The domain within your query sequence starts at position 159 and ends at position 283; the E-value for the RHOD domain shown below is 1.71e-11.

Some of the required catalytic sites were not detected in this domain. It is probably inactive! Check the literature (PubMed 20251047 ) for details.

Catalytic residues
PositionAmino acidPresent?


Rhodanese Homology Domain
SMART accession number:SM00450
Description: An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.
Interpro abstract (IPR001763):

Rhodanese, a sulphurtransferase involved in cyanide detoxification (see IPR001307 ) shares evolutionary relationship with a large family of proteins [ (PUBMED:9733650) ], 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 [ (PUBMED:8702871) ].

Family alignment:
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There are 171652 RHOD domains in 136038 proteins in SMART's nrdb database.

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