Copper metallothionein that protects the cell against copper toxicity by tightly chelating copper ions (PubMed:21819456, PubMed:23498952). Required for antioxidant-mediated growth rescue in the presence of fluconazole (PubMed:31694529). Acts as a critical factors for lung colonization and virulence (PubMed:23498952). Expression is induced in a dose-dependent manner in response to high concentrations of copper and basal transcription is repressed in the presence of the copper chelator bathocuproin sulphonate (BCS) (PubMed:21819456). Expression is regulated by the CUF1 copper-dependent transcription factor (PubMed:21819456). Highly induced during mice pulmonary infection (PubMed:23498952). Divided into 4 Cys-rich domains by 3 spacer sequences termed B1-B3 (PubMed:23498952). Each cystein-rich domain contains the conserved copper-binding motif Cys-X-Cys-X6-Cys-X-Cys-X4-Cys-X-Cys-X2-Cys (PubMed:23498952). The copper-binding domains together are able to chelate up to 16 copper ions (PubMed:23498952). Fungi lacking both CMT1 and CMT2 show attenuated virulence and reduced pulmonary colonization in mice (PubMed:23498952). Impairs growth rescue by antioxidants when cells are treated with fluconazole (PubMed:31694529). Belongs to the metallothionein superfamily.