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 03-APR-2013, entry version 126.
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 204511 / S288c / AB972;
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;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
RX PubMed=17563356; DOI=10.1073/pnas.0701622104;
RA Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
RT "Proteome-wide identification of in vivo targets of DNA damage
RT checkpoint kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS
RP SPECTROMETRY.
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 [7]
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 DIP; DIP-5046N; -.
DR IntAct; Q05506; 3.
DR MINT; MINT-482020; -.
DR STRING; 4932.YDR341C; -.
DR PaxDb; Q05506; -.
DR PeptideAtlas; Q05506; -.
DR EnsemblFungi; YDR341C; YDR341C; YDR341C.
DR GeneID; 851942; -.
DR KEGG; sce:YDR341C; -.
DR KEGG; sce:YDR346C; -.
DR CYGD; YDR341c; -.
DR SGD; S000002749; YDR341C.
DR eggNOG; COG0018; -.
DR GeneTree; ENSGT00530000063407; -.
DR HOGENOM; HOG000247211; -.
DR KO; K01887; -.
DR OMA; ETIRGCL; -.
DR OrthoDB; EOG4FR40V; -.
DR EvolutionaryTrace; Q05506; -.
DR NextBio; 970021; -.
DR Genevestigator; Q05506; -.
DR GermOnline; YDR341C; Saccharomyces cerevisiae.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
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 GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR Gene3D; 3.30.1360.70; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR001278; Arg-tRNA-ligase_Ia.
DR InterPro; IPR015945; Arg-tRNA-synth_Ia_core.
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; SSF55190; Arg-tRNA-synth_Ic_N; 1.
DR SUPFAM; SSF47323; tRNAsyn_1a_bind; 1.
DR TIGRFAMs; TIGR00456; argS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding;
KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1 607 Arginine--tRNA ligase, cytoplasmic.
FT /FTId=PRO_0000151664.
FT MOTIF 151 162 "HIGH" region.
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
//
