Figure 2B shows the sequence alignment of 1–358 residues of hACE2 and ACE2 of Myotis daubentonii and Rhinolophus ferrumequinum (Omega Clustal). 78.77% sequence identity is observable for Myotis daubentonii, 77.93% for Rhinolophus ferrumequinum (UniProt ID: E2DHI2), and 81.24% for Rhinolophus ferrumequinum (UniProt ID: B6ZGN7). The identity refers to all the residues ranging from 1 to 358. Most of the residues essential for the binding with S protein are conserved. In particular, Rhinolophus ferrumequinum preserves the residues E37, Q42, N330, and K353, with D38 (Homo sapiens) replaced by N38 (Rhinolophus ferrumequinum), which conserves the physical-chemical properties of the amino acid. Myotis daubentonii preserved H34, E37, D38, and K353, with K31 and Q42 (Homo sapiens) replaced by N31 and E42 (Myotis daubentonii), respectively. Considering these results together with the data deriving from in silico calculations, Rhinolophus ferrumequinum is to be considered a potential primary animal reservoir within the Italian distribution area [37].