ID   SYR_NITWN               Reviewed;         597 AA.
AC   Q3SRM3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=Nwi_1807;
OS   Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS   NCIMB 11846 / Nb-255).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX   PubMed=16517654; DOI=10.1128/aem.72.3.2050-2063.2006;
RA   Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA   Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA   Hickey W.J.;
RT   "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT   Nitrobacter winogradskyi Nb-255.";
RL   Appl. Environ. Microbiol. 72:2050-2063(2006).
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; CP000115; ABA05068.1; -; Genomic_DNA.
DR   RefSeq; WP_011315064.1; NC_007406.1.
DR   AlphaFoldDB; Q3SRM3; -.
DR   SMR; Q3SRM3; -.
DR   STRING; 323098.Nwi_1807; -.
DR   EnsemblBacteria; ABA05068; ABA05068; Nwi_1807.
DR   KEGG; nwi:Nwi_1807; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_5; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000002531; 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   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; Reference proteome.
FT   CHAIN           1..597
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242055"
FT   MOTIF           138..148
FT                   /note="'HIGH' region"
SQ   SEQUENCE   597 AA;  65428 MW;  A6DF8E91710B0424 CRC64;
     MTDSSPSQHL FADVLARVHR ACAALAEEGA LPSGLDLARI VVEPPRDASH GDMATNAAMV
     LAKDAKAKPR DLAERIVTKL RADDLIESAD IAGPGFINLT LKLPVWADVL RDVLRDGEGY
     GRSAIGAGEK VNVEYVSANP TGPMHVGHCR GAVFGDALAS LLSFAGYDVT REYYINDAGS
     QVDVLARSAF LRYREALGED IGEIPDGLYP GDYLKPVGQA LAAGHGDSLV KAPEAEWLGL
     VRAKAIGMMM EMIRGDLAAL NIRHDVFFSE RSLIDGSADR VAETIGFLRE KGDVYEGRLP
     PPKGAPVEDY EDREQTLFRA TAYGDDVDRP LKKSDGGYTY FASDIAYHKT KFDRGFHNMV
     DVWGADHGGY IKRVQAAIKA VTSGKGTLDV KIVQLVKLLR NGEPVKMSKR AGDFVTLREV
     VEEVGSDAVR FMMLFRKNDA VLDFDLARVI EQSKDNPVFY VQYGHARGFS IFRNAREVFP
     DLPEADAERR QFLGTADLER LSDPAELGLL RKLALYPRTV EAAAAAHEPH RIAFYLYDLA
     SEFHALWTKG RDLPHLRFII NNDAQITRAR LALVQGVVAV LASGLTVLGV HAPTEMR