SYR_BRUA1
ID SYR_BRUA1 Reviewed; 585 AA.
AC B2S5B0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=BAbS19_I08360;
OS Brucella abortus (strain S19).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=430066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S19;
RX PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S.,
RA Bricker B., Yu G., Du L., Sobral B.W.;
RT "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT virulent strains yields candidate virulence genes.";
RL PLoS ONE 3:E2193-E2193(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; CP000887; ACD72357.1; -; Genomic_DNA.
DR RefSeq; WP_002964007.1; NC_010742.1.
DR AlphaFoldDB; B2S5B0; -.
DR SMR; B2S5B0; -.
DR EnsemblBacteria; ACD72357; ACD72357; BAbS19_I08360.
DR GeneID; 3788619; -.
DR KEGG; bmc:BAbS19_I08360; -.
DR HOGENOM; CLU_006406_0_1_5; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000002565; Chromosome 1.
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_1000095339"
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