ID   SYR_BURTA               Reviewed;         594 AA.
AC   Q2T1N6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=BTH_I0355;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(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; CP000086; ABC39196.1; -; Genomic_DNA.
DR   RefSeq; WP_009893259.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2T1N6; -.
DR   SMR; Q2T1N6; -.
DR   PRIDE; Q2T1N6; -.
DR   EnsemblBacteria; ABC39196; ABC39196; BTH_I0355.
DR   GeneID; 66545881; -.
DR   KEGG; bte:BTH_I0355; -.
DR   HOGENOM; CLU_006406_0_1_4; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000001930; 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..594
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242000"
FT   MOTIF           139..149
FT                   /note="'HIGH' region"
SQ   SEQUENCE   594 AA;  64580 MW;  F68CAC6E57BFBF19 CRC64;
     MLPAQKHTLE TLLENSVKQV VQASKGDADA AFVLPAIALE RPKVAAHGDV ACNVALQLAK
     PLGANPRQLA ERIVAALTAQ PAAAGLVDAA EIAGPGFINL RLTPASKQAV IGAVFAQGRA
     FGASEREHGK RVLLEFVSAN PTGPLHVGHG RQAALGDALA NVLASQGYAV HREFYYNDAG
     VQIGNLAIST QARARGLKPG DAGWPEAAYN GEYIADIARD YLNGETVAAS DGEPVTGKRD
     ADDLEAIRKF AVAYLRREQD MDLKAFGVKF DQYYLESSLY TEGRVEKTVD ALIAAGMTYE
     QEGALWLRTT DEGDDKDRVM RKTDGTYTYF VPDVAYHVTK WERGFTKVIN IQGSDHHGTI
     ARVRAGLQGL HIGIPKGYPD YVLHKMVTVM RDGQEVKISK RAGSYVTVRD LIEWSGGATP
     GSEVSPELLD EATITRGRDA VRFFLISRKA DTEFVFDIDL ALKQNDENPV YYVQYAHARI
     CSVLNEWKSR YGATDALLPG ADLSPLDSKQ AMALMQKLAE YPDVLAHAAN ELAPHAVAFY
     LRELASEFHS FYNAERVLVD EEAPRTARIA LLAATRQVLE NGLAMLGVSA PSKM