ID   SYR_THEMA               Reviewed;         546 AA.
AC   Q9X0H8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   Name=argS; OrderedLocusNames=TM_1093;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000512; AAD36169.1; -; Genomic_DNA.
DR   PIR; D72298; D72298.
DR   RefSeq; NP_228899.1; NC_000853.1.
DR   RefSeq; WP_004080362.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9X0H8; -.
DR   SMR; Q9X0H8; -.
DR   STRING; 243274.TM_1093; -.
DR   PaxDb; 243274-THEMA_08885; -.
DR   EnsemblBacteria; AAD36169; AAD36169; TM_1093.
DR   KEGG; tma:TM1093; -.
DR   eggNOG; COG0018; Bacteria.
DR   InParanoid; Q9X0H8; -.
DR   OrthoDB; 9805987at2; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
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; 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   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.
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..546
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151628"
FT   MOTIF           122..132
FT                   /note="'HIGH' region"
SQ   SEQUENCE   546 AA;  62482 MW;  C255EF5281C0FE93 CRC64;
     MLVNAIRQKV SEVISKAYGS EIEFEVEIPP RKEFGDLSTN VAMKLAKTLK KNPREIAQEI
     VKSLDEDPSF DRIEIMGPGF INFFLSNELL RGVVKTVLEK KDEYGRENVG NGMKVQFEYG
     SANPTGPFTV GHGRQIIIGD VLSEVYKELG YDVTREMYIN DAGKQIRLLA QSLWARYNQL
     LGVEKEIPEG GYRGEYLVDI ARDLVNEIGD RYKDLWNEEV EEFFKQTALN RILSSMKDTL
     EKIGSSFDVY FSEKSLIEDG TVEEVLKLLK NKDVVYEKDG AVWLKVSAFI DEEDKVLVRS
     DGTYTYFMTD IAYHYKKYKR GFRKVYDIWG SDHHGHIPRM KAAMKALDIP DDFFNVILHQ
     FVTLKRGGEI VRMSTRAGEF VTLDELLDEV GRDATRYFFA MVDPNTHMVF DIDLAKAKSM
     DNPVYYVQYA HARIHNLFSN AEKKGVKFEE GKHLELLGNE EERVLMRNLG MFNTALKEVA
     QMFAPNRLTN YLQSLAESFH AFYTKHVIVD PENPELSNAR LNLALATGIV LRKGLKLIGV
     SAPERM
//