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P46655 (SYEC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Glutamate--tRNA ligase, cytoplasmic

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
P85
Gene names
Name:GUS1
Ordered Locus Names:YGL245W
ORF Names:G0583, HRB724
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length708 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity.

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).

Subunit structure

Interacts with ARC1. Ref.11 Ref.12

Subcellular location

Cytoplasm Ref.7.

Miscellaneous

Present with 48700 molecules/cell in log phase SD medium.

Sequence similarities

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

Sequence caution

The sequence AAA78905.1 differs from that shown. Reason: Frameshift at position 698.

The sequence CAA64142.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA89009.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA96964.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARC1P466727EBI-18665,EBI-7224

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 708708Glutamate--tRNA ligase, cytoplasmic
PRO_0000119739

Regions

Nucleotide binding437 – 4415ATP By similarity
Region205 – 2073Glutamate binding By similarity
Region382 – 3865Glutamate binding By similarity
Motif210 – 21910"HIGH" region
Motif437 – 4415"KMSKS" region

Sites

Binding site2151ATP By similarity
Binding site2411Glutamate By similarity
Binding site4001Glutamate By similarity
Binding site4031ATP By similarity

Amino acid modifications

Modified residue3001Phosphothreonine Ref.9

Experimental info

Sequence conflict2091E → D in AAA78905. Ref.1
Sequence conflict4731V → A in AAA78905. Ref.1
Sequence conflict5101P → S in AAA78905. Ref.1
Sequence conflict5461V → M in AAA78905. Ref.1

Secondary structure

.............................. 708
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46655 [UniParc].

Last modified September 5, 2006. Version 3.
Checksum: EADAD430A2D98974

FASTA70880,843
        10         20         30         40         50         60 
MPSTLTINGK APIVAYAELI AARIVNALAP NSIAIKLVDD KKAPAAKLDD ATEDVFNKIT 

        70         80         90        100        110        120 
SKFAAIFDNG DKEQVAKWVN LAQKELVIKN FAKLSQSLET LDSQLNLRTF ILGGLKYSAA 

       130        140        150        160        170        180 
DVACWGALRS NGMCGSIIKN KVDVNVSRWY TLLEMDPIFG EAHDFLSKSL LELKKSANVG 

       190        200        210        220        230        240 
KKKETHKANF EIDLPDAKMG EVVTRFPPEP SGYLHIGHAK AALLNQYFAQ AYKGKLIIRF 

       250        260        270        280        290        300 
DDTNPSKEKE EFQDSILEDL DLLGIKGDRI TYSSDYFQEM YDYCVQMIKD GKAYCDDTPT 

       310        320        330        340        350        360 
EKMREERMDG VASARRDRSV EENLRIFTEE MKNGTEEGLK NCVRAKIDYK ALNKTLRDPV 

       370        380        390        400        410        420 
IYRCNLTPHH RTGSTWKIYP TYDFCVPIVD AIEGVTHALR TIEYRDRNAQ YDWMLQALRL 

       430        440        450        460        470        480 
RKVHIWDFAR INFVRTLLSK RKLQWMVDKD LVGNWDDPRF PTVRGVRRRG MTVEGLRNFV 

       490        500        510        520        530        540 
LSQGPSRNVI NLEWNLIWAF NKKVIDPIAP RHTAIVNPVK IHLEGSEAPQ EPKIEMKPKH 

       550        560        570        580        590        600 
KKNPAVGEKK VIYYKDIVVD KDDADVINVD EEVTLMDWGN VIITKKNDDG SMVAKLNLEG 

       610        620        630        640        650        660 
DFKKTKHKLT WLADTKDVVP VDLVDFDHLI TKDRLEEDES FEDFLTPQTE FHTDAIADLN 

       670        680        690        700 
VKDMKIGDII QFERKGYYRL DALPKDGKPY VFFTIPDGKS VNKYGAKK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and sequence characterization of the gene encoding the yeast cytosolic glutamyl-tRNA synthetase."
Frantz J.D., Gilbert W.
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The sequence of an 11.1 kb DNA fragment between ADH4 and ADE5 on the left arm of chromosome VII, reveals the presence of eight open reading frames."
Vandenbol M., Durand P., Portetelle D., Hilger F.
Yeast 11:1519-1523(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"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. expand/collapse author list , 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.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Sequence of a 39,411 bp DNA fragment covering the left end of chromosome VII of Saccharomyces cerevisiae."
Coissac E., Maillier E., Robineau S., Netter P.
Yeast 12:1555-1562(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129.
Strain: ATCC 96604 / S288c / FY1679.
[6]"Sequencing and comparison of yeast species to identify genes and regulatory elements."
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[7]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"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].
[9]"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 THR-300, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA-aminoacylation and nuclear-export cofactor Arc1p reveal a novel function for an old fold."
Simader H., Hothorn M., Suck D.
Acta Crystallogr. D 62:1510-1519(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-191, INTERACTION WITH ARC1.
[12]"Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes."
Simader H., Hothorn M., Koehler C., Basquin J., Simos G., Suck D.
Nucleic Acids Res. 34:3968-3979(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-191, INTERACTION WITH ARC1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U32265 Genomic DNA. Translation: AAA78905.1. Sequence problems.
Z49149 Genomic DNA. Translation: CAA89009.1. Different initiation.
Z72767 Genomic DNA. Translation: CAA96964.1. Different initiation.
X94357 Genomic DNA. Translation: CAA64142.1. Different initiation.
BK006941 Genomic DNA. Translation: DAA07874.1.
PIRS53934.
RefSeqNP_011269.2. NM_001181111.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HRAX-ray1.90A/B1-191[»]
2HRKX-ray2.05A1-191[»]
2HSMX-ray3.00A1-191[»]
ProteinModelPortalP46655.
SMRP46655. Positions 1-180, 193-692.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32995. 113 interactions.
DIPDIP-2212N.
IntActP46655. 25 interactions.
MINTMINT-491904.
STRING4932.YGL245W.

Proteomic databases

PaxDbP46655.
PeptideAtlasP46655.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL245W; YGL245W; YGL245W.
GeneID852606.
KEGGsce:YGL245W.

Organism-specific databases

CYGDYGL245w.
SGDS000003214. GUS1.

Phylogenomic databases

eggNOGCOG0008.
GeneTreeENSGT00550000074815.
HOGENOMHOG000259234.
KOK01885.
OMAFARMNFI.
OrthoDBEOG7MKWFN.

Enzyme and pathway databases

BioCycYEAST:G3O-30716-MONOMER.
BRENDA6.1.1.17. 984.
SABIO-RKP46655.

Gene expression databases

GenevestigatorP46655.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
1.20.1050.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR010987. Glutathione-S-Trfase_C-like.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF50715. SSF50715. 1 hit.
TIGRFAMsTIGR00463. gltX_arch. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP46655.
NextBio971793.

Entry information

Entry nameSYEC_YEAST
AccessionPrimary (citable) accession number: P46655
Secondary accession number(s): D6VV90
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 5, 2006
Last modified: April 16, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries