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Protein

Tyrosine--tRNA ligase, cytoplasmic

Gene

TYS1

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

Functioni

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). The specificity determinants on tRNA(Tyr) are the base pair C1-G72, the discriminator residue A73, and the three anticodon bases G34, U35 and A36. Also involved in nuclear tRNA export.2 Publications

Catalytic activityi

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).

Enzyme regulationi

Inhibited by N-ethylmaleimide and p-chloromercuribenzoate.1 Publication

Kineticsi

The catalytic activity is reduced by substitutions of residues forming the specificity determinant on the target tRNA(Tyr).

  1. KM=54 nM for tRNA(Tyr)1 Publication
  1. Vmax=280 nmol/min/mg enzyme for tRNA(Tyr)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431TyrosineBy similarity
Binding sitei170 – 1701TyrosineBy similarity
Binding sitei174 – 1741TyrosineBy similarity
Binding sitei177 – 1771TyrosineBy similarity
Binding sitei192 – 1921TyrosineBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • tyrosine-tRNA ligase activity Source: SGD

GO - Biological processi

  • tyrosyl-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-30875-MONOMER.
BRENDAi6.1.1.1. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine--tRNA ligase, cytoplasmic (EC:6.1.1.1)
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name:
TyrRS
Gene namesi
Name:TYS1
Synonyms:MGM104
Ordered Locus Names:YGR185C
ORF Names:G7522
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR185C.
SGDiS000003417. TYS1.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Predominantly cytoplasmic, only a small fraction (about 1.5%) found in the nucleus.

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 431Y → G: Decreases catalytic activity for L-tyrosine 400-fold, but allows the utilization of 3-iodo-L-tyrosine and other 3-modified tyrosines as substrates. 1 Publication
Mutagenesisi364 – 3685KKAKK → EEAEE: Abolishes nuclear localization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 394393Tyrosine--tRNA ligase, cytoplasmicPRO_0000055676Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei235 – 2351PhosphoserineCombined sources
Modified residuei359 – 3591PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP36421.
PeptideAtlasiP36421.

PTM databases

iPTMnetiP36421.

Interactioni

Subunit structurei

Homodimer. Interacts with KNR4/SMI1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SMI1P325663EBI-18843,EBI-17452

Protein-protein interaction databases

BioGridi33437. 107 interactions.
DIPiDIP-5548N.
IntActiP36421. 18 interactions.
MINTiMINT-572629.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 179Combined sources
Beta strandi21 – 244Combined sources
Helixi26 – 349Combined sources
Beta strandi41 – 466Combined sources
Helixi54 – 563Combined sources
Helixi57 – 6812Combined sources
Beta strandi72 – 776Combined sources
Helixi79 – 846Combined sources
Turni85 – 873Combined sources
Helixi93 – 11119Combined sources
Beta strandi120 – 1234Combined sources
Helixi125 – 1284Combined sources
Helixi131 – 14111Combined sources
Helixi146 – 1527Combined sources
Turni153 – 1564Combined sources
Helixi166 – 18015Combined sources
Beta strandi184 – 1896Combined sources
Helixi190 – 1923Combined sources
Helixi193 – 20210Combined sources
Helixi203 – 2064Combined sources
Beta strandi212 – 2165Combined sources
Helixi243 – 25210Combined sources
Helixi264 – 2718Combined sources
Helixi273 – 2786Combined sources
Beta strandi280 – 2823Combined sources
Beta strandi288 – 2903Combined sources
Helixi294 – 2963Combined sources
Beta strandi300 – 3045Combined sources
Helixi305 – 3139Combined sources
Helixi319 – 34325Combined sources
Helixi345 – 35410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DLCX-ray2.40X1-394[»]
ProteinModelPortaliP36421.
SMRiP36421. Positions 8-356.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36421.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi48 – 569"HIGH" region
Motifi227 – 2315"KMSKS" region
Motifi360 – 37819Nuclear localization signalAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00790000123100.
HOGENOMiHOG000228237.
InParanoidiP36421.
KOiK01866.
OMAiISVEKXE.
OrthoDBiEOG70KH0F.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002307. Tyr-tRNA-ligase.
IPR023617. Tyr-tRNA-ligase_arc/euk-type.
[Graphical view]
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PIRSFiPIRSF006588. TyrRS_arch_euk. 1 hit.
PRINTSiPR01040. TRNASYNTHTYR.
TIGRFAMsiTIGR00234. tyrS. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P36421-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSAATVDPN EAFGLITKNL QEVLNPQIIK DVLEVQKRHL KLYWGTAPTG
60 70 80 90 100
RPHCGYFVPM TKLADFLKAG CEVTVLLADL HAFLDNMKAP LEVVNYRAKY
110 120 130 140 150
YELTIKAILR SINVPIEKLK FVVGSSYQLT PDYTMDIFRL SNIVSQNDAK
160 170 180 190 200
RAGADVVKQV ANPLLSGLIY PLMQALDEQF LDVDCQFGGV DQRKIFVLAE
210 220 230 240 250
ENLPSLGYKK RAHLMNPMVP GLAQGGKMSA SDPNSKIDLL EEPKQVKKKI
260 270 280 290 300
NSAFCSPGNV EENGLLSFVQ YVIAPIQELK FGTNHFEFFI DRPEKFGGPI
310 320 330 340 350
TYKSFEEMKL AFKEEKLSPP DLKIGVADAI NELLEPIRQE FANNKEFQEA
360 370 380 390
SEKGYPVATP QKSKKAKKPK NKGTKYPGAT KTNEIATKLE ETKL
Length:394
Mass (Da):44,020
Last modified:January 23, 2007 - v3
Checksum:i57E8DB9BE6D054B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12221 mRNA. Translation: AAB59329.1.
X71998 Genomic DNA. No translation available.
X99074 Genomic DNA. Translation: CAA67529.1.
Z72970 Genomic DNA. Translation: CAA97211.1.
U13015 Genomic DNA. Translation: AAA61641.1.
BK006941 Genomic DNA. Translation: DAA08279.1.
PIRiA45999.
RefSeqiNP_011701.3. NM_001181314.3.

Genome annotation databases

EnsemblFungiiYGR185C; YGR185C; YGR185C.
GeneIDi853097.
KEGGisce:YGR185C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12221 mRNA. Translation: AAB59329.1.
X71998 Genomic DNA. No translation available.
X99074 Genomic DNA. Translation: CAA67529.1.
Z72970 Genomic DNA. Translation: CAA97211.1.
U13015 Genomic DNA. Translation: AAA61641.1.
BK006941 Genomic DNA. Translation: DAA08279.1.
PIRiA45999.
RefSeqiNP_011701.3. NM_001181314.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DLCX-ray2.40X1-394[»]
ProteinModelPortaliP36421.
SMRiP36421. Positions 8-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33437. 107 interactions.
DIPiDIP-5548N.
IntActiP36421. 18 interactions.
MINTiMINT-572629.

PTM databases

iPTMnetiP36421.

Proteomic databases

MaxQBiP36421.
PeptideAtlasiP36421.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR185C; YGR185C; YGR185C.
GeneIDi853097.
KEGGisce:YGR185C.

Organism-specific databases

EuPathDBiFungiDB:YGR185C.
SGDiS000003417. TYS1.

Phylogenomic databases

GeneTreeiENSGT00790000123100.
HOGENOMiHOG000228237.
InParanoidiP36421.
KOiK01866.
OMAiISVEKXE.
OrthoDBiEOG70KH0F.

Enzyme and pathway databases

BioCyciYEAST:G3O-30875-MONOMER.
BRENDAi6.1.1.1. 984.

Miscellaneous databases

EvolutionaryTraceiP36421.
NextBioi973090.
PROiP36421.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002307. Tyr-tRNA-ligase.
IPR023617. Tyr-tRNA-ligase_arc/euk-type.
[Graphical view]
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PIRSFiPIRSF006588. TyrRS_arch_euk. 1 hit.
PRINTSiPR01040. TRNASYNTHTYR.
TIGRFAMsiTIGR00234. tyrS. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Saccharomyces cerevisiae cytoplasmic tyrosyl-tRNA synthetase gene. Isolation by complementation of a mutant Escherichia coli suppressor tRNA defective in aminoacylation and sequence analysis."
    Chow C.M., RajBhandary U.L.
    J. Biol. Chem. 268:12855-12863(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cytoplasmic tyrosyl-tRNA synthetase rescues the defect in mitochondrial genome maintenance caused by the nuclear mutation mgm104-1 in the yeast Saccharomyces cerevisiae."
    Guan M.-X.
    Mol. Gen. Genet. 255:525-532(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "DNA sequence analysis of a 23,002 bp DNA fragment of the right arm of Saccharomyces cerevisiae chromosome VII."
    Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez-Perez M., Nombela C.
    Yeast 13:357-363(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
    Strain: ATCC 208279 / BJ926.
  7. Bienvenut W.V., Peters C.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-18 AND 324-338, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Tyroslyl-tRNA synthetase from baker's yeast. Rapid isolation by affinity elution, molecular weight of the enzyme, and determination of essential sulfhydryl groups."
    Faulhammer H.G., Cramer F.
    Eur. J. Biochem. 75:561-570(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, ENZYME REGULATION.
  9. "Specific substitution into the anticodon loop of yeast tyrosine transfer RNA."
    Bare L.A., Uhlenbeck O.C.
    Biochemistry 25:5825-5830(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  10. "Nuclear tRNA aminoacylation and its role in nuclear export of endogenous tRNAs in Saccharomyces cerevisiae."
    Sarkar S., Azad A.K., Hopper A.K.
    Proc. Natl. Acad. Sci. U.S.A. 96:14366-14371(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Identity of tRNA for yeast tyrosyl-tRNA synthetase: tyrosylation is more sensitive to identity nucleotides than to structural features."
    Fechter P., Rudinger-Thirion J., Theobald-Dietrich A., Giege R.
    Biochemistry 39:1725-1733(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Interaction of Knr4 protein, a protein involved in cell wall synthesis, with tyrosine tRNA synthetase encoded by TYS1 in Saccharomyces cerevisiae."
    Dagkessamanskaia A., Martin-Yken H., Basmaji F., Briza P., Francois J.
    FEMS Microbiol. Lett. 200:53-58(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KNR4/SMI1.
  13. "Changing the amino acid specificity of yeast tyrosyl-tRNA synthetase by genetic engineering."
    Ohno S., Yokogawa T., Nishikawa K.
    J. Biochem. 130:417-423(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-43.
  14. "Role of nuclear pools of aminoacyl-tRNA synthetases in tRNA nuclear export."
    Azad A.K., Stanford D.R., Sarkar S., Hopper A.K.
    Mol. Biol. Cell 12:1381-1392(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 364-LYS--LYS-368, SUBCELLULAR LOCATION.
  15. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  16. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  17. "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-235 AND THR-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYYC_YEAST
AccessioniPrimary (citable) accession number: P36421
Secondary accession number(s): D6VUW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2710 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.