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InterPro: IPR001763 Rhodanese-like

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11334 proteins

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Architectures
Accession List
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Accession

IPR001763 Rhodanese-like

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.40.250.10	Rhodanese-like	10626
Pfam	PF00581	Rhodanese	8124
PROSITE profile	PS50206	RHODANESE_3	11049
SMART	SM00450	RHOD	10520
SuperFamily	SSF52821	Rhodanese-like	11183
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000751 M-phase inducer phosphatase
IPR008343 MAP kinase phosphatase
IPR014323 Phage shock operon rhodanese PspE
IPR014393 Dual specificity protein phosphatase (MAP kinase phosphatase)
IPR017582 tRNA 2-selenouridine synthase

Contains

IPR001307 Thiosulphate sulfurtransferase, conserved site

InterPro annotation

Entry Details in BioMart

Abstract

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].

Structural links Help

PDB - click here

SCOP: c.46.1.1 , c.46.1.2 , c.46.1.3 , c.46.1.4

CATH: 3.40.250.10

Database links Help

PROSITE doc: PDOC00322

PANDIT: PF00581

Blocks: IPB001763

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001763

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2BDX3 Adenylyltransferase and sulfurtransferase MOCS3

O17730 Putative thiosulfate sulfurtransferase D2023.5

O95396 Adenylyltransferase and sulfurtransferase MOCS3

P20483 M-phase inducer phosphatase

P42937 Uncharacterized protein YGR203W

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000594	UBA/THIF-type NAD/FAD binding fold
IPR000751	M-phase inducer phosphatase
IPR016040	NAD(P)-binding domain
IPR009036	Molybdenum cofactor biosynthesis, MoeB
IPR001763	Rhodanese-like
IPR007901	MoeZ/MoeB
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Hofmann K, Bucher P, Kajava AV. 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 1998 [PubMed: 9733650] http://dx.doi.org/10.1006/jmbi.1998.1998
2.	Gliubich F, Gazerro M, Zanotti G, Delbono S, Bombieri G, Berni R. Active site structural features for chemically modified forms of rhodanese. J. Biol. Chem. 271 21054-61 1996 [PubMed: 8702871] http://dx.doi.org/10.1074/jbc.271.35.21054

Additional Reading Open in usermanual
	Cornilescu G, Vinarov DA, Tyler EM, Markley JL, Cornilescu CC. Solution structure of a single-domain thiosulfate sulfurtransferase from Arabidopsis thaliana. Protein Sci. 15 2006 2836-41 [PubMed: 17088324] http://dx.doi.org/10.1110/ps.062395206
	Donadio S, Shafiee A, Hutchinson CR. Disruption of a rhodaneselike gene results in cysteine auxotrophy in Saccharopolyspora erythraea. J. Bacteriol. 172 1990 350-60 [PubMed: 2294090] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=2294090
	Weiland KL, Dooley TP. Molecular cloning, sequencing and characterization of cDNA to rat liver rhodanese, a thiosulphate sulphurtransferase. Biochem. J. 275 ( Pt 1) 1991 227-31 [PubMed: 2018478] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=2018478
	Laudenbach DE, Ehrhardt D, Green L, Grossman A. Isolation and characterization of a sulfur-regulated gene encoding a periplasmically localized protein with sequence similarity to rhodanese. J. Bacteriol. 173 1991 2751-60 [PubMed: 1708376] http://jb.asm.org/cgi/content/abstract/173/9/2751
	Sohn J, Buhrman G, Rudolph J. Kinetic and structural studies of specific protein-protein interactions in substrate catalysis by Cdc25B phosphatase. Biochemistry 46 2007 807-18 [PubMed: 17223702] http://dx.doi.org/10.1021/bi061257y
	Westley J. Thiosulfate: cyanide sulfurtransferase (rhodanese). Meth. Enzymol. 77 1981 285-91 [PubMed: 6948991] http://dx.doi.org/10.1016/S0076-6879(81)77039-3
	Bordo D, Deriu D, Colnaghi R, Carpen A, Pagani S, Bolognesi M. The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families. J. Mol. Biol. 298 2000 691-704 [PubMed: 10788330] http://dx.doi.org/10.1006/jmbi.2000.3651
	Spallarossa A, Donahue JL, Larson TJ, Bolognesi M, Bordo D. Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily. Structure 9 2001 1117-25 [PubMed: 11709175] http://dx.doi.org/10.1016/S0969-2126(01)00666-9
	Avvakumov GV, Walker JR, Xue S, Finerty PJ Jr, Mackenzie F, Newman EM, Dhe-Paganon S. Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). J. Biol. Chem. 281 2006 38061-70 [PubMed: 17035239] http://dx.doi.org/10.1074/jbc.M606704200
	Sohn J, Parks JM, Buhrman G, Brown P, Kristjansdottir K, Safi A, Edelsbrunner H, Yang W, Rudolph J. Experimental validation of the docking orientation of Cdc25 with its Cdk2-CycA protein substrate. Biochemistry 44 2005 16563-73 [PubMed: 16342947] http://dx.doi.org/10.1021/bi0516879
	Buhrman G, Parker B, Sohn J, Rudolph J, Mattos C. Structural mechanism of oxidative regulation of the phosphatase Cdc25B via an intramolecular disulfide bond. Biochemistry 44 2005 5307-16 [PubMed: 15807524] http://dx.doi.org/10.1021/bi047449f

InterPro 23.1