ID   SYR_BORBU               Reviewed;         585 AA.
AC   O51540;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   25-MAY-2022, entry version 133.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   Name=argS; OrderedLocusNames=BB_0594;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000783; AAC66956.2; -; Genomic_DNA.
DR   PIR; A70174; A70174.
DR   RefSeq; NP_212728.2; NC_001318.1.
DR   RefSeq; WP_010889774.1; NC_001318.1.
DR   AlphaFoldDB; O51540; -.
DR   SMR; O51540; -.
DR   STRING; 224326.BB_0594; -.
DR   PRIDE; O51540; -.
DR   EnsemblBacteria; AAC66956; AAC66956; BB_0594.
DR   KEGG; bbu:BB_0594; -.
DR   PATRIC; fig|224326.49.peg.985; -.
DR   HOGENOM; CLU_006406_6_1_12; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:CAFA.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..585
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151534"
FT   MOTIF           127..137
FT                   /note="'HIGH' region"
SQ   SEQUENCE   585 AA;  66852 MW;  B3E59137BDE34656 CRC64;
     MNKSVKKKIK DEINVIVTNL ALSNNIKLDN ININIQKPPK SDLGDISILM FEIGKTLKLP
     IEIISEEIIK NLKTKYEIKA VGPYLNIKIS RKEYINNTIQ MVNTQKDTYG TSKYLDNKKI
     ILEFSSPNTN KPLHVGHLRN DVIGESLSRI LKAVGAKITK INLINDRGVH ICKSMLAYKK
     FGNGITPEKA FKKGDHLIGD FYVKYNKYSQ ENENAEKEIQ DLLLLWEQKD VSTIELWKKL
     NKWAIEGIKE TYEITNTSFD KIYLESEIFK IGKNVVLEGL EKGFCYKRED GAICIDLPSD
     SDEKADTKVK QKVLIRSNGT SIYLTQDLGN IAVRTKEFNF EEMIYVVGSE QIQHFKSLFF
     VAEKLGLSKN KKLIHLSHGM VNLVDGKMKS REGNVIDADN LISNLIELII PEMTQKIENK
     ESAKKNALNI ALGAIHYYLL KSAIHKDIVF NKKESLSFTG NSGPYIQYVG ARINSILEKY
     KALSIPVMEK IDFELLKHEK EWEIIKIISE LEENIINAAK DLNPSILTSY SYSLAKHFST
     YYQEVKVIDT NNINLTAARI EFLKAILQTI KNCMYLLNIP YMLKM