Arginine is present, even as a dimer, in the viral polybasic furin cleavage sites, including that of SARS-CoV-2 in its protein S, whose acquisition is one of its characteristics that distinguishes it from the rest of the sarbecoviruses. The CGGCGG sequence encodes the SARS-CoV-2 furin site RR dimer. The aim of this work is to report the other SARS-CoV-2 arginine pairs, with particular emphasis in their codon usage. Here we show the presence of RR dimers in the orf1ab related non structural proteins nsp3, nsp4, nsp6, nsp13 and nsp14A2. Also, with a higher proportion in the structural protein nucleocapsid. All these RR dimers were strictly conserved in the sarbecovirus strains closest to SARS-CoV-2, and none of them was encoded by the CGGCGG sequence.