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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   14-MAY-2014, entry version 136.
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 (By similarity).
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.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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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; 55.
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   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-SubCell.
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.
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   MOD_RES      15     15       Phosphoserine.
FT   HELIX         3     13
FT   HELIX        19     22
FT   TURN         27     29
FT   HELIX        31     47
FT   HELIX        51     54
FT   HELIX        55     57
FT   HELIX        64     66
FT   STRAND       68     72
FT   HELIX        73     76
FT   HELIX        83     92
FT   TURN         97     99
FT   STRAND      100    106
FT   STRAND      109    114
FT   HELIX       116    130
FT   HELIX       131    133
FT   STRAND      144    148
FT   HELIX       160    162
FT   HELIX       163    178
FT   STRAND      182    190
FT   HELIX       194    206
FT   HELIX       209    214
FT   HELIX       216    233
FT   STRAND      235    238
FT   TURN        240    242
FT   STRAND      243    245
FT   HELIX       246    257
FT   HELIX       260    283
FT   STRAND      289    293
FT   HELIX       294    296
FT   HELIX       299    311
FT   STRAND      315    318
FT   STRAND      321    325
FT   HELIX       326    328
FT   TURN        331    333
FT   STRAND      335    339
FT   TURN        341    343
FT   HELIX       347    362
FT   STRAND      365    370
FT   HELIX       373    375
FT   HELIX       376    388
FT   HELIX       392    396
FT   STRAND      397    400
FT   STRAND      405    407
FT   TURN        410    413
FT   HELIX       418    434
FT   HELIX       437    440
FT   HELIX       446    463
FT   HELIX       475    479
FT   STRAND      482    485
FT   HELIX       486    502
FT   TURN        503    505
FT   HELIX       508    511
FT   HELIX       516    518
FT   HELIX       522    531
FT   HELIX       534    544
FT   HELIX       547    567
FT   HELIX       575    599
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
//
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