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Q12093 (MTU1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial tRNA-specific 2-thiouridylase 1

EC=2.8.1.-
Alternative name(s):
Mitochondrial translation optimization protein 2
Synthetic lethal with MSS4 3
Gene names
Name:SLM3
Synonyms:MTO2, MTU1
Ordered Locus Names:YDL033C
ORF Names:D2761
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base. Ref.1 Ref.5 Ref.6

Subcellular location

Mitochondrion Ref.1 Ref.5.

Miscellaneous

Present with 1510 molecules/cell in log phase SD medium.

During the reaction, ATP is used to activate the C2 atom of U34 by adenylation. After this, the persulfide sulfur on the catalytic cysteine is transferred to the C2 atom of the wobble base (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards the activated C2 atom on U34. Subsequently, a transient disulfide bond is formed between the two active site cysteine residues By similarity.

Sequence similarities

Belongs to the MnmA/TRMU family.

Caution

Was originally thought to be a 5-methylaminomethyl-2-methyltransferase involved in tRNA modification.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-19558,EBI-19558
HSP60P198821EBI-19558,EBI-8586

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Mitochondrial tRNA-specific 2-thiouridylase 1
PRO_0000121711

Regions

Nucleotide binding32 – 398ATP By similarity
Region122 – 1243Interaction with target base in tRNA By similarity
Region179 – 1813Interaction with tRNA By similarity
Region354 – 3552Interaction with tRNA By similarity

Sites

Active site1271Nucleophile By similarity
Active site2291Cysteine persulfide intermediate By similarity
Binding site581ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site1541ATP; via amide nitrogen By similarity
Site1551Interaction with tRNA By similarity
Site2811Interaction with tRNA By similarity
Site3911Interaction with tRNA By similarity

Amino acid modifications

Disulfide bond127 ↔ 229Alternate By similarity

Experimental info

Mutagenesis381D → A: Loss of activity. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q12093 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 15BF63FD9A094890

FASTA41747,049
        10         20         30         40         50         60 
MLARYLNLIG RRSASPYRPQ RLPAKFDNVI VAMSSGVDSS VAAALFAGEF PNTRGVYMQN 

        70         80         90        100        110        120 
WSESQSLDDP GKEPCYERDW RDVNRVAKHL NIRVDKVNFE QDYWIDVFEP MLRGYSEGST 

       130        140        150        160        170        180 
PNPDIGCNKF VKFGKLREWL DEKYGTGNYW LVTGHYARVM QEMNGKGLFH LLRSIYRPKD 

       190        200        210        220        230        240 
QSYYLSQINS TVLSSLLLPI GHLTKPEVRD LAKYAGLPTA EKPDSQGICF VNNSQHGKFK 

       250        260        270        280        290        300 
NFLKHYLPSS PGDIITVDPQ SGAKTTWGRH DGLWSYTIGQ KVGISMPQAD PNYQGTWFVS 

       310        320        330        340        350        360 
EKLRDTNEIL IVRGRDNPAL YSDTMRIENF SSLGPREDTI NAFQNTGALT LQFRSLQVPV 

       370        380        390        400        410 
QIKSCKLNRS ADNLDITIHL ASKQRAITPG QSCCLYIDDR VLGSGPISHV NNNDTHA 

« Hide

References

« Hide 'large scale' references
[1]"Mutations in MTO2 related to tRNA modification impair mitochondrial gene expression and protein synthesis in the presence of a paromomycin resistance mutation in mitochondrial 15 S rRNA."
Yan Q., Li X., Faye G., Guan M.-X.
J. Biol. Chem. 280:29151-29157(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
Strain: ATCC 201238 / W303-1B.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"Mitochondria-specific RNA-modifying enzymes responsible for the biosynthesis of the wobble base in mitochondrial tRNAs. Implications for the molecular pathogenesis of human mitochondrial diseases."
Umeda N., Suzuki T., Yukawa M., Ohya Y., Shindo H., Watanabe K., Suzuki T.
J. Biol. Chem. 280:1613-1624(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-38.
[6]"Deletion of the MTO2 gene related to tRNA modification causes a failure in mitochondrial RNA metabolism in the yeast Saccharomyces cerevisiae."
Wang X., Yan Q., Guan M.X.
FEBS Lett. 581:4228-4234(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY624369 Genomic DNA. Translation: AAT44736.1.
Z71781 Genomic DNA. Translation: CAA96456.1.
Z74081 Genomic DNA. Translation: CAA98591.1.
BK006938 Genomic DNA. Translation: DAA11820.1.
PIRS67566.
RefSeqNP_010251.1. NM_001180092.1.

3D structure databases

ProteinModelPortalQ12093.
SMRQ12093. Positions 29-409.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32024. 150 interactions.
IntActQ12093. 2 interactions.
MINTMINT-640057.
STRING4932.YDL033C.

Proteomic databases

MaxQBQ12093.
PaxDbQ12093.
PeptideAtlasQ12093.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL033C; YDL033C; YDL033C.
GeneID851529.
KEGGsce:YDL033C.

Organism-specific databases

CYGDYDL033c.
SGDS000002191. SLM3.

Phylogenomic databases

eggNOGCOG0482.
GeneTreeENSGT00390000014323.
HOGENOMHOG000218046.
KOK00566.
OMACAFYEGD.
OrthoDBEOG7034VG.

Enzyme and pathway databases

BioCycYEAST:G3O-29458-MONOMER.

Gene expression databases

GenevestigatorQ12093.

Family and domain databases

Gene3D2.30.30.280. 1 hit.
3.40.50.620. 1 hit.
InterProIPR023382. Adenine_a_hdrlase_dom.
IPR014729. Rossmann-like_a/b/a_fold.
IPR004506. tRNA-specific_2-thiouridylase.
[Graphical view]
PANTHERPTHR11933. PTHR11933. 1 hit.
PfamPF03054. tRNA_Me_trans. 1 hit.
[Graphical view]
TIGRFAMsTIGR00420. trmU. 1 hit.
ProtoNetSearch...

Other

NextBio968917.
PROQ12093.

Entry information

Entry nameMTU1_YEAST
AccessionPrimary (citable) accession number: Q12093
Secondary accession number(s): D6VRW0, Q6IUF4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 14, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families