InterPro domain: IPR036873

Rhodanese, a sulphurtransferase involved in cyanide detoxification (see IPR001307 ) shares evolutionary relationship with a large family of proteins [ 1 ], including

• Cdc25 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 (see IPR001307 ).

Rhodanese has an internal duplication. This domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases [ 2 ]. The structure of this domain is composed of three layers (alpha/beta/alpha) arranged in parallel beta-sheet of five strands.

1. A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain. J. Mol. Biol. 282, 195-208
2. Active site structural features for chemically modified forms of rhodanese. J. Biol. Chem. 271, 21054-61