ID   SYR_THISH               Reviewed;         586 AA.
AC   B8GU79;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
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};
GN   OrderedLocusNames=Tgr7_0263;
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7;
RX   PubMed=21475584; DOI=10.4056/sigs.1483693;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL71362.1; -; Genomic_DNA.
DR   RefSeq; WP_012636851.1; NC_011901.1.
DR   AlphaFoldDB; B8GU79; -.
DR   SMR; B8GU79; -.
DR   STRING; 396588.Tgr7_0263; -.
DR   KEGG; tgr:Tgr7_0263; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_6; -.
DR   OrthoDB; 9803211at2; -.
DR   Proteomes; UP000002383; 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; 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..586
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000198940"
FT   MOTIF           128..138
FT                   /note="'HIGH' region"
SQ   SEQUENCE   586 AA;  65513 MW;  C1DA50E0DB9D5609 CRC64;
     MKDQLQALIE QAIDALRQDG TLPGDTAVDV QVTRTKDKAH GDFATNVALQ LAKPARKKPR
     DVAEAIVARL PASGLVARTE IAGPGFINLF LGEQAKLSVI ATIREQGERY GRSQLGAGKK
     VQVEFVSANP TGPLHVGHGR GAAYGAAVAD LLEAVGFDVH REYYVNDAGR QMDILGTSVW
     LRYLELTGVE LPFPTNAYRG DYVYDIAATL HREHGDHYKR EAAEILDGLP PDEPDGGDKE
     EYIDAMIARA KELLGDNHYR FVFELGLNVI LDDIRDDLAE FGVTYDTWYS ERSLTDKGAV
     NLAIERLREA GHLYEKDGAL WFRSTDFGDE KDRVVQRDNG QTTYFASDIA YHMDKMERGY
     DRVIDVWGAD HHGYVPRVKA ALKALGEDET RLDVLLVQFA ILYRGGERVQ MSTRSGSFVT
     LRELREEVGK DAARFFYVMR RCEQHLDFDL DLAKSQSADN PVYYIQYAHA RVCSVLRQME
     AKGLKHDPSH GEAKLSLLTE SHEQEILATL ARFPEVIEAA ALVEEPHQIA NYLRELANDF
     HTYYNAHQFL VDEPAIRDAR LSLILAVRQV IANGLGLLGV SAPQEM
//