v5.1.0.3
Glycine data from LIS
Type | Homologous_superfamily |
Description | Rhodanese, a sulphurtransferase involved in cyanide detoxification (see ) 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 (see ). 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 β-sheet of five strands. |
Short Name | Rhodanese-like_dom_sf |