| Description | Characterization of two novel proteins containing the rhodanese homology domain: YgaP and YbbB of Escherichia coli Abstract Rhodanese homology domains are ubiquitous structural
modules found in eubacteria, eukaryotes and archaea. The rhodanese
homology domain may comprise the entire structure of a protein.
Alternatively it is found as tandemly repeated modules in which the
C-terminal domain displays the properly structured active site. Finally
it is found as a member of many multidomain proteins. Although some
members of this family of proteins show sulfurtransferase activity in
vitro, their specific physiological functions remain largely undefined.
Fusion of a rhodanese domain to different protein domains of known or
unknown functions provides important clues to the diverse roles for
these proteins
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