ID   SYR_SALRD               Reviewed;         562 AA.
AC   Q2S3W3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=SRU_0986;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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; CP000159; ABC46058.1; -; Genomic_DNA.
DR   RefSeq; WP_011403746.1; NC_007677.1.
DR   RefSeq; YP_445118.1; NC_007677.1.
DR   AlphaFoldDB; Q2S3W3; -.
DR   SMR; Q2S3W3; -.
DR   STRING; 309807.SRU_0986; -.
DR   PRIDE; Q2S3W3; -.
DR   EnsemblBacteria; ABC46058; ABC46058; SRU_0986.
DR   KEGG; sru:SRU_0986; -.
DR   PATRIC; fig|309807.25.peg.1023; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_10; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000008674; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..562
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242087"
FT   MOTIF           126..136
FT                   /note="'HIGH' region"
SQ   SEQUENCE   562 AA;  62397 MW;  08A98C82AEAAA7ED CRC64;
     MKDYLRTQIR RVLDALGDVP DDFEIELEAP DRPEHGDLAT NTALRLASVL GDNPRSIAET
     LAERLRERVD PARIKSVEVA GPGFVNFRFA QDYLFDGLAD LLAQGDTFGQ TDAGAGERAL
     VEYVSANPTG PLNVGHGRNA VLGDTIANLL AWTGYDVTRE YYYNDAGRQM RVLAQSVRAR
     YEALAGNVPT TTLTLDDDTT VEVPETFPED GYLGQYIVEI AQALYDEHGD ALCATDDLAP
     FRAAAETAIF GDIEATLRAL NIDMDGYANE QALHDEGRVD AVLDGLADAG YTYEEDGALW
     FKTTEFGTED DTVLVKQTGE PTYRTPDIAY HTAKFERGFD LMVDVFGADH HAAYPDVLSA
     LDVLGYDTDR VDVILYQFVT LVRGDEPVKM STRRANYVTL DDLIEQVGAD VTRFFFLMRS
     PDTHLNFDLE LAEEESEKNP VFYLQYAHAR ICSVLDKAEE VGFSHDEDAD LALLTHEDEI
     ALIKELLRFP RELQNAADAR APHFVPNYLR DVATAFSQFY DNCRIIGEEQ ELASARMRLA
     LAAKTVLKNG LTVLGISAPR QM