Rhodanese, a sulphurtransferase involved in cyanide detoxification shares evolutionary relationship with a large family of proteins, includingCdc25 phosphatase catalytic domain.non-catalytic domains of eukaryotic dual-specificity MAPK-phosphatases.non-catalytic domains of yeast PTP-type MAPK-phosphatases.non-catalytic domains of yeast Ubp4, Ubp5, Ubp7.non-catalytic domains of mammalian Ubp-Y.Drosophila heat shock protein HSP-67BB.several bacterial cold-shock and phage shock proteins.plant senescence associated proteins.catalytic and non-catalytic domains of rhodanese .Rhodanese has an internal duplication. This domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases. The structure of this domain is composed of three layers (alpha/beta/alpha) arranged in parallel beta-sheet of five strands.