is activated and phosphorylation of serine residues can be removed when Mg2+-ATP binds to Asn132. Protein F13 of the Monkeypox virus is a Rab GTPase when Mg2+-GTP binds to Asn132.