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 03-AUG-2022, entry version 194.
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; Saccharomycetes;
OC 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., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Dephoure N.,
RA 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 BY
RP 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 BY
RP 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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP 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 insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8] {ECO:0007744|PDB:1BS2}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH L-ARGININE, AND
RP SUBUNIT.
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).
RN [9] {ECO:0007744|PDB:1F7U, ECO:0007744|PDB:1F7V}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH L-ARGININE AND RNA.
RX PubMed=11060012; DOI=10.1093/emboj/19.21.5599;
RA Delagoutte B., Moras D., Cavarelli J.;
RT "tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations
RT during substrates binding.";
RL EMBO J. 19:5599-5610(2000).
CC -!- FUNCTION: Forms part of a macromolecular complex that catalyzes the
CC attachment of specific amino acids to cognate tRNAs during protein
CC synthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC EC=6.1.1.19;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9736621}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54136}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54136}.
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 family.
CC {ECO:0000305}.
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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 AlphaFoldDB; Q05506; -.
DR SMR; Q05506; -.
DR BioGRID; 32398; 127.
DR DIP; DIP-5046N; -.
DR IntAct; Q05506; 4.
DR STRING; 4932.YDR341C; -.
DR iPTMnet; Q05506; -.
DR MaxQB; Q05506; -.
DR PaxDb; Q05506; -.
DR PRIDE; Q05506; -.
DR TopDownProteomics; Q05506; -.
DR EnsemblFungi; YDR341C_mRNA; YDR341C; YDR341C.
DR GeneID; 851942; -.
DR KEGG; sce:YDR341C; -.
DR SGD; S000002749; YDR341C.
DR VEuPathDB; FungiDB:YDR341C; -.
DR eggNOG; KOG1195; Eukaryota.
DR GeneTree; ENSGT00530000063407; -.
DR HOGENOM; CLU_006406_6_2_1; -.
DR InParanoid; Q05506; -.
DR OMA; YEFKWER; -.
DR BioCyc; YEAST:G3O-29896-MON; -.
DR BRENDA; 6.1.1.19; 984.
DR EvolutionaryTrace; Q05506; -.
DR PRO; PR:Q05506; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q05506; protein.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA: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:0032543; P:mitochondrial translation; IBA:GO_Central.
DR CDD; cd00671; ArgRS_core; 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; IPR036695; Arg-tRNA-synth_N_sf.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_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 Cytoplasm; Ligase; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..607
FT /note="Arginine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000151664"
FT REGION 59..60
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000269|PubMed:11060012"
FT REGION 106..111
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000269|PubMed:11060012"
FT REGION 484..498
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000269|PubMed:11060012"
FT MOTIF 151..162
FT /note="'HIGH' region"
FT BINDING 148..153
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:11060012,
FT ECO:0000269|PubMed:9736621, ECO:0007744|PDB:1BS2,
FT ECO:0007744|PDB:1F7U"
FT BINDING 162
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:9736621,
FT ECO:0007744|PDB:1BS2"
FT BINDING 347
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:11060012,
FT ECO:0000269|PubMed:9736621, ECO:0007744|PDB:1BS2,
FT ECO:0007744|PDB:1F7U"
FT BINDING 351
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:11060012,
FT ECO:0000269|PubMed:9736621, ECO:0007744|PDB:1BS2,
FT ECO:0007744|PDB:1F7U"
FT BINDING 375
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:11060012,
FT ECO:0000269|PubMed:9736621, ECO:0007744|PDB:1BS2,
FT ECO:0007744|PDB:1F7U"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:1F7U"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 31..47
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:1F7U"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 163..178
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 216..233
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:1BS2"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 260..283
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 299..311
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1F7U"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:1F7U"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:1BS2"
FT HELIX 347..362
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 392..396
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:1F7U"
FT TURN 410..413
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 418..434
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 437..440
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 446..463
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 475..479
FT /evidence="ECO:0007829|PDB:1F7U"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 486..502
FT /evidence="ECO:0007829|PDB:1F7U"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 508..511
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 522..531
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 534..544
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 547..567
FT /evidence="ECO:0007829|PDB:1F7U"
FT HELIX 575..599
FT /evidence="ECO:0007829|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
