<p>Rhodanese, a sulphurtransferase involved in cyanide detoxification (see <db_xref db="INTERPRO" dbkey="IPR001307"/>) shares evolutionary relationship with a large family of proteins [<cite idref="PUB00006580"/>], including<ul><li>Cdc25 phosphatase catalytic domain.</li><li>non-catalytic domains of eukaryotic dual-specificity MAPK-phosphatases.</li><li>non-catalytic domains of yeast PTP-type MAPK-phosphatases.</li><li>non-catalytic domains of yeast Ubp4, Ubp5, Ubp7.</li><li>non-catalytic domains of mammalian Ubp-Y.</li><li>Drosophila heat shock protein HSP-67BB.</li><li>several bacterial cold-shock and phage shock proteins.</li><li>plant senescence associated proteins.</li><li>catalytic and non-catalytic domains of rhodanese (see <db_xref db="INTERPRO" dbkey="IPR001307"/>).</li></ul> </p><p>Rhodanese has an internal duplication. This domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases [<cite idref="PUB00002964"/>].</p>