ID   SYR_SYMTH               Reviewed;         558 AA.
AC   Q67TI9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=STH19;
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863;
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD39004.1; -; Genomic_DNA.
DR   RefSeq; WP_011194154.1; NC_006177.1.
DR   AlphaFoldDB; Q67TI9; -.
DR   SMR; Q67TI9; -.
DR   STRING; 292459.STH19; -.
DR   KEGG; sth:STH19; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_9; -.
DR   OrthoDB; 9805987at2; -.
DR   Proteomes; UP000000417; 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; cd07956; Anticodon_Ia_Arg; 1.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..558
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242103"
FT   MOTIF           134..144
FT                   /note="'HIGH' region"
SQ   SEQUENCE   558 AA;  63061 MW;  BA0FA42459141ED8 CRC64;
     MRIVEQIKSE IRQALADAVS RAVAAGALVG PAPEVFLETP KAREHGDFAT NLAMVMARQE
     KKAPRVIAQA IVDHLQTEGT WIESAEIAGP GFINLRLRQG WVHQVLPAIQ AEGADYGKSD
     HGGKQRILLE YVSANPTGPM VLVQARAGAF GSSLARLLNW AGYECHTEFY VNDAGNQVKI
     LARTVDLRAQ ELRGATVEIP EGYYPGEDVI DCARALLEQY PDFLEKPEEE RLAFLERWAP
     EYFRSGHERV LRSYGVEFDR WFSERSLREA GAPARLVEWL KERGEAYEKD GAVWMRTTAY
     GDDKDRVLVK SDGEYTYFAA DACYHKDKYD RGYATLIDIL GQDHHGYLGR MKAMVECLGH
     PRDSLEILFT QMVRLFKDGQ EFRMSKRRGN YVTLEDLLEQ VSVDAARYFF LMRSLDTHMD
     FDLDLANLKS SDNPVFYVQY AHARICSILR QAREQGLEVP AASEVDTALL ADESEVELMR
     KLAEFPEEII GAADAREVHR IPRYLNELAT LFHQFYSRCR VVSDDVPLSR ARLLLVDCTR
     TVLANALGIL GVSAPERM
//