Small cysteine-rich proteins sharing most if not all of the general features used to define the metallothionein (MT) superfamily are found in yeast and fungi. Unlike MTs from mammalian sources, most of the known yeast and fungal MTs are Cu(I) rather than Zn(II) or Cd(II) binding proteins. The sequences of fungal MTs reported so far are quite diverse, in such a way that fungal MTs are assigned to six different families. Family 8 contains the MTs with the highest similarity to the N-terminal domains of mammalian MTs. The best characterized member of this family is isolated from the ascomycete Neurospora crassa. It represents a copper-induced polypeptide of only about 25 amino acid residues and harbors a single cluster made up of six Cu(I) that are bound to its seven cysteine residues. The MTs assigned to families 9 and 10 are MT-1 and MT-2 found in the human pathogenic yeast Candida glabrata. The regulation of these proteins employing a copper sensitive transcription factor shares the same principle as were described for the MTs found in Saccharomyces cerevisiae, Cu-MT and Crs5, that are assigned to families 12 and 13. S. cerevisiae Cu-MT is the only MT, of which the structure including its Cu(I)8-thiolate core has been revealed. It should be emphasized that this is the largest known Cu cluster in biological systems. Besides the presentation of these well studied aspects, the open questions of Cd(II) and Zn(II) binding in yeasts and fungi are addressed and future directions of the MT research are discussed.