Fig. 2

Human cytidine and adenosine deaminase family members. a The cytidine deaminase AID/APOBECs family is shown. Activation-induced cytidine deaminase (AID or AICDA) and all apolipoprotein B mRNA editing enzyme-catalytic polypeptide-like (APOBECs) have one catalytically active cytidine or deoxycytidine deaminase domain (ZDD). APOBEC3 diversifies in 7 submembers (APOBEC3A, APOBEC3B, APOBEC3C, APOBEC3D, APOBEC3F, APOBEC3G, APOBEC3H) whereas some have dual deaminase domain structures but the one in the N terminus is catalytically inactive. b The adenosine deaminase ADARs, ADATs and ADADs families are shown. Three members of the adenosine deaminase acting on RNAs (ADAR1, ADAR2, ADAR3). Two isoforms are known for ADAR1, ADAR1-p150 and ADAR1-p110 and harbour Z-DNA-binding domains. ADAR3 has a unique arginine-rich R domain. Three members of the adenosine deaminase acting on tRNAs (ADAT1, ADAT2 ADAT3). Up to three repeats of the dsRNA binding domain (dsRBD) and a catalytic deaminase domain are present in adenosine deaminases. Two adenosine deaminase domain-containing proteins (ADAD1, ADAD2) are also known as TENR and TENRL respectively. Amino acid length and motifs retrieved from UniProt database [198]. Length is not drawn to scale