Table shows the PTEN domains and motifs of E of Andes and Hantaan. Both have C2 Tensin-type and Phosphatase tensin-type domains, as shown in Table . These two domains contain sites that overlap. Both domains include the pattern "HCXXGXXR" and are at C-terminal. The "HCXXGXXR" motif of Hantaan is "HCYGACQK". The "HCXXGXXR" motif of Andes is "HCYGACTK". The penultimate amino acid residue distinguishes the two motifs. Andes' E is denoted by the letter T, while the letter Q denotes Hantaan's E, at penultimate amino acid residue. This mutation results in the Andes' E has PID and SH2 domains with the "HCXXGXXR" motif. The G and R in the "HCXXGXXR" motif were changed to A and K in the two viral sequences, respectively. The two mutations G->A and R->K may confer a particular membrane-binding function on Hantavirus. Hantaan E has a shorter protein kinase domain. Hantaan E's phorbol-ester/DAG structure is capable of activating serine/threonine-protein kinase. It suggests that Hantaan E may function as a serine/threonine-protein kinase. Andes E contains a "Tyrosine-protein phosphatase" domain, implying that it contains a tyrosine-protein kinase domain. These mutations and changes in Andes E may enhance Andes Hantavirus endocytosis.