ID   SYR_THEVB               Reviewed;         584 AA.
AC   Q8DKN4;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=tll0826;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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; BA000039; BAC08377.1; -; Genomic_DNA.
DR   RefSeq; NP_681615.1; NC_004113.1.
DR   RefSeq; WP_011056669.1; NC_004113.1.
DR   AlphaFoldDB; Q8DKN4; -.
DR   SMR; Q8DKN4; -.
DR   STRING; 197221.22294547; -.
DR   EnsemblBacteria; BAC08377; BAC08377; BAC08377.
DR   KEGG; tel:tll0826; -.
DR   PATRIC; fig|197221.4.peg.870; -.
DR   eggNOG; COG0018; Bacteria.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000000440; 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..584
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151624"
FT   MOTIF           125..135
FT                   /note="'HIGH' region"
SQ   SEQUENCE   584 AA;  65503 MW;  D2E5B5314EC98CF3 CRC64;
     MVAPIKILGD RLRRALQAAL PLDTYPQPLL VPASQVKFGD YQSNVCLSLA KQLGKAPREL
     AQEVVPHLEV EDLCQPVEIA GPGFLNFRLK PEFLAATLQA ARGSDRLGIP PAREPRRVVV
     DFSSPNIAKE MHVGHLRSTI IGDCIARILE FQGHTVLRLN HVGDWGTQFG MLIAYLDEVY
     PDALTTANAL DLGDLVTFYK KAKQRFDSDP EFQQKARAKV VALQQGEEQS RRAWQLLCEQ
     SRREFQKIYD LLDIQLTERG ESFYNPFLPA VIEDLAACGL LVEDQGAKVV FLEGFTNKEG
     QPQPLIIQKS DGGYNYATTD LAALRYRIDK DQADWIIYVT DVGQSTHFAQ VFQVAQRAGW
     VPPHVTLTHV PFGLVLGEDG KRLKTRSGET IRLIDLLTEA IARSRADLEQ RLATEGRTES
     PEFIDTVARA IGIGAVKYAD LSQNRNSNYV FSYDKMLSLQ GNTAPYLLYA YVRVQGLTRR
     GDIDWCTLSP DSPLLLEDET EQHLAKHLVQ LEETLDLVST ELLPNRLCQY LFELSQLFNQ
     FYDRCPILSA PQPTKQSRLT LAYLTAQTLK LGLSLLGIPV LDRI