ID   SYR_AQUAE               Reviewed;         583 AA.
AC   O67068;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   Name=argS; OrderedLocusNames=aq_923;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000657; AAC07033.1; -; Genomic_DNA.
DR   PIR; A70380; A70380.
DR   RefSeq; NP_213630.1; NC_000918.1.
DR   RefSeq; WP_010880568.1; NC_000918.1.
DR   AlphaFoldDB; O67068; -.
DR   SMR; O67068; -.
DR   STRING; 224324.aq_923; -.
DR   EnsemblBacteria; AAC07033; AAC07033; aq_923.
DR   KEGG; aae:aq_923; -.
DR   PATRIC; fig|224324.8.peg.723; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_0; -.
DR   InParanoid; O67068; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..583
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151524"
FT   MOTIF           121..131
FT                   /note="'HIGH' region"
SQ   SEQUENCE   583 AA;  68319 MW;  350807CA39C1220B CRC64;
     MKELVKEKVL KALKELYNTQ VENFKVEKPK EEAHGDLASN VAFLLARELK KPPVNIAQEL
     ADFLSKDETF KSVEAVKGFI NFRFSEDFLK EEFKKFLLSG EAYFKEDLGK GLKVQLEYVS
     ANPTGPLHLG HGRGAVVGDT LARLFKFFNY DVTREYYIND AGRQVYLLGI SIYYRYLEKC
     PERDEETFKE IKEIFEKDGY RGEYVKEIAE RLRKLVGESL CKPEEANLKE VREKILKEES
     IELYYTKKYE PKDVVDLLSN YGLDLMMKEI REDLSLMDIS FDVWFSERSL YDSGEVERLI
     NLLKEKGYVY EKDGALWLKT SLFGDDKDRV VKRSDGTYTY FASDIAYHYN KFKRGFEKVI
     NVWGADHHGY IPRVKAALKM LEIPEDWLEI LLVQMVKLFR EGKEVKMSKR AGTFVTLREL
     LDEVGKDAVR FIFLTKRSDT PLDFDVEKAK EKSSENPVYY VQYAHARISG IFREFKERYK
     KDVSVEELIN YVQHLEEEAE IKLIKKVLFF KDELVDITLK REPHLLTYYL IDLAGDFHHY
     YNHHRILGME ENVMFSRLAL VKGIKEVVRL GLNLMGVSAP ERM