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Protein

Tryptophan--tRNA ligase, mitochondrial

Gene

MSW1

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

Catalytic activityi

ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei247 – 2471ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. tryptophan-tRNA ligase activity Source: SGD

GO - Biological processi

  1. mitochondrial tryptophanyl-tRNA aminoacylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29838-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan--tRNA ligase, mitochondrial (EC:6.1.1.2)
Alternative name(s):
Tryptophanyl-tRNA synthetase
Short name:
TrpRS
Gene namesi
Name:MSW1
Synonyms:MSW
Ordered Locus Names:YDR268W
ORF Names:D9954.7
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR268w.
EuPathDBiFungiDB:YDR268W.
SGDiS000002676. MSW1.

Subcellular locationi

  1. Mitochondrion matrix 3 Publications

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Tryptophan--tRNA ligase, mitochondrialPRO_0000136745Add
BLAST

Proteomic databases

MaxQBiP04803.
PaxDbiP04803.
PeptideAtlasiP04803.

Expressioni

Gene expression databases

GenevestigatoriP04803.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself1EBI-18837,EBI-18837

Protein-protein interaction databases

BioGridi32324. 3 interactions.
DIPiDIP-4584N.
IntActiP04803. 4 interactions.
MINTiMINT-518167.
STRINGi4932.YDR268W.

Structurei

3D structure databases

ProteinModelPortaliP04803.
SMRiP04803. Positions 36-379.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi43 – 519"HIGH" region
Motifi244 – 2485"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0180.
GeneTreeiENSGT00510000047425.
HOGENOMiHOG000059940.
InParanoidiP04803.
KOiK01867.
OMAiKCTIFYQ.
OrthoDBiEOG7M6DK3.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002306. Trp-tRNA-ligase.
[Graphical view]
PANTHERiPTHR10055. PTHR10055. 1 hit.
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01039. TRNASYNTHTRP.
TIGRFAMsiTIGR00233. trpS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04803-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNKQAVLKL ISKRWISTVQ RADFKLNSEA LHSNATVFSM IQPTGCFHLG
60 70 80 90 100
NYLGATRVWT DLCELKQPGQ ELIFGVADLH AITVPKPDGE MFRKFRHEAV
110 120 130 140 150
ASILAVGVDP EKASVIYQSA IPQHSELHWL LSTLASMGLL NRMTQWKSKS
160 170 180 190 200
NIKQSTNGDY LVNDSDVGKV RLGLFSYPVL QAADILLYKS THVPVGDDQS
210 220 230 240 250
QHLELTRHLA EKFNKMYKKN FFPKPVTMLA QTKKVLSLST PEKKMSKSDP
260 270 280 290 300
NHDSVIFLND EPKAIQKKIR KALTDSISDR FYYDPVERPG VSNLINIVSG
310 320 330 340 350
IQRKSIEDVV EDVSRFNNYR DFKDYVSEVI IEELKGPRTE FEKYINEPTY
360 370
LHSVVESGMR KAREKAAKNL ADIHKIMGF
Length:379
Mass (Da):43,015
Last modified:October 1, 1993 - v2
Checksum:i807B6D21A991E108
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti268 – 2714KIRK → RLE in AAA34809 (PubMed:2999114).Curated
Sequence conflicti371 – 3799ADIHKIMGF → PTFIK in AAA34809 (PubMed:2999114).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12081 Genomic DNA. Translation: AAA34809.1.
X66165 Genomic DNA. Translation: CAA46947.1.
U51030 Genomic DNA. Translation: AAB64452.1.
BK006938 Genomic DNA. Translation: DAA12112.1.
PIRiS70128. YWBYM.
RefSeqiNP_010554.1. NM_001180576.1.

Genome annotation databases

EnsemblFungiiYDR268W; YDR268W; YDR268W.
GeneIDi851861.
KEGGisce:YDR268W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12081 Genomic DNA. Translation: AAA34809.1.
X66165 Genomic DNA. Translation: CAA46947.1.
U51030 Genomic DNA. Translation: AAB64452.1.
BK006938 Genomic DNA. Translation: DAA12112.1.
PIRiS70128. YWBYM.
RefSeqiNP_010554.1. NM_001180576.1.

3D structure databases

ProteinModelPortaliP04803.
SMRiP04803. Positions 36-379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32324. 3 interactions.
DIPiDIP-4584N.
IntActiP04803. 4 interactions.
MINTiMINT-518167.
STRINGi4932.YDR268W.

Proteomic databases

MaxQBiP04803.
PaxDbiP04803.
PeptideAtlasiP04803.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR268W; YDR268W; YDR268W.
GeneIDi851861.
KEGGisce:YDR268W.

Organism-specific databases

CYGDiYDR268w.
EuPathDBiFungiDB:YDR268W.
SGDiS000002676. MSW1.

Phylogenomic databases

eggNOGiCOG0180.
GeneTreeiENSGT00510000047425.
HOGENOMiHOG000059940.
InParanoidiP04803.
KOiK01867.
OMAiKCTIFYQ.
OrthoDBiEOG7M6DK3.

Enzyme and pathway databases

BioCyciYEAST:G3O-29838-MONOMER.

Miscellaneous databases

NextBioi969803.
PROiP04803.

Gene expression databases

GenevestigatoriP04803.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002306. Trp-tRNA-ligase.
[Graphical view]
PANTHERiPTHR10055. PTHR10055. 1 hit.
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01039. TRNASYNTHTRP.
TIGRFAMsiTIGR00233. trpS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MSW, a yeast gene coding for mitochondrial tryptophanyl-tRNA synthetase."
    Myers A.M., Tzagoloff A.
    J. Biol. Chem. 260:15371-15377(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "An yeast nuclear mutation conferring temperature-sensitivity to the mitochondrial tryptophanyl-tRNA synthetase."
    Entrup R., Langgut W., Lisowsky T., Schweizer E.
    Curr. Genet. 21:281-283(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
    , 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.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  8. "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].

Entry informationi

Entry nameiSYWM_YEAST
AccessioniPrimary (citable) accession number: P04803
Secondary accession number(s): D6VSQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: October 1, 1993
Last modified: April 29, 2015
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 672 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

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 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.