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Protein

Thiosulfate sulfurtransferase RDL2, mitochondrial

Gene

RDL2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Thiosulfate sulfurtransferase which catalyzes the transfer of sulfane sulfur from thiosulfate to cyanide.1 Publication

Catalytic activityi

Thiosulfate + cyanide = sulfite + thiocyanate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei106 – 1061Cysteine persulfide intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • thiosulfate sulfurtransferase activity Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12520.
YEAST:G3O-33772-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiosulfate sulfurtransferase RDL2, mitochondrial (EC:2.8.1.1)
Alternative name(s):
Altered inheritance of mitochondria protein 42
Found in mitochondrial proteome protein 31
Rhodanese-like protein 2
Gene namesi
Name:RDL2
Synonyms:AIM42, FMP31
Ordered Locus Names:YOR286W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR286W.
SGDiS000005812. RDL2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Increases frequency of mitochondrial genome loss.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionSequence analysisAdd
BLAST
Chaini26 – 149124Thiosulfate sulfurtransferase RDL2, mitochondrialPRO_0000245268Add
BLAST

Proteomic databases

MaxQBiQ08742.

Interactioni

Protein-protein interaction databases

BioGridi34673. 20 interactions.
DIPiDIP-4456N.
IntActiQ08742. 1 interaction.
MINTiMINT-570061.

Structurei

3D structure databases

ProteinModelPortaliQ08742.
SMRiQ08742. Positions 33-142.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 146102RhodanesePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00510000047949.
InParanoidiQ08742.
OMAiKELIFFC.
OrthoDBiEOG7MKWJ9.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q08742-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKHSTGILS RTVSARSPTL VLRTFTTKAP KIYTFDQVRN LVEHPNDKKL
60 70 80 90 100
LVDVREPKEV KDYKMPTTIN IPVNSAPGAL GLPEKEFHKV FQFAKPPHDK
110 120 130 140
ELIFLCAKGV RAKTAEELAR SYGYENTGIY PGSITEWLAK GGADVKPKK
Length:149
Mass (Da):16,697
Last modified:November 1, 1996 - v1
Checksum:i8BF91B05233CB81F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75194 Genomic DNA. Translation: CAA99513.1.
AY692684 Genomic DNA. Translation: AAT92703.1.
BK006948 Genomic DNA. Translation: DAA11050.1.
PIRiS67188.
RefSeqiNP_014929.3. NM_001183705.3.

Genome annotation databases

EnsemblFungiiYOR286W; YOR286W; YOR286W.
GeneIDi854460.
KEGGisce:YOR286W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75194 Genomic DNA. Translation: CAA99513.1.
AY692684 Genomic DNA. Translation: AAT92703.1.
BK006948 Genomic DNA. Translation: DAA11050.1.
PIRiS67188.
RefSeqiNP_014929.3. NM_001183705.3.

3D structure databases

ProteinModelPortaliQ08742.
SMRiQ08742. Positions 33-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34673. 20 interactions.
DIPiDIP-4456N.
IntActiQ08742. 1 interaction.
MINTiMINT-570061.

Proteomic databases

MaxQBiQ08742.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR286W; YOR286W; YOR286W.
GeneIDi854460.
KEGGisce:YOR286W.

Organism-specific databases

EuPathDBiFungiDB:YOR286W.
SGDiS000005812. RDL2.

Phylogenomic databases

GeneTreeiENSGT00510000047949.
InParanoidiQ08742.
OMAiKELIFFC.
OrthoDBiEOG7MKWJ9.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12520.
YEAST:G3O-33772-MONOMER.

Miscellaneous databases

PROiQ08742.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  7. "Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
    Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
    J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. "Computationally driven, quantitative experiments discover genes required for mitochondrial biogenesis."
    Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J., Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M., Troyanskaya O.G., Caudy A.A.
    PLoS Genet. 5:E1000407-E1000407(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. Cited for: FUNCTION.

Entry informationi

Entry nameiRDL2_YEAST
AccessioniPrimary (citable) accession number: Q08742
Secondary accession number(s): D6W2Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4220 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.