Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P48527 (SYYM_YEAST)

Last modified November 3, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tyrosyl-tRNA synthetase, mitochondrial
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase
      Short name=TyrRS
Gene names
Name: MSY1
Ordered Locus Names: YPL097W
ORF Names: LPG11W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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) By similarity.

Catalytic activity

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

Subcellular location

Mitochondrion matrix. Ref.3 Ref.5 Ref.6

Miscellaneous

Present with 996 molecules/cell in log phase SD medium. Ref.4

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtyrosyl-tRNA aminoacylation

Traceable author statement. Source: SGD

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction. Source: IntAct

tyrosine-tRNA ligase activity

Traceable author statement. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-18851,EBI-18851

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 492Tyrosyl-tRNA synthetase, mitochondrialPRO_0000035835

Regions

Motif94 – 10310"HIGH" region
Motif303 – 3075"KMSKS" region

Sites

Binding site3061ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P48527-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 2159116E1CB5ED2E

FASTA49255,287
        10         20         30         40         50         60 
MLELRSCSNL VNSSRRLVPL VTYSGLSAIT LPKSRFYSQP SALEVQGTSD SRSDNILDEL 

        70         80         90        100        110        120 
KQRGLVSQVS QPESFLRTKL NGNDKIKLYC GVDPTAQSLH LGNLVPLMVL LHFYVKGHDI 

       130        140        150        160        170        180 
VTVIGGATGK VGDPSGRKTE RDVMENDIRQ SNVASISQQL QRFFKNGLEY YRNRCALTED 

       190        200        210        220        230        240 
VPSGKYTPRN NFNWWKDIKM LDFLADFGRH IRVQSMLARD SISSRLQTKN GLGFNEFTYQ 

       250        260        270        280        290        300 
VLQAYDFYHL YKEENVTIQV GGNDQWGNIT AGIDLINRIQ PIKNKGLPFG ITVPLLTTAT 

       310        320        330        340        350        360 
GEKFGKSAGN AVFIDPSINT AYDVYQFFYN TLDADVPKFL KIFTFLNSSE IKKIVETHIK 

       370        380        390        400        410        420 
SPSLRYGQTL LAKEVTDMLY GVGSGSDSEA LSNIIFGRYD GTLSAAKLVD LCKKARILQY 

       430        440        450        460        470        480 
ADREIDLIKL ICKLVNCSVS EARRKLSQGS VYLHHSKSKV NENISNLAPF LIDDRVLILR 

       490 
IGKQKCFIIE MR 

« Hide

References

« Hide 'large scale' references
[1]"The nuclear gene MSY1 of Saccharomyces cerevisiae codes for mitochondrial tyrosyl-tRNA synthetase."
Hill J.E., Tzagoloff A.A.
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 24657 / D273-10B.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"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].
[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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]"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: 16823961] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

L42333 Genomic DNA. Translation: AAA67122.1.
U43281 Genomic DNA. Translation: AAB68202.1.
PIRS59733.
RefSeqNP_015228.1.

3D structure databases

HSSPHSSP built from PDB template 1TYC based on UniProtKB P00952.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:3826N.
IntActP48527. 2 interactions.
STRINGP48527.

Genome annotation databases

EnsemblYPL097W; YPL097W; YPL097W; Saccharomyces cerevisiae. [Genome view]
GeneID856007.
GenomeReviewsGene locus YPL097W in contig U00094_GR.
KEGGsce:YPL097W.
NMPDRfig|4932.3.peg.6360.

Organism-specific databases

CYGDYPL097w.
SGDS000006018. MSY1.

Phylogenomic databases

HOGENOMP48527.
OMAMLARDSI.

Enzyme and pathway databases

BRENDA6.1.1.1. 250.

Gene expression databases

ArrayExpressP48527.
GenevestigatorP48527.
GermOnlineYPL097W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ib.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002307. Tyr-tRNA-synth_Ib_bac/mito.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11766. Tyr_tRNA-synt_1b. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01040. TRNASYNTHTYR.
TIGRFAMsTIGR00234. tyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio980887.

Entry information

Entry nameSYYM_YEAST
AccessionPrimary (citable) accession number: P48527
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 3, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Yeast

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents