SYR_BRUSU
ID SYR_BRUSU Reviewed; 585 AA.
AC Q8G146; G0K9A5;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=BR0877, BS1330_I0873;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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; AE014291; AAN29805.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18222.1; -; Genomic_DNA.
DR RefSeq; WP_004689634.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8G146; -.
DR SMR; Q8G146; -.
DR EnsemblBacteria; AEM18222; AEM18222; BS1330_I0873.
DR GeneID; 45051940; -.
DR GeneID; 55590582; -.
DR KEGG; bms:BR0877; -.
DR KEGG; bsi:BS1330_I0873; -.
DR PATRIC; fig|204722.21.peg.2568; -.
DR HOGENOM; CLU_006406_0_1_5; -.
DR OMA; NKPLHLG; -.
DR PhylomeDB; Q8G146; -.
DR Proteomes; UP000007104; 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; -; 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_0000151538"
FT MOTIF 131..141
FT /note="'HIGH' region"
SQ SEQUENCE 585 AA; 65124 MW; D9F99D72766C2B6B CRC64;
MNIFADFDAR IKKTLQDIDL 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 KLPPPKGQLP
EDWEDREQTL FRSTEVGDDI DRPLMKSDGS FTYFAGDVAY FKDKYDRGFN EMIYVLGADH
GGYVKRLEAV ARAVSDGKAK LTVLLCQLVK LFRNGEPVRM SKRAGEFITL RDVVDEVGRD
PVRFMMLYRK NDAPLDFDFA KVTEQSKDNP VFYVQYASAR CHSVFRQAAD QLGLVDLDRV
AMGSHFEKLT DESEIALVRK LAEYPRLIES AAIHQEPHRL AFYLYDLASS FHSQWNRGTE
NPDLRFIKVN DPDLSLARLG LVQVVSDVLT SGLTIIGADA PTEMR
