ID   SYR_RUEST               Reviewed;         580 AA.
AC   Q1GI80;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=TM1040_0903;
OS   Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria; unclassified Ruegeria.
OX   NCBI_TaxID=292414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040;
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   Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL   Submitted (MAY-2006) 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; CP000377; ABF63636.1; -; Genomic_DNA.
DR   RefSeq; WP_011538248.1; NC_008044.1.
DR   AlphaFoldDB; Q1GI80; -.
DR   SMR; Q1GI80; -.
DR   STRING; 292414.TM1040_0903; -.
DR   PRIDE; Q1GI80; -.
DR   EnsemblBacteria; ABF63636; ABF63636; TM1040_0903.
DR   KEGG; sit:TM1040_0903; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_5; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000000636; 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..580
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000018123"
FT   MOTIF           131..141
FT                   /note="'HIGH' region"
SQ   SEQUENCE   580 AA;  63653 MW;  80D4613EEC9CA8A7 CRC64;
     MNLFTDIRTL VIDSLAAMTA EGALPEGLDF ANVTVEPPRD AAHGDMATNA AMVLAKPAKM
     KPRDIAEALA AKLAQDKRIT SAEVAGPGFL NLRLDLSVWQ DVLGKALNAE EAYGRSDMGQ
     GKRVNVEYVS ANPTGPLHVG HTRGAVFGDA LASLLDFAGY DVTREYYIND GGAQVDVLAR
     SAYLRYLEAH GQSVEFPDGT YPGEYLKDVG AALKDKFGDR FVGQPEETWL EEVRNFATDM
     MMDLIREDLA LLGVEMDVFY SEKSLYGTGR IEAALESLDA KGLIYEGVLE PPKGKKPDDW
     EPRIQTLFKS TEHGDDVDRP VKKSDGAWTY FAPDIAYHYD KVSRGFDMLI DIFGADHGGY
     VKRMKAAVSA LSDGKVPLDV KLCQLVKLFK DGQEFKMSKR AGTFVTLRDV VDAVGADVTR
     FMLLTRKNDQ GFDFDLDKAL EQSKDNPVFY VQYANARIHS TLRKAREAGI ACDEATLSGA
     DLSLLTHDAQ LAVARKVAEW PRQVEIAART NEPHRIAFFL YELASDLHGL YHLGKSEESL
     RFVNESSELA THANLALARA VSIVISAGLG ILGVKPAQEM