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P46655

- SYEC_YEAST

UniProt

P46655 - SYEC_YEAST

Protein

Glutamate--tRNA ligase, cytoplasmic

Gene

GUS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 3 (05 Sep 2006)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei215 – 2151ATPBy similarity
    Binding sitei241 – 2411GlutamateBy similarity
    Binding sitei400 – 4001GlutamateBy similarity
    Binding sitei403 – 4031ATPBy similarity

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. glutamyl-tRNA aminoacylation Source: SGD

    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
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGL245w.
    SGDiS000003214. GUS1.

    Subcellular locationi

    Cytoplasm. Mitochondrion
    Note: Largely excluded from the nucleus.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi148 – 1481R → A: Abolishes interaction with ARC1. 1 Publication

    PTM / Processingi

    Molecule processing

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

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

    Structurei

    Secondary structure

    1
    708
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46655.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni106 – 11510Interaction with ARC1
    Regioni141 – 15717Interaction with ARC1Add
    BLAST
    Regioni205 – 2073Glutamate bindingBy similarity
    Regioni382 – 3865Glutamate bindingBy 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 AAA78905.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAA64142.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAA89009.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAA96964.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

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

    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

    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. "The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases."
      Simos G., Segref A., Fasiolo F., Hellmuth K., Shevshenko A., Mann M., Hurt E.C.
      EMBO J. 15:5437-5448(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARC1.
    7. "A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases."
      Simos G., Sauer A., Fasiolo F., Hurt E.C.
      Mol. Cell 1:235-242(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARC1.
    8. "The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p."
      Galani K., Grosshans H., Deinert K., Hurt E.C., Simos G.
      EMBO J. 20:6889-6898(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH ARC1, SUBCELLULAR LOCATION.
    9. "Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs."
      Deinert K., Fasiolo F., Hurt E.C., Simos G.
      J. Biol. Chem. 276:6000-6008(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    10. "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.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. "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].
    14. "Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS."
      Frechin M., Senger B., Braye M., Kern D., Martin R.P., Becker H.D.
      Genes Dev. 23:1119-1130(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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.
    17. "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 IN COMPLEX WITH ARC1, MUTAGENESIS OF ARG-148.

    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: October 1, 2014
    This is version 134 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

    External Data

    Dasty 3