ID   SYR_THET8               Reviewed;         592 AA.
AC   Q5SM45;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=TTHA0098;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) 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; AP008226; BAD69921.1; -; Genomic_DNA.
DR   RefSeq; WP_011227708.1; NC_006461.1.
DR   RefSeq; YP_143364.1; NC_006461.1.
DR   PDB; 1IQ0; X-ray; 2.30 A; A=1-592.
DR   PDBsum; 1IQ0; -.
DR   AlphaFoldDB; Q5SM45; -.
DR   SMR; Q5SM45; -.
DR   STRING; 300852.55771480; -.
DR   EnsemblBacteria; BAD69921; BAD69921; BAD69921.
DR   GeneID; 3169614; -.
DR   KEGG; ttj:TTHA0098; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_0; -.
DR   OMA; NKPLHLG; -.
DR   PhylomeDB; Q5SM45; -.
DR   EvolutionaryTrace; Q5SM45; -.
DR   Proteomes; UP000000532; 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   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   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..592
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242112"
FT   MOTIF           112..122
FT                   /note="'HIGH' region"
SQ   SEQUENCE   592 AA;  66227 MW;  BA300E5F28F672E6 CRC64;
     MLRRALEEAI AQALKEMGVP VRLKVARAPK DKPGDYGVPL FALAKELRKP PQAIAQELKD
     RLPLPEFVEE AVPVGGYLNF RLRTEALLRE ALRPKAPFPR RPGVVLVEHT SVNPNKELHV
     GHLRNIALGD AIARILAYAG REVLVLNYID DTGRQAAETL FALRHYGLTW DGKEKYDHFA
     GRAYVRLHQD PEYERLQPAI EEVLHALERG ELREEVNRIL LAQMATMHAL NARYDLLVWE
     SDIVRAGLLQ KALALLEQSP HVFRPREGKY AGALVMDASP VIPGLEDPFF VLLRSNGTAT
     YYAKDIAFQF WKMGILEGLR FRPYENPYYP GLRTSAPEGE AYTPKAEETI NVVDVRQSHP
     QALVRAALAL AGYPALAEKA HHLAYETVLL EGRQMSGRKG LAVSVDEVLE EATRRARAIV
     EEKNPDHPDK EEAARMVALG AIRFSMVKTE PKKQIDFRYQ EALSFEGDTG PYVQYAHARA
     HSILRKAGEW GAPDLSQATP YERALALDLL DFEEAVLEAA EERTPHVLAQ YLLDLAASWN
     AYYNARENGQ PATPVLTAPE GLRELRLSLV QSLQRTLATG LDLLGIPAPE VM