ID   SYR_BRUAB               Reviewed;         585 AA.
AC   Q57DN0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 93.
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};
GN   OrderedLocusNames=BruAb1_0889;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AE017223; AAX74254.1; -; Genomic_DNA.
DR   RefSeq; WP_002964007.1; NC_006932.1.
DR   AlphaFoldDB; Q57DN0; -.
DR   SMR; Q57DN0; -.
DR   EnsemblBacteria; AAX74254; AAX74254; BruAb1_0889.
DR   GeneID; 3788619; -.
DR   KEGG; bmb:BruAb1_0889; -.
DR   HOGENOM; CLU_006406_0_1_5; -.
DR   Proteomes; UP000000540; Chromosome I.
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; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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_0000241994"
FT   MOTIF           131..141
FT                   /note="'HIGH' region"
SQ   SEQUENCE   585 AA;  65186 MW;  354143BD9F45FD56 CRC64;
     MNIFADFDAR IKKTFQDIDL KPKDGGELDL SRIGVEPPRD ASHGDIATNA AMVLSKAVGQ
     NPRELAARIA EALKADEDVE SVDVAGPGFI NLRLKASYWQ RELLVMLNEG TDFGRSRLGA
     GKKVNVEYVS ANPTGPMHVG HCRGAVVGDV LANLLKFAGY DVVKEYYIND AGAQIDVLAR
     SVMLRYREAL GESIGEIPAG LYPGDYLVRV GQELAGEFGT KLLEMPEAEA LAIVKDRTID
     AMMAMIRADL DALNVHHDVF YSERKLHVDH ARAIRNAIND LTLKGHVYKG KLPPPKGRLP
     EDWEDREQTL FRSTEVGDDI DRPLMKSDGS FTYFAGDVTY FKDKYDRGFN EMIYVLGADH
     GGYVKRLEAV ARAVSDGKAK LTVLLCQLVK LFRNGEPVRM SKRAGEFITL RDVVDEVGRD
     PVRFMMLYRK NDAPLDFDFA KVTEQSKDNP VFYVQYASAR CHSVFRQAAD QLGLVDLDRV
     AMGSHFEKLT DESEIALVRK LAEYPRLIES AAIHQEPHRL AFYLYDLASS FHSQWNRGAE
     NPDLRFIKVN DPDLSLARLG LVQVVSDVLT SGLTIIGADA PTEMR
//