Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thiosulfate sulfurtransferase TUM1

Gene

TUM1

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

Required for formation of the 2-thio group of the 5-methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs.1 Publication

Catalytic activityi

Thiosulfate + cyanide = sulfite + thiocyanate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei191 – 1911SubstrateBy similarity
Active sitei259 – 2591Cysteine persulfide intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • thiosulfate sulfurtransferase activity Source: SGD

GO - Biological processi

  • tRNA wobble position uridine thiolation Source: SGD
  • tRNA wobble uridine modification Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciYEAST:YOR251C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiosulfate sulfurtransferase TUM1 (EC:2.8.1.1)
Alternative name(s):
Thiouridine modification protein 1
Gene namesi
Name:TUM1
Ordered Locus Names:YOR251C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR251C.
SGDiS000005777. TUM1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304Thiosulfate sulfurtransferase TUM1PRO_0000139402Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei201 – 2011PhosphoserineCombined sources
Modified residuei264 – 2641PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ08686.
PeptideAtlasiQ08686.

PTM databases

iPTMnetiQ08686.

Interactioni

Protein-protein interaction databases

BioGridi34641. 37 interactions.
DIPiDIP-4457N.
IntActiQ08686. 6 interactions.
MINTiMINT-478300.

Structurei

Secondary structure

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Helixi9 – 1810Combined sources
Beta strandi20 – 223Combined sources
Beta strandi24 – 285Combined sources
Helixi34 – 363Combined sources
Helixi40 – 467Combined sources
Turni58 – 603Combined sources
Beta strandi66 – 683Combined sources
Helixi75 – 8410Combined sources
Beta strandi92 – 965Combined sources
Beta strandi98 – 1036Combined sources
Helixi104 – 11310Combined sources
Beta strandi117 – 1237Combined sources
Helixi125 – 1306Combined sources
Helixi158 – 1614Combined sources
Helixi165 – 1739Combined sources
Helixi177 – 1804Combined sources
Beta strandi182 – 1854Combined sources
Helixi189 – 1924Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi211 – 2133Combined sources
Helixi216 – 2194Combined sources
Turni222 – 2243Combined sources
Helixi232 – 24413Combined sources
Beta strandi255 – 2584Combined sources
Beta strandi260 – 2623Combined sources
Helixi263 – 27412Combined sources
Beta strandi279 – 2857Combined sources
Helixi286 – 2949Combined sources
Helixi296 – 2983Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UTNX-ray1.90X1-304[»]
ProteinModelPortaliQ08686.
SMRiQ08686. Positions 1-304.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 137118Rhodanese 1PROSITE-ProRule annotationAdd
BLAST
Domaini177 – 299123Rhodanese 2PROSITE-ProRule annotationAdd
BLAST

Domaini

Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).By similarity

Sequence similaritiesi

Contains 2 rhodanese domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
InParanoidiQ08686.
KOiK01011.
OMAiAWFLPND.
OrthoDBiEOG7ZGXDV.

Family and domain databases

Gene3Di3.40.250.10. 2 hits.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTiSM00450. RHOD. 2 hits.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 2 hits.
PROSITEiPS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08686-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLFDLISPK AFVKLVASEK VHRIVPVDAT WYLPSWKLDN KVDFLTKPRI
60 70 80 90 100
PNSIFFDIDA ISDKKSPYPH MFPTKKVFDD AMSNLGVQKD DILVVYDRVG
110 120 130 140 150
NFSSPRCAWT LGVMGHPKVY LLNNFNQYRE FKYPLDSSKV AAFSPYPKSH
160 170 180 190 200
YESSESFQDK EIVDYEEMFQ LVKSGELAKK FNAFDARSLG RFEGTEPEPR
210 220 230 240 250
SDIPSGHIPG TQPLPYGSLL DPETKTYPEA GEAIHATLEK ALKDFHCTLD
260 270 280 290 300
PSKPTICSCG TGVSGVIIKT ALELAGVPNV RLYDGSWTEW VLKSGPEWIA

ENRD
Length:304
Mass (Da):34,219
Last modified:November 1, 1996 - v1
Checksum:iF8082DF7CC279E82
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75159 Genomic DNA. Translation: CAA99473.1.
AY692732 Genomic DNA. Translation: AAT92751.1.
BK006948 Genomic DNA. Translation: DAA11018.1.
PIRiS67148.
RefSeqiNP_014894.3. NM_001183670.3.

Genome annotation databases

EnsemblFungiiYOR251C; YOR251C; YOR251C.
GeneIDi854425.
KEGGisce:YOR251C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75159 Genomic DNA. Translation: CAA99473.1.
AY692732 Genomic DNA. Translation: AAT92751.1.
BK006948 Genomic DNA. Translation: DAA11018.1.
PIRiS67148.
RefSeqiNP_014894.3. NM_001183670.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UTNX-ray1.90X1-304[»]
ProteinModelPortaliQ08686.
SMRiQ08686. Positions 1-304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34641. 37 interactions.
DIPiDIP-4457N.
IntActiQ08686. 6 interactions.
MINTiMINT-478300.

PTM databases

iPTMnetiQ08686.

Proteomic databases

MaxQBiQ08686.
PeptideAtlasiQ08686.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR251C; YOR251C; YOR251C.
GeneIDi854425.
KEGGisce:YOR251C.

Organism-specific databases

EuPathDBiFungiDB:YOR251C.
SGDiS000005777. TUM1.

Phylogenomic databases

GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
InParanoidiQ08686.
KOiK01011.
OMAiAWFLPND.
OrthoDBiEOG7ZGXDV.

Enzyme and pathway databases

BioCyciYEAST:YOR251C-MONOMER.

Miscellaneous databases

NextBioi976640.
PROiQ08686.

Family and domain databases

Gene3Di3.40.250.10. 2 hits.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTiSM00450. RHOD. 2 hits.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 2 hits.
PROSITEiPS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1 and VPH1."
    Poirey R., Jauniaux J.-C.
    Yeast 13:483-487(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae."
    Huang B., Lu J., Bystroem A.S.
    RNA 14:2183-2194(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTHTR_YEAST
AccessioniPrimary (citable) accession number: Q08686
Secondary accession number(s): D6W2V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 136 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 5770 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. 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.