Tyrosyl-tRNA synthetase, cytoplasmic - Saccharomyces cerevisiae (Baker's yeast)

Names and origin

Protein names

Recommended name:
    Tyrosyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.1
Alternative name(s):
    Tyrosyl--tRNA ligase
      Short name=TyrRS

Gene names

Name:	TYS1
Synonyms:	MGM104
Ordered Locus Names:	YGR185C
ORF Names:	G7522

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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. Ref.9 Ref.10
Catalytic activity	ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).
Enzyme regulation	Inhibited by N-ethylmaleimide and p-chloromercuribenzoate. Ref.7
Subunit structure	Homodimer. Interacts with KNR4/SMI1. Ref.7 Ref.11
Subcellular location	Cytoplasm. Nucleus. Note: Predominantly cytoplasmic, only a small fraction (about 1.5%) found in the nucleus. Ref.13 Ref.15
Miscellaneous	Present with 2710 molecules/cell in log phase SD medium. Ref.16
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.
Biophysicochemical properties	Kinetic parameters: The catalytic activity is reduced by substitutions of residues forming the specificity determinant on the target tRNA(Tyr). K_M=54 nM for tRNA(Tyr) V_max=280 nmol/min/mg enzyme for tRNA(Tyr)

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Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	tyrosyl-tRNA aminoacylation Ref.1 Inferred from direct assay. Source: SGD
Cellular component	cytoplasm Ref.13 Inferred from direct assay. Source: SGD nucleus Ref.13 Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct tyrosine-tRNA ligase activity Ref.1 Inferred from direct assay. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
MRPS16	Q02608	1	EBI-18843,EBI-16281
SMI1	P32566	3	EBI-18843,EBI-17452

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed Ref.6

Chain

2 – 394

393

Tyrosyl-tRNA synthetase, cytoplasmic

PRO_0000055676

Regions

Motif

48 – 56

9

"HIGH" region

Motif

227 – 231

5

"KMSKS" region

Motif

360 – 378

19

Nuclear localization signal

Sites

Binding site

43

1

Tyrosine By similarity

Binding site

170

1

Tyrosine By similarity

Binding site

174

1

Tyrosine By similarity

Binding site

177

1

Tyrosine By similarity

Binding site

192

1

Tyrosine By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.6

Modified residue

235

1

Phosphoserine Ref.17

Modified residue

359

1

Phosphothreonine Ref.17 Ref.14

Experimental info

Mutagenesis

43

1

Y → 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. Ref.12

Mutagenesis

364 – 368

5

KKAKK → EEAEE: Abolishes nuclear localization. Ref.13

Secondary structure

1

.

394

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P36421-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 57E8DB9BE6D054B7
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FASTA

394

44,020

        10         20         30         40         50         60 
MSSAATVDPN EAFGLITKNL QEVLNPQIIK DVLEVQKRHL KLYWGTAPTG RPHCGYFVPM 

        70         80         90        100        110        120 
TKLADFLKAG CEVTVLLADL HAFLDNMKAP LEVVNYRAKY YELTIKAILR SINVPIEKLK 

       130        140        150        160        170        180 
FVVGSSYQLT PDYTMDIFRL SNIVSQNDAK RAGADVVKQV ANPLLSGLIY PLMQALDEQF 

       190        200        210        220        230        240 
LDVDCQFGGV DQRKIFVLAE ENLPSLGYKK RAHLMNPMVP GLAQGGKMSA SDPNSKIDLL 

       250        260        270        280        290        300 
EEPKQVKKKI NSAFCSPGNV EENGLLSFVQ YVIAPIQELK FGTNHFEFFI DRPEKFGGPI 

       310        320        330        340        350        360 
TYKSFEEMKL AFKEEKLSPP DLKIGVADAI NELLEPIRQE FANNKEFQEA SEKGYPVATP 

       370        380        390 
QKSKKAKKPK NKGTKYPGAT KTNEIATKLE ETKL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8509419] [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: 9294037] [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: 9133739] [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. Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"TFIIF-TAF-RNA polymerase II connection." Henry N.L., Campbell A.M., Feaver W.J., Poon D., Weil P.A., Kornberg R.D. Genes Dev. 8:2868-2878(1994) [PubMed: 7995524] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36. Strain: ATCC 208279 / BJ926.
[6]	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, MASS SPECTROMETRY.
[7]	"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: 328277] [Abstract] Cited for: SUBUNIT, ENZYME REGULATION.
[8]	"Specific substitution into the anticodon loop of yeast tyrosine transfer RNA." Bare L.A., Uhlenbeck O.C. Biochemistry 25:5825-5830(1986) [PubMed: 3535890] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[9]	"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: 10588711] [Abstract] Cited for: FUNCTION.
[10]	"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: 10677221] [Abstract] Cited for: FUNCTION.
[11]	"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: 11410349] [Abstract] Cited for: INTERACTION WITH KNR4/SMI1.
[12]	"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: 11530018] [Abstract] Cited for: MUTAGENESIS OF TYR-43.
[13]	"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: 11359929] [Abstract] Cited for: MUTAGENESIS OF 364-LYS--LYS-368, SUBCELLULAR LOCATION.
[14]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359, MASS SPECTROMETRY.
[15]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[16]	"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: 14562106] [Abstract] 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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND THR-359, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

A45999.

RefSeq

NP_011701.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DLC	X-ray	2.40	X	2-393	[»]

ModBase

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Protein-protein interaction databases

DIP

DIP-5548N.

IntAct

P36421. 17 interactions.

STRING

P36421.

Proteomic databases

PeptideAtlas

P36421.

Genome annotation databases

Ensembl

YGR185C; YGR185C; YGR185C; Saccharomyces cerevisiae. [Genome view]

GeneID

853097.

KEGG

sce:YGR185C.

NMPDR

fig|4932.3.peg.2828.

Organism-specific databases

CYGD

YGR185c.

SGD

S000003417. TYS1.

Phylogenomic databases

eggNOG

HOGENOM

OMA

OrthoDB

PhylomeDB

P36421.

Enzyme and pathway databases

BRENDA

6.1.1.1. 250.

Gene expression databases

ArrayExpress

P36421.

Genevestigator

P36421.

GermOnline

YGR185C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002305. aa-tRNA-synth_Ib.
IPR014729. Rossmann-like_a/b/a_fold.
IPR015624. Tyr-tRNA-synth_Ib_arc/euk.
IPR002307. Tyr-tRNA-synth_Ib_bac/mito.
IPR016485. TyrRS_arch_euk.
[Graphical view]

Gene3D

G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.

PANTHER

PTHR11946:SF8. Tyr-tRNA_synth. 1 hit.

Pfam

PF00579. tRNA-synt_1b. 1 hit.
[Graphical view]

PIRSF

PIRSF006588. TyrRS_arch_euk. 1 hit.

PRINTS

PR01040. TRNASYNTHTYR.

TIGRFAMs

TIGR00234. tyrS. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

973090.

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Entry information

Entry name

SYYC_YEAST

Accession

Primary (citable) accession number: P36421

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome VII

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents