ID   SYR_BORT9               Reviewed;         584 AA.
AC   A1R025;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   27-MAR-2024, entry version 84.
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=BT0594;
OS   Borrelia turicatae (strain 91E135).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC   Borrelia.
OX   NCBI_TaxID=314724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91E135;
RA   Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA   Schwan T.G.;
RT   "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT   comparative analysis of two agents of endemic N. America relapsing fever.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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; CP000049; AAX17917.1; -; Genomic_DNA.
DR   RefSeq; WP_011772535.1; NZ_CP073176.1.
DR   AlphaFoldDB; A1R025; -.
DR   SMR; A1R025; -.
DR   KEGG; btu:BT0594; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_12; -.
DR   Proteomes; UP000001205; 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; 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..584
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000198876"
FT   MOTIF           127..137
FT                   /note="'HIGH' region"
SQ   SEQUENCE   584 AA;  67356 MW;  566B4123FB1BD2EE CRC64;
     MISKIKKDLE NKISKTIKEL ALKQNITLDK INIIMKKPPK SELGDLSILI FEFSKILKLS
     TSVIIEEIIK QIGKKYTTKS MGAYLNIKFN RKEYIKDIIK KVNEQKEKYG INNVLKNKRI
     IIEFSSPNTN KPLHVGHLRN DIIGESLSRI LKASGGQVTK INLINDRGTH ICKTMLAYKK
     FGNNTTPELS LKKGDHLIGD FYVKYNEYAK NNKMAEDEIQ QLLCKWEEGD EETVKLWKKL
     NKWAIEGIKE TYKLTNITFD KIYLESEIFK IGREIILQGL EKGLCYKRED GAICINIPIE
     TNEMTDQKFK QKVLLRANGT SIYLTQDLGN ILTRKNEFDF DEMIYVVGSE QIHHFKTLFY
     VADKLGITKE NNLVHLSYGM VNLPTGKMKS REGHVIDADN LIHDLSESTM IEIKKRHSNE
     QDSKKIALNI SLGAIHYYLL KTAIHKDILF NKEESLSFTG NSGPYIQYVG ARINSILDKY
     DELNLPSKNI NFDLLINENE WAIIKIISEF EEYIIKAAKD RNPSIIVNYS YLLAKSFSAY
     YQDTKIIDKD NPELTHARTD LSKAVLQTIK NCMHLLNIPY MKKM
//