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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

Present with 48700 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei215ATPBy similarity1
Binding sitei241GlutamateBy similarity1
Binding sitei400GlutamateBy similarity1
Binding sitei403ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi437 – 441ATPBy similarity5

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-30716-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.1.1.17 984

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GUS1
Ordered Locus Names:YGL245W
ORF Names:G0583, HRB724
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome VII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000003214 GUS1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi148R → A: Abolishes interaction with ARC1. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001197391 – 708Glutamate--tRNA ligase, cytoplasmicAdd BLAST708

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei300PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P46655

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P46655

PRoteomics IDEntifications database

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PRIDEi
P46655

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P46655

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
32995, 360 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1947 Methionyl glutamyl tRNA synthetase complex

Database of interacting proteins

More...
DIPi
DIP-2212N

Protein interaction database and analysis system

More...
IntActi
P46655, 46 interactors

Molecular INTeraction database

More...
MINTi
P46655

STRING: functional protein association networks

More...
STRINGi
4932.YGL245W

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1708
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P46655

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P46655

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P46655

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni106 – 115Interaction with ARC110
Regioni141 – 157Interaction with ARC1Add BLAST17
Regioni205 – 207Glutamate bindingBy similarity3
Regioni382 – 386Glutamate bindingBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi210 – 219"HIGH" region10
Motifi437 – 441"KMSKS" region5

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00550000074815

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000259234

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P46655

KEGG Orthology (KO)

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KOi
K01885

Identification of Orthologs from Complete Genome Data

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OMAi
MRFAPNP

Database of Orthologous Groups

More...
OrthoDBi
EOG092C0OTH

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.240.10, 2 hits
3.40.50.620, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_02076 Glu_tRNA_synth_type2, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001412 aa-tRNA-synth_I_CS
IPR004526 Glu-tRNA-synth_arc/euk
IPR000924 Glu/Gln-tRNA-synth
IPR020058 Glu/Gln-tRNA-synth_Ib_cat-dom
IPR020059 Glu/Gln-tRNA-synth_Ib_codon-bd
IPR036282 Glutathione-S-Trfase_C_sf
IPR020056 Rbsml_L25/Gln-tRNA_synth_N
IPR011035 Ribosomal_L25/Gln-tRNA_synth
IPR014729 Rossmann-like_a/b/a_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00749 tRNA-synt_1c, 1 hit
PF03950 tRNA-synt_1c_C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00987 TRNASYNTHGLU

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47616 SSF47616, 1 hit
SSF50715 SSF50715, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00463 gltX_arch, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00178 AA_TRNA_LIGASE_I, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iEADAD430A2D98974
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
S53934

NCBI Reference Sequences

More...
RefSeqi
NP_011269.2, NM_001181111.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGL245W_mRNA; YGL245W_mRNA; YGL245W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852606

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGL245W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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, 360 interactors
ComplexPortaliCPX-1947 Methionyl glutamyl tRNA synthetase complex
DIPiDIP-2212N
IntActiP46655, 46 interactors
MINTiP46655
STRINGi4932.YGL245W

PTM databases

iPTMnetiP46655

Proteomic databases

MaxQBiP46655
PaxDbiP46655
PRIDEiP46655

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL245W_mRNA; YGL245W_mRNA; YGL245W
GeneIDi852606
KEGGisce:YGL245W

Organism-specific databases

SGDiS000003214 GUS1

Phylogenomic databases

GeneTreeiENSGT00550000074815
HOGENOMiHOG000259234
InParanoidiP46655
KOiK01885
OMAiMRFAPNP
OrthoDBiEOG092C0OTH

Enzyme and pathway databases

BioCyciYEAST:G3O-30716-MONOMER
BRENDAi6.1.1.17 984

Miscellaneous databases

EvolutionaryTraceiP46655

Protein Ontology

More...
PROi
PR:P46655

Family and domain databases

Gene3Di2.40.240.10, 2 hits
3.40.50.620, 1 hit
HAMAPiMF_02076 Glu_tRNA_synth_type2, 1 hit
InterProiView protein in InterPro
IPR001412 aa-tRNA-synth_I_CS
IPR004526 Glu-tRNA-synth_arc/euk
IPR000924 Glu/Gln-tRNA-synth
IPR020058 Glu/Gln-tRNA-synth_Ib_cat-dom
IPR020059 Glu/Gln-tRNA-synth_Ib_codon-bd
IPR036282 Glutathione-S-Trfase_C_sf
IPR020056 Rbsml_L25/Gln-tRNA_synth_N
IPR011035 Ribosomal_L25/Gln-tRNA_synth
IPR014729 Rossmann-like_a/b/a_fold
PfamiView protein in Pfam
PF00749 tRNA-synt_1c, 1 hit
PF03950 tRNA-synt_1c_C, 1 hit
PRINTSiPR00987 TRNASYNTHGLU
SUPFAMiSSF47616 SSF47616, 1 hit
SSF50715 SSF50715, 1 hit
TIGRFAMsiTIGR00463 gltX_arch, 1 hit
PROSITEiView protein in PROSITE
PS00178 AA_TRNA_LIGASE_I, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSYEC_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P46655
Secondary accession number(s): D6VV90
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 5, 2006
Last modified: December 5, 2018
This is version 178 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
  5. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
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