ID   SYR_FRATT               Reviewed;         581 AA.
AC   Q5NHI8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=FTT_0466c;
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4;
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA   Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA   Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA   Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA   Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(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; AJ749949; CAG45099.1; -; Genomic_DNA.
DR   RefSeq; WP_003020254.1; NZ_CP010290.1.
DR   RefSeq; YP_169504.1; NC_006570.2.
DR   AlphaFoldDB; Q5NHI8; -.
DR   SMR; Q5NHI8; -.
DR   IntAct; Q5NHI8; 4.
DR   STRING; 177416.FTT_0466c; -.
DR   DNASU; 3190944; -.
DR   EnsemblBacteria; CAG45099; CAG45099; FTT_0466c.
DR   KEGG; ftu:FTT_0466c; -.
DR   eggNOG; COG0018; Bacteria.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000001174; 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; 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..581
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242023"
FT   MOTIF           122..132
FT                   /note="'HIGH' region"
SQ   SEQUENCE   581 AA;  65995 MW;  4CBF10AAA5B6C004 CRC64;
     MNIENYLSET LAKVFQKLGY AESFAKVVTS TREDVRHFQC NGAMPLAKFA KKPPLAIAEE
     IVEHIDAEDI FAKLEVAKPG FINITLAPKF LADTTNRFLN SNKFGVQNNL PNRKVVLDFG
     GPNVAKPMHV GHIRSALLGD ALQRIHRFCG DTVVSDVHLG DWGTQMGMLI EEIKLQSPQL
     VYFDENYTGE YPTESPVTVQ ELAEIYPRAS KRCKSDINEM EKARLATFEL QQGRRGYVAL
     WQHFVRISID AVKKDFDSLD VHFDLWLGES DANKFIDEMI SYFQANNFIY EDEGAWVIDT
     NKDGVPPLIV IKKDGGVMYG TTDLATLWQR SKDLDPDEII YVVDKRQSLH FKQVFSVAER
     TKVVSEKCKL KHVAFGTVNG KDGRPFKTRE GGVMHLADLI SQAKEYAKNR MPDENDDSII
     NQIAMATIKF GDLINNYAND YFFDLEKFAQ HEGKTGPYLL YTVVRAKSIL RKIFGDNYDI
     KSLAKDYKVV NAHNEYEEKL QLQLIQFPIA VQRAYENSQP HHICEYAYSL ANSFNKFYVN
     CPINNLDDES LKKARIALCM ATVKAMTIAS DLIGISIPER M