ID   SYR_GEOUR               Reviewed;         561 AA.
AC   A5G3W5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Gura_2304;
OS   Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=351605;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1134 / JCM 13001 / Rf4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA   Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter uraniireducens Rf4.";
RL   Submitted (MAY-2007) 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; CP000698; ABQ26483.1; -; Genomic_DNA.
DR   RefSeq; WP_011939177.1; NC_009483.1.
DR   AlphaFoldDB; A5G3W5; -.
DR   SMR; A5G3W5; -.
DR   STRING; 351605.Gura_2304; -.
DR   EnsemblBacteria; ABQ26483; ABQ26483; Gura_2304.
DR   KEGG; gur:Gura_2304; -.
DR   HOGENOM; CLU_006406_0_1_7; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000006695; 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..561
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000076216"
FT   MOTIF           129..139
FT                   /note="'HIGH' region"
SQ   SEQUENCE   561 AA;  62651 MW;  E0262C1DD274788B CRC64;
     MKELLRDLIT KELASCFADG SLSSGVFPSI VIEKPAHAEH GDFATNVAML LAKAEKKAPR
     VVAEILVSRL QESADICSKL EVAGPGFINF YVKDEAWRQT LIAIDRACAD YGKSRIGEGK
     KIQVEFVSAN PTGPLHIGHG RGAAIGDTIC RLLAAIGWDV TREFYYNDAG QQIANLALSV
     QARCLGIEPD DPRWPLDGYQ GDYIRDVARS YLGQETVEAD DQHVTAAGDP QDLDAIRRFA
     VAYLRREQDQ DLTAFDVHFD VYSLESALYA EGRVEAVVQR LIDSGHTYEQ DGALWLRTTT
     FGDDKDRVMR KADGGYTYFV PDVAYHLSKW ERGFTRVINE QGADHHSTIT RVRAGLQALN
     AGIPVGWPEY VLHQMVTVMR GGEEVKISKR AGSYVTLRDL IDEVGRDATR FFFVMRKPDS
     QLVFDIDLAK QQTLDNPVYY VQYAHARICS IFENALERGF VLPAAESVPL ERLVTLEEMT
     IIKTLASFPE ILEGSALNFE PHRVTYYLQE LAGQFHSFYN RNRVITEDAE LTAARLFLLK
     CVALTLKNAL TVLGISAPEK M