Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutamate--tRNA ligase, cytoplasmic

Gene

GUS1

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 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). In mitochondria, constitutes the nondiscriminating glutamyl-tRNA synthase that generates the mitochondrial mischarged glutamyl-tRNA(Gln) substrate for the tRNA-dependent amidotransferase (AdT), which generates mitochondrial glutaminyl-tRNA(Gln) by transamidation of glutamyl-tRNA(Gln).2 Publications

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei215ATPBy similarity1
Binding sitei241GlutamateBy similarity1
Binding sitei400GlutamateBy similarity1
Binding sitei403ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi437 – 441ATPBy similarity5

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • glutamate-tRNA ligase activity Source: SGD
  • glutamine-tRNA ligase activity Source: GO_Central

GO - Biological processi

  • glutaminyl-tRNA aminoacylation Source: GO_Central
  • 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

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:
(c)ERS
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
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL245W.
SGDiS000003214. GUS1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytoplasmic stress granule Source: SGD
  • cytosol Source: GO_Central
  • methionyl glutamyl tRNA synthetase complex Source: SGD
  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi148R → A: Abolishes interaction with ARC1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001197391 – 708Glutamate--tRNA ligase, cytoplasmicAdd BLAST708

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei300PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP46655.
PRIDEiP46655.

PTM databases

iPTMnetiP46655.

Interactioni

Subunit structurei

Component of a yeast aminoacyl-tRNA synthase (aaRS) complex formed by methionyl-tRNA synthase MES1, glutamyl-tRNA synthase GUS1 and the tRNA aminoacylation cofactor ARC1 in a stoichiometric complex. Interacts (via N-ter) with ARC1 (via N-ter). Can also form a stable binary complex with ARC1 that is functional in terms of aminoacylation. ARC1 increases the affinity for cognate tRNAs due to the presence of a tRNA binding domain in the middle and C-terminal part of ARC1.5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi32995. 117 interactors.
DIPiDIP-2212N.
IntActiP46655. 25 interactors.
MINTiMINT-491904.

Structurei

Secondary structure

1708
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Helixi16 – 28Combined sources13
Beta strandi32 – 38Combined sources7
Beta strandi41 – 43Combined sources3
Beta strandi45 – 48Combined sources4
Helixi55 – 62Combined sources8
Turni63 – 66Combined sources4
Helixi72 – 84Combined sources13
Turni85 – 87Combined sources3
Helixi91 – 104Combined sources14
Turni105 – 107Combined sources3
Helixi119 – 130Combined sources12
Helixi134 – 140Combined sources7
Helixi144 – 154Combined sources11
Helixi157 – 160Combined sources4
Helixi162 – 177Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HRAX-ray1.90A/B1-191[»]
2HRKX-ray2.05A1-191[»]
2HSMX-ray3.00A1-191[»]
ProteinModelPortaliP46655.
SMRiP46655.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46655.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni106 – 115Interaction with ARC110
Regioni141 – 157Interaction with ARC1Add BLAST17
Regioni205 – 207Glutamate bindingBy similarity3
Regioni382 – 386Glutamate bindingBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi210 – 219"HIGH" region10
Motifi437 – 441"KMSKS" region5

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000259234.
InParanoidiP46655.
KOiK01885.
OMAiDYFDYLY.
OrthoDBiEOG092C0OTH.

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]
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

        10         20         30         40         50
MPSTLTINGK APIVAYAELI AARIVNALAP NSIAIKLVDD KKAPAAKLDD
60 70 80 90 100
ATEDVFNKIT SKFAAIFDNG DKEQVAKWVN LAQKELVIKN FAKLSQSLET
110 120 130 140 150
LDSQLNLRTF ILGGLKYSAA DVACWGALRS NGMCGSIIKN KVDVNVSRWY
160 170 180 190 200
TLLEMDPIFG EAHDFLSKSL LELKKSANVG KKKETHKANF EIDLPDAKMG
210 220 230 240 250
EVVTRFPPEP SGYLHIGHAK AALLNQYFAQ AYKGKLIIRF DDTNPSKEKE
260 270 280 290 300
EFQDSILEDL DLLGIKGDRI TYSSDYFQEM YDYCVQMIKD GKAYCDDTPT
310 320 330 340 350
EKMREERMDG VASARRDRSV EENLRIFTEE MKNGTEEGLK NCVRAKIDYK
360 370 380 390 400
ALNKTLRDPV IYRCNLTPHH RTGSTWKIYP TYDFCVPIVD AIEGVTHALR
410 420 430 440 450
TIEYRDRNAQ YDWMLQALRL RKVHIWDFAR INFVRTLLSK RKLQWMVDKD
460 470 480 490 500
LVGNWDDPRF PTVRGVRRRG MTVEGLRNFV LSQGPSRNVI NLEWNLIWAF
510 520 530 540 550
NKKVIDPIAP RHTAIVNPVK IHLEGSEAPQ EPKIEMKPKH KKNPAVGEKK
560 570 580 590 600
VIYYKDIVVD KDDADVINVD EEVTLMDWGN VIITKKNDDG SMVAKLNLEG
610 620 630 640 650
DFKKTKHKLT WLADTKDVVP VDLVDFDHLI TKDRLEEDES FEDFLTPQTE
660 670 680 690 700
FHTDAIADLN VKDMKIGDII QFERKGYYRL DALPKDGKPY VFFTIPDGKS

VNKYGAKK
Length:708
Mass (Da):80,843
Last modified:September 5, 2006 - v3
Checksum:iEADAD430A2D98974
GO

Sequence cautioni

The sequence AAA78905 differs from that shown. Reason: Frameshift at position 698.Curated
The sequence AAA78905 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA64142 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA89009 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA96964 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti209E → D in AAA78905 (Ref. 1) Curated1
Sequence conflicti473V → A in AAA78905 (Ref. 1) Curated1
Sequence conflicti510P → S in AAA78905 (Ref. 1) Curated1
Sequence conflicti546V → M in AAA78905 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HRAX-ray1.90A/B1-191[»]
2HRKX-ray2.05A1-191[»]
2HSMX-ray3.00A1-191[»]
ProteinModelPortaliP46655.
SMRiP46655.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32995. 117 interactors.
DIPiDIP-2212N.
IntActiP46655. 25 interactors.
MINTiMINT-491904.

PTM databases

iPTMnetiP46655.

Proteomic databases

MaxQBiP46655.
PRIDEiP46655.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YGL245W.
SGDiS000003214. GUS1.

Phylogenomic databases

HOGENOMiHOG000259234.
InParanoidiP46655.
KOiK01885.
OMAiDYFDYLY.
OrthoDBiEOG092C0OTH.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP46655.
PROiP46655.

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]
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 157 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.1 Publication

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

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.