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SYR_BRAHW
ID   SYR_BRAHW               Reviewed;         534 AA.
AC   C0R2B0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=BHWA1_01783;
OS   Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC   Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX   NCBI_TaxID=565034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49526 / WA1;
RX   PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA   Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA   Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA   Barrero R., Phillips N.D., Hampson D.J.;
RT   "Genome sequence of the pathogenic intestinal spirochete Brachyspira
RT   hyodysenteriae reveals adaptations to its lifestyle in the porcine large
RT   intestine.";
RL   PLoS ONE 4:E4641-E4641(2009).
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; CP001357; ACN84248.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0R2B0; -.
DR   SMR; C0R2B0; -.
DR   STRING; 565034.BHWA1_01783; -.
DR   EnsemblBacteria; ACN84248; ACN84248; BHWA1_01783.
DR   KEGG; bhy:BHWA1_01783; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_12; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000001803; 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; -; 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; 2.
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   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..534
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000198877"
FT   MOTIF           131..141
FT                   /note="'HIGH' region"
SQ   SEQUENCE   534 AA;  61484 MW;  F988F31EA474BB82 CRC64;
     MESRRMLKKI ISNILKEALK EYLKDTDVKD IESYIEIGYA VDDKFGDYAC PVAMRLAKVL
     KKNPLEIANS ITEKIDKKYF DKIEVAKPGF INLTLSYNYI NECINDLINN DDYGKNTVED
     KKKILVEYVS ANPTGPLHIG HGRWAAIGSA LSNILKYAGH EVYQEFYVND AGEQITKLNE
     SVKAVQEGRE IPEDGYHGEY IKDVAKQDGV PKDIILESQK KLLERFGTHM DNYASELKIR
     EGGELEKTMD FLDKEGLLFE EDNAVWFKST KYGDDKDRVV KKSNGTYTYF APDITYHKNK
     IDRGYHYLID ILGADHHGYV PRITAAVRAV SKDTASLKVI LGQLVRLYRG NELVRMSKRT
     GDMISLEDVI DEIGVDPTRY FLLMRSYSSS LDFDLELAKK KDNDNPVYYV QYAYARICNI
     FFKLEEKNMS YDDNKPLDIS KIANESSLKL AKMILRFPDE IYEAAKSLEV YTLINYTYEI
     ASALHRFYYD NIVLEENAEI RQERLTLIKA VKKILGLCFD IIGISKVERM WSEE
 
 
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