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P46655

- SYEC_YEAST

UniProt

P46655 - SYEC_YEAST

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Protein
Glutamate--tRNA ligase, cytoplasmic
Gene
GUS1, YGL245W, G0583, HRB724
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei215 – 2151ATP By similarity
Binding sitei241 – 2411Glutamate By similarity
Binding sitei400 – 4001Glutamate By similarity
Binding sitei403 – 4031ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi437 – 4415ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. RNA binding Source: UniProtKB-KW
  3. glutamate-tRNA ligase activity Source: SGD
  4. protein binding Source: IntAct

GO - Biological processi

  1. glutamyl-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, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30716-MONOMER.
BRENDAi6.1.1.17. 984.
SABIO-RKP46655.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase, cytoplasmic (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
P85
Gene namesi
Name:GUS1
Ordered Locus Names:YGL245W
ORF Names:G0583, HRB724
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL245w.
SGDiS000003214. GUS1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. methionyl glutamyl tRNA synthetase complex Source: SGD
  3. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 708708Glutamate--tRNA ligase, cytoplasmic
PRO_0000119739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei300 – 3001Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP46655.
PaxDbiP46655.
PeptideAtlasiP46655.

Expressioni

Gene expression databases

GenevestigatoriP46655.

Interactioni

Subunit structurei

Interacts with ARC1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARC1P466727EBI-18665,EBI-7224

Protein-protein interaction databases

BioGridi32995. 113 interactions.
DIPiDIP-2212N.
IntActiP46655. 25 interactions.
MINTiMINT-491904.
STRINGi4932.YGL245W.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86
Helixi16 – 2813
Beta strandi32 – 387
Beta strandi41 – 433
Beta strandi45 – 484
Helixi55 – 628
Turni63 – 664
Helixi72 – 8413
Turni85 – 873
Helixi91 – 10414
Turni105 – 1073
Helixi119 – 13012
Helixi134 – 1407
Helixi144 – 15411
Helixi157 – 1604
Helixi162 – 17716

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HRAX-ray1.90A/B1-191[»]
2HRKX-ray2.05A1-191[»]
2HSMX-ray3.00A1-191[»]
ProteinModelPortaliP46655.
SMRiP46655. Positions 1-180, 193-692.

Miscellaneous databases

EvolutionaryTraceiP46655.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni205 – 2073Glutamate binding By similarity
Regioni382 – 3865Glutamate binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi210 – 21910"HIGH" region
Motifi437 – 4415"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
GeneTreeiENSGT00550000074815.
HOGENOMiHOG000259234.
KOiK01885.
OMAiTDRNPQY.
OrthoDBiEOG7MKWFN.

Family and domain databases

Gene3Di1.10.1160.10. 1 hit.
1.20.1050.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
InterProiIPR001412. 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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF50715. SSF50715. 1 hit.
TIGRFAMsiTIGR00463. gltX_arch. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46655-1 [UniParc]FASTAAdd to Basket

« Hide

MPSTLTINGK APIVAYAELI AARIVNALAP NSIAIKLVDD KKAPAAKLDD    50
ATEDVFNKIT SKFAAIFDNG DKEQVAKWVN LAQKELVIKN FAKLSQSLET 100
LDSQLNLRTF ILGGLKYSAA DVACWGALRS NGMCGSIIKN KVDVNVSRWY 150
TLLEMDPIFG EAHDFLSKSL LELKKSANVG KKKETHKANF EIDLPDAKMG 200
EVVTRFPPEP SGYLHIGHAK AALLNQYFAQ AYKGKLIIRF DDTNPSKEKE 250
EFQDSILEDL DLLGIKGDRI TYSSDYFQEM YDYCVQMIKD GKAYCDDTPT 300
EKMREERMDG VASARRDRSV EENLRIFTEE MKNGTEEGLK NCVRAKIDYK 350
ALNKTLRDPV IYRCNLTPHH RTGSTWKIYP TYDFCVPIVD AIEGVTHALR 400
TIEYRDRNAQ YDWMLQALRL RKVHIWDFAR INFVRTLLSK RKLQWMVDKD 450
LVGNWDDPRF PTVRGVRRRG MTVEGLRNFV LSQGPSRNVI NLEWNLIWAF 500
NKKVIDPIAP RHTAIVNPVK IHLEGSEAPQ EPKIEMKPKH KKNPAVGEKK 550
VIYYKDIVVD KDDADVINVD EEVTLMDWGN VIITKKNDDG SMVAKLNLEG 600
DFKKTKHKLT WLADTKDVVP VDLVDFDHLI TKDRLEEDES FEDFLTPQTE 650
FHTDAIADLN VKDMKIGDII QFERKGYYRL DALPKDGKPY VFFTIPDGKS 700
VNKYGAKK 708
Length:708
Mass (Da):80,843
Last modified:September 5, 2006 - v3
Checksum:iEADAD430A2D98974
GO

Sequence cautioni

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091E → D in AAA78905. 1 Publication
Sequence conflicti473 – 4731V → A in AAA78905. 1 Publication
Sequence conflicti510 – 5101P → S in AAA78905. 1 Publication
Sequence conflicti546 – 5461V → M in AAA78905. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS53934.
RefSeqiNP_011269.2. NM_001181111.1.

Genome annotation databases

EnsemblFungiiYGL245W; YGL245W; YGL245W.
GeneIDi852606.
KEGGisce:YGL245W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S53934.
RefSeqi NP_011269.2. NM_001181111.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HRA X-ray 1.90 A/B 1-191 [» ]
2HRK X-ray 2.05 A 1-191 [» ]
2HSM X-ray 3.00 A 1-191 [» ]
ProteinModelPortali P46655.
SMRi P46655. Positions 1-180, 193-692.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32995. 113 interactions.
DIPi DIP-2212N.
IntActi P46655. 25 interactions.
MINTi MINT-491904.
STRINGi 4932.YGL245W.

Proteomic databases

MaxQBi P46655.
PaxDbi P46655.
PeptideAtlasi P46655.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL245W ; YGL245W ; YGL245W .
GeneIDi 852606.
KEGGi sce:YGL245W.

Organism-specific databases

CYGDi YGL245w.
SGDi S000003214. GUS1.

Phylogenomic databases

eggNOGi COG0008.
GeneTreei ENSGT00550000074815.
HOGENOMi HOG000259234.
KOi K01885.
OMAi TDRNPQY.
OrthoDBi EOG7MKWFN.

Enzyme and pathway databases

BioCyci YEAST:G3O-30716-MONOMER.
BRENDAi 6.1.1.17. 984.
SABIO-RK P46655.

Miscellaneous databases

EvolutionaryTracei P46655.
NextBioi 971793.

Gene expression databases

Genevestigatori P46655.

Family and domain databases

Gene3Di 1.10.1160.10. 1 hit.
1.20.1050.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
InterProi IPR001412. 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 ]
PANTHERi PTHR10119. PTHR10119. 1 hit.
Pfami PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view ]
PRINTSi PR00987. TRNASYNTHGLU.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF50715. SSF50715. 1 hit.
TIGRFAMsi TIGR00463. gltX_arch. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. 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. 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.

Entry informationi

Entry nameiSYEC_YEAST
AccessioniPrimary (citable) accession number: P46655
Secondary accession number(s): D6VV90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 5, 2006
Last modified: July 9, 2014
This is version 133 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 48700 molecules/cell in log phase SD medium.

Keywords - Technical termi

3D-structure, Complete proteome, 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

External Data

Dasty 3

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