GenomeNet

Database: UniProt/SWISS-PROT
Entry: SYRC_YEAST
LinkDB: SYRC_YEAST
Original site: SYRC_YEAST 
ID   SYRC_YEAST              Reviewed;         607 AA.
AC   Q05506; D6VSX2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   26-NOV-2014, entry version 139.
DE   RecName: Full=Arginine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   OrderedLocusNames=YDR341C; ORFNames=D9651.10;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
RX   PubMed=9736621; DOI=10.1093/emboj/17.18.5438;
RA   Cavarelli J., Delagoutte B., Eriani G., Gangloff J., Moras D.;
RT   "L-arginine recognition by yeast arginyl-tRNA synthetase.";
RL   EMBO J. 17:5438-5448(1998).
CC   -!- FUNCTION: Forms part of a macromolecular complex that catalyzes
CC       the attachment of specific amino acids to cognate tRNAs during
CC       protein synthesis. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP +
CC       diphosphate + L-arginyl-tRNA(Arg).
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 20600 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U51032; AAB64777.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12182.1; -; Genomic_DNA.
DR   PIR; S70106; S70106.
DR   RefSeq; NP_010628.3; NM_001180649.3.
DR   PDB; 1BS2; X-ray; 2.75 A; A=1-607.
DR   PDB; 1F7U; X-ray; 2.20 A; A=1-607.
DR   PDB; 1F7V; X-ray; 2.90 A; A=1-607.
DR   PDBsum; 1BS2; -.
DR   PDBsum; 1F7U; -.
DR   PDBsum; 1F7V; -.
DR   ProteinModelPortal; Q05506; -.
DR   SMR; Q05506; 2-607.
DR   BioGrid; 32398; 56.
DR   DIP; DIP-5046N; -.
DR   IntAct; Q05506; 1.
DR   MINT; MINT-482020; -.
DR   STRING; 4932.YDR341C; -.
DR   MaxQB; Q05506; -.
DR   PaxDb; Q05506; -.
DR   PeptideAtlas; Q05506; -.
DR   EnsemblFungi; YDR341C; YDR341C; YDR341C.
DR   GeneID; 851942; -.
DR   KEGG; sce:YDR341C; -.
DR   CYGD; YDR341c; -.
DR   SGD; S000002749; YDR341C.
DR   eggNOG; COG0018; -.
DR   GeneTree; ENSGT00530000063407; -.
DR   HOGENOM; HOG000247211; -.
DR   InParanoid; Q05506; -.
DR   KO; K01887; -.
DR   OMA; CEDRGAL; -.
DR   OrthoDB; EOG7NKKV8; -.
DR   BioCyc; YEAST:G3O-29896-MONOMER; -.
DR   EvolutionaryTrace; Q05506; -.
DR   NextBio; 970021; -.
DR   PRO; PR:Q05506; -.
DR   Genevestigator; Q05506; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IDA:SGD.
DR   Gene3D; 1.10.730.10; -; 1.
DR   Gene3D; 3.30.1360.70; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
DR   InterPro; IPR005148; Arg-tRNA-synth_N.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR   PANTHER; PTHR11956; PTHR11956; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM01016; Arg_tRNA_synt_N; 1.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF55190; SSF55190; 1.
DR   TIGRFAMs; TIGR00456; argS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW   Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:22814378}.
FT   CHAIN         2    607       Arginine--tRNA ligase, cytoplasmic.
FT                                /FTId=PRO_0000151664.
FT   MOTIF       151    162       "HIGH" region.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000269|PubMed:22814378}.
FT   MOD_RES      15     15       Phosphoserine.
FT                                {ECO:0000269|PubMed:17330950,
FT                                ECO:0000269|PubMed:18407956,
FT                                ECO:0000269|PubMed:19779198}.
FT   HELIX         3     13       {ECO:0000244|PDB:1F7U}.
FT   HELIX        19     22       {ECO:0000244|PDB:1F7U}.
FT   TURN         27     29       {ECO:0000244|PDB:1F7U}.
FT   HELIX        31     47       {ECO:0000244|PDB:1F7U}.
FT   HELIX        51     54       {ECO:0000244|PDB:1F7U}.
FT   HELIX        55     57       {ECO:0000244|PDB:1F7U}.
FT   HELIX        64     66       {ECO:0000244|PDB:1F7U}.
FT   STRAND       68     72       {ECO:0000244|PDB:1F7U}.
FT   HELIX        73     76       {ECO:0000244|PDB:1F7U}.
FT   HELIX        83     92       {ECO:0000244|PDB:1F7U}.
FT   TURN         97     99       {ECO:0000244|PDB:1F7U}.
FT   STRAND      100    106       {ECO:0000244|PDB:1F7U}.
FT   STRAND      109    114       {ECO:0000244|PDB:1F7U}.
FT   HELIX       116    130       {ECO:0000244|PDB:1F7U}.
FT   HELIX       131    133       {ECO:0000244|PDB:1F7U}.
FT   STRAND      144    148       {ECO:0000244|PDB:1F7U}.
FT   HELIX       160    162       {ECO:0000244|PDB:1F7U}.
FT   HELIX       163    178       {ECO:0000244|PDB:1F7U}.
FT   STRAND      182    190       {ECO:0000244|PDB:1F7U}.
FT   HELIX       194    206       {ECO:0000244|PDB:1F7U}.
FT   HELIX       209    214       {ECO:0000244|PDB:1F7U}.
FT   HELIX       216    233       {ECO:0000244|PDB:1F7U}.
FT   STRAND      235    238       {ECO:0000244|PDB:1BS2}.
FT   TURN        240    242       {ECO:0000244|PDB:1F7U}.
FT   STRAND      243    245       {ECO:0000244|PDB:1F7U}.
FT   HELIX       246    257       {ECO:0000244|PDB:1F7U}.
FT   HELIX       260    283       {ECO:0000244|PDB:1F7U}.
FT   STRAND      289    293       {ECO:0000244|PDB:1F7U}.
FT   HELIX       294    296       {ECO:0000244|PDB:1F7U}.
FT   HELIX       299    311       {ECO:0000244|PDB:1F7U}.
FT   STRAND      315    318       {ECO:0000244|PDB:1F7U}.
FT   STRAND      321    325       {ECO:0000244|PDB:1F7U}.
FT   HELIX       326    328       {ECO:0000244|PDB:1F7U}.
FT   TURN        331    333       {ECO:0000244|PDB:1F7U}.
FT   STRAND      335    339       {ECO:0000244|PDB:1F7U}.
FT   TURN        341    343       {ECO:0000244|PDB:1BS2}.
FT   HELIX       347    362       {ECO:0000244|PDB:1F7U}.
FT   STRAND      365    370       {ECO:0000244|PDB:1F7U}.
FT   HELIX       373    375       {ECO:0000244|PDB:1F7U}.
FT   HELIX       376    388       {ECO:0000244|PDB:1F7U}.
FT   HELIX       392    396       {ECO:0000244|PDB:1F7U}.
FT   STRAND      397    400       {ECO:0000244|PDB:1F7U}.
FT   STRAND      405    407       {ECO:0000244|PDB:1F7U}.
FT   TURN        410    413       {ECO:0000244|PDB:1F7U}.
FT   HELIX       418    434       {ECO:0000244|PDB:1F7U}.
FT   HELIX       437    440       {ECO:0000244|PDB:1F7U}.
FT   HELIX       446    463       {ECO:0000244|PDB:1F7U}.
FT   HELIX       475    479       {ECO:0000244|PDB:1F7U}.
FT   STRAND      482    485       {ECO:0000244|PDB:1F7U}.
FT   HELIX       486    502       {ECO:0000244|PDB:1F7U}.
FT   TURN        503    505       {ECO:0000244|PDB:1F7U}.
FT   HELIX       508    511       {ECO:0000244|PDB:1F7U}.
FT   HELIX       516    518       {ECO:0000244|PDB:1F7U}.
FT   HELIX       522    531       {ECO:0000244|PDB:1F7U}.
FT   HELIX       534    544       {ECO:0000244|PDB:1F7U}.
FT   HELIX       547    567       {ECO:0000244|PDB:1F7U}.
FT   HELIX       575    599       {ECO:0000244|PDB:1F7U}.
SQ   SEQUENCE   607 AA;  69525 MW;  8349ABC0E30E50F1 CRC64;
     MASTANMISQ LKKLSIAEPA VAKDSHPDVN IVDLMRNYIS QELSKISGVD SSLIFPALEW
     TNTMERGDLL IPIPRLRIKG ANPKDLAVQW AEKFPCGDFL EKVEANGPFI QFFFNPQFLA
     KLVIPDILTR KEDYGSCKLV ENKKVIIEFS SPNIAKPFHA GHLRSTIIGG FLANLYEKLG
     WEVIRMNYLG DWGKQFGLLA VGFERYGNEE ALVKDPIHHL FDVYVRINKD IEEEGDSIPL
     EQSTNGKARE YFKRMEDGDE EALKIWKRFR EFSIEKYIDT YARLNIKYDV YSGESQVSKE
     SMLKAIDLFK EKGLTHEDKG AVLIDLTKFN KKLGKAIVQK SDGTTLYLTR DVGAAMDRYE
     KYHFDKMIYV IASQQDLHAA QFFEILKQMG FEWAKDLQHV NFGMVQGMST RKGTVVFLDN
     ILEETKEKMH EVMKKNENKY AQIEHPEEVA DLVGISAVMI QDMQGKRINN YEFKWERMLS
     FEGDTGPYLQ YAHSRLRSVE RNASGITQEK WINADFSLLK EPAAKLLIRL LGQYPDVLRN
     AIKTHEPTTV VTYLFKLTHQ VSSCYDVLWV AGQTEELATA RLALYGAARQ VLYNGMRLLG
     LTPVERM
//
DBGET integrated database retrieval system