Betaarterivirus americense causes a clinical condition with a high epidemiological risk in Peru and worldwide. Therefore, the aim of this study was to identify the genetic diversity of circulating viruses in different commercial swine farms in Lima. A total of 24 viral sequences from our previously published work were analyzed, and phylogenetic inference was performed based on amino acid alignments. The results revealed that all isolates clustered within sublineage 1.5 of the representative NADC34 variant. Sequence analysis of ORF5 (GP5) identified a high number of amino acid substitutions in key regions, including aa34 (24/24), aa39 (6/24), aa44 (4/24), aa47 (24/24), aa57 (24/24), aa58 (24/24), and aa59 (24/24), located within epitopes A, B, and C. N-glycosylation analysis revealed 10 potential N-glycosylation sites: N30, N32, N33, N34, N35, N44, N51, N57, N128, and N151. Among these, the major conserved sites (N34, N44, and N51) were fully preserved in strains 40 and 41; in 20 out of 24 strains, only sites N44 and N51 were conserved, whereas strains 36, 37, 38, and 39 showed complete loss of these glycosylation sites. The signal peptide cleavage site was identified between amino acids 1 and 31. Genetic diversity analysis revealed rapid viral evolution and a high mutation rate, with 530 variable sites and 860 mutations. Tajimas D statistical analysis indicated population subdivision, yielding a D value of −0.78746. The high number of substitutions in key domains of the GP5 glycoprotein and the variability of potential N-glycosylation sites among the 24 NADC34 variant isolates of Betaarterivirus americense suggest that these strains exhibit high genetic variability and recombination potential.