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Q05506

- SYRC_YEAST

UniProt

Q05506 - SYRC_YEAST

Protein

Arginine--tRNA ligase, cytoplasmic

Gene

YDR341C

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis.By similarity

    Catalytic activityi

    ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).

    GO - Molecular functioni

    1. arginine-tRNA ligase activity Source: SGD
    2. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. arginyl-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-29896-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine--tRNA ligase, cytoplasmic (EC:6.1.1.19)
    Alternative name(s):
    Arginyl-tRNA synthetase
    Short name:
    ArgRS
    Gene namesi
    Ordered Locus Names:YDR341C
    ORF Names:D9651.10
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR341c.
    SGDiS000002749. YDR341C.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 607606Arginine--tRNA ligase, cytoplasmicPRO_0000151664Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei15 – 151Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ05506.
    PaxDbiQ05506.
    PeptideAtlasiQ05506.

    Expressioni

    Gene expression databases

    GenevestigatoriQ05506.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi32398. 55 interactions.
    DIPiDIP-5046N.
    IntActiQ05506. 1 interaction.
    MINTiMINT-482020.
    STRINGi4932.YDR341C.

    Structurei

    Secondary structure

    1
    607
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1311
    Helixi19 – 224
    Turni27 – 293
    Helixi31 – 4717
    Helixi51 – 544
    Helixi55 – 573
    Helixi64 – 663
    Beta strandi68 – 725
    Helixi73 – 764
    Helixi83 – 9210
    Turni97 – 993
    Beta strandi100 – 1067
    Beta strandi109 – 1146
    Helixi116 – 13015
    Helixi131 – 1333
    Beta strandi144 – 1485
    Helixi160 – 1623
    Helixi163 – 17816
    Beta strandi182 – 1909
    Helixi194 – 20613
    Helixi209 – 2146
    Helixi216 – 23318
    Beta strandi235 – 2384
    Turni240 – 2423
    Beta strandi243 – 2453
    Helixi246 – 25712
    Helixi260 – 28324
    Beta strandi289 – 2935
    Helixi294 – 2963
    Helixi299 – 31113
    Beta strandi315 – 3184
    Beta strandi321 – 3255
    Helixi326 – 3283
    Turni331 – 3333
    Beta strandi335 – 3395
    Turni341 – 3433
    Helixi347 – 36216
    Beta strandi365 – 3706
    Helixi373 – 3753
    Helixi376 – 38813
    Helixi392 – 3965
    Beta strandi397 – 4004
    Beta strandi405 – 4073
    Turni410 – 4134
    Helixi418 – 43417
    Helixi437 – 4404
    Helixi446 – 46318
    Helixi475 – 4795
    Beta strandi482 – 4854
    Helixi486 – 50217
    Turni503 – 5053
    Helixi508 – 5114
    Helixi516 – 5183
    Helixi522 – 53110
    Helixi534 – 54411
    Helixi547 – 56721
    Helixi575 – 59925

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BS2X-ray2.75A1-607[»]
    1F7UX-ray2.20A1-607[»]
    1F7VX-ray2.90A1-607[»]
    ProteinModelPortaliQ05506.
    SMRiQ05506. Positions 2-607.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ05506.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi151 – 16212"HIGH" regionAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0018.
    GeneTreeiENSGT00530000063407.
    HOGENOMiHOG000247211.
    KOiK01887.
    OMAiCEDRGAL.
    OrthoDBiEOG7NKKV8.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPiMF_00123. Arg_tRNA_synth.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR001278. Arg-tRNA-ligase.
    IPR005148. Arg-tRNA-synth_N.
    IPR008909. DALR_anticod-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view]
    PANTHERiPTHR11956. PTHR11956. 1 hit.
    PfamiPF03485. Arg_tRNA_synt_N. 1 hit.
    PF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 1 hit.
    [Graphical view]
    PRINTSiPR01038. TRNASYNTHARG.
    SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
    SM00836. DALR_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF55190. SSF55190. 1 hit.
    TIGRFAMsiTIGR00456. argS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q05506-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASTANMISQ LKKLSIAEPA VAKDSHPDVN IVDLMRNYIS QELSKISGVD    50
    SSLIFPALEW TNTMERGDLL IPIPRLRIKG ANPKDLAVQW AEKFPCGDFL 100
    EKVEANGPFI QFFFNPQFLA KLVIPDILTR KEDYGSCKLV ENKKVIIEFS 150
    SPNIAKPFHA GHLRSTIIGG FLANLYEKLG WEVIRMNYLG DWGKQFGLLA 200
    VGFERYGNEE ALVKDPIHHL FDVYVRINKD IEEEGDSIPL EQSTNGKARE 250
    YFKRMEDGDE EALKIWKRFR EFSIEKYIDT YARLNIKYDV YSGESQVSKE 300
    SMLKAIDLFK EKGLTHEDKG AVLIDLTKFN KKLGKAIVQK SDGTTLYLTR 350
    DVGAAMDRYE KYHFDKMIYV IASQQDLHAA QFFEILKQMG FEWAKDLQHV 400
    NFGMVQGMST RKGTVVFLDN ILEETKEKMH EVMKKNENKY AQIEHPEEVA 450
    DLVGISAVMI QDMQGKRINN YEFKWERMLS FEGDTGPYLQ YAHSRLRSVE 500
    RNASGITQEK WINADFSLLK EPAAKLLIRL LGQYPDVLRN AIKTHEPTTV 550
    VTYLFKLTHQ VSSCYDVLWV AGQTEELATA RLALYGAARQ VLYNGMRLLG 600
    LTPVERM 607
    Length:607
    Mass (Da):69,525
    Last modified:November 1, 1996 - v1
    Checksum:i8349ABC0E30E50F1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51032 Genomic DNA. Translation: AAB64777.1.
    BK006938 Genomic DNA. Translation: DAA12182.1.
    PIRiS70106.
    RefSeqiNP_010628.3. NM_001180649.3.

    Genome annotation databases

    EnsemblFungiiYDR341C; YDR341C; YDR341C.
    GeneIDi851942.
    KEGGisce:YDR341C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51032 Genomic DNA. Translation: AAB64777.1 .
    BK006938 Genomic DNA. Translation: DAA12182.1 .
    PIRi S70106.
    RefSeqi NP_010628.3. NM_001180649.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BS2 X-ray 2.75 A 1-607 [» ]
    1F7U X-ray 2.20 A 1-607 [» ]
    1F7V X-ray 2.90 A 1-607 [» ]
    ProteinModelPortali Q05506.
    SMRi Q05506. Positions 2-607.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32398. 55 interactions.
    DIPi DIP-5046N.
    IntActi Q05506. 1 interaction.
    MINTi MINT-482020.
    STRINGi 4932.YDR341C.

    Proteomic databases

    MaxQBi Q05506.
    PaxDbi Q05506.
    PeptideAtlasi Q05506.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR341C ; YDR341C ; YDR341C .
    GeneIDi 851942.
    KEGGi sce:YDR341C.

    Organism-specific databases

    CYGDi YDR341c.
    SGDi S000002749. YDR341C.

    Phylogenomic databases

    eggNOGi COG0018.
    GeneTreei ENSGT00530000063407.
    HOGENOMi HOG000247211.
    KOi K01887.
    OMAi CEDRGAL.
    OrthoDBi EOG7NKKV8.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29896-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q05506.
    NextBioi 970021.
    PROi Q05506.

    Gene expression databases

    Genevestigatori Q05506.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPi MF_00123. Arg_tRNA_synth.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR001278. Arg-tRNA-ligase.
    IPR005148. Arg-tRNA-synth_N.
    IPR008909. DALR_anticod-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view ]
    PANTHERi PTHR11956. PTHR11956. 1 hit.
    Pfami PF03485. Arg_tRNA_synt_N. 1 hit.
    PF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 1 hit.
    [Graphical view ]
    PRINTSi PR01038. TRNASYNTHARG.
    SMARTi SM01016. Arg_tRNA_synt_N. 1 hit.
    SM00836. DALR_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47323. SSF47323. 1 hit.
    SSF55190. SSF55190. 1 hit.
    TIGRFAMsi TIGR00456. argS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    4. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    5. "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 SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. "L-arginine recognition by yeast arginyl-tRNA synthetase."
      Cavarelli J., Delagoutte B., Eriani G., Gangloff J., Moras D.
      EMBO J. 17:5438-5448(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).

    Entry informationi

    Entry nameiSYRC_YEAST
    AccessioniPrimary (citable) accession number: Q05506
    Secondary accession number(s): D6VSX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 137 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 20600 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3