ID   SYR_BORDL               Reviewed;         585 AA.
AC   B5RME6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN   Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; OrderedLocusNames=BDU_595;
OS   Borrelia duttonii (strain Ly).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=412419;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ly;
RX   PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA   Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA   Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT   "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT   relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL   PLoS Genet. 4:E1000185-E1000185(2008).
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00123};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR   EMBL; CP000976; ACH93532.1; -; Genomic_DNA.
DR   RefSeq; WP_012538341.1; NC_011229.1.
DR   AlphaFoldDB; B5RME6; -.
DR   SMR; B5RME6; -.
DR   STRING; 412419.BDU_595; -.
DR   PRIDE; B5RME6; -.
DR   EnsemblBacteria; ACH93532; ACH93532; BDU_595.
DR   KEGG; bdu:BDU_595; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_12; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000000611; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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.
FT   CHAIN           1..585
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000095335"
FT   MOTIF           127..137
FT                   /note="'HIGH' region"
SQ   SEQUENCE   585 AA;  67249 MW;  CE96893EF201D2AE CRC64;
     MIKTIKADLK NKIQKTIKEL ALSSNIKLDK INIVMQKPPK SEMGDLSILI FEFSKILKLS
     IPVITQEIIK QIGNEYKTKS MGPYLNIKFN RKEYIQNTIK KVNKEKENYG ANNSLQNKKT
     IIEFSSPNTN KPLHVGHLRN DIIGESLSRI LKASGSKVTK INLINDRGTH ICKSMLAYKK
     FGNNITPEIA QKKGDHLIGD FYVKYNEYAS QNSEIAENEI QQLLCQWEQG DEKTVQLWTK
     LNKWAIDGIK ETYNTTNITF DKIYLESEIF KIGREVVING LKEGLCYKRE DGAICINIPT
     EKNNIDNQNF KQKVLLRANG TSIYLTQDLG NIVARKNEFD FDEMIYVVGS EQIHHFKTLF
     YVADKLGVTN ENNLIHLSYG MVNLPEGKMK SREGNIIDAD NLIHDLSQST MLELKKRYEN
     EQNLQKLALN ISLGAIHYYL LKTAIHKDIL FNKTESLSFT GNSGPYIQYV GARINSILDK
     YNNLNLANKN TNFDLLVNEN EWEIIKIISE FEEYIIKASK DRNPSIIANY SYLLAKNFST
     YYQDTKIIDK DNLELTHARI DLAKAVLQTI KNCMHLLNIP YIQKM