ID   SYR_STAES               Reviewed;         553 AA.
AC   Q8CTN9;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 112.
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=SE_0380;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO03977.1; -; Genomic_DNA.
DR   RefSeq; NP_763935.1; NC_004461.1.
DR   RefSeq; WP_002438772.1; NZ_WBME01000026.1.
DR   AlphaFoldDB; Q8CTN9; -.
DR   SMR; Q8CTN9; -.
DR   STRING; 176280.SE_0380; -.
DR   DNASU; 1056748; -.
DR   EnsemblBacteria; AAO03977; AAO03977; SE_0380.
DR   GeneID; 50019461; -.
DR   KEGG; sep:SE_0380; -.
DR   PATRIC; fig|176280.10.peg.354; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_9; -.
DR   OMA; YEFKWER; -.
DR   Proteomes; UP000001411; 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.
FT   CHAIN           1..553
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151611"
FT   MOTIF           130..140
FT                   /note="'HIGH' region"
SQ   SEQUENCE   553 AA;  62535 MW;  EB776F5242F36AB1 CRC64;
     MNIIDQVKQT LIEEIEASIR KANLAEDIPE IKIEIPKDTK NGDYSSNIAM VLTKIAKRNP
     REIAQAIVDH LDTSKAHVKQ VDIAGPGFIN FYLDNQYLTD IIPEAITKGD RFGYATQSKN
     TNILLEYVSA NPTGDLHIGH ARNAAVGDSL ANILIAAGYN VTREYYINDA GNQITNLARS
     IEARYFEALG DTSYEMPADG YNGKDIIEIG KDLAVKHPEI KDYSDEERLK TFRQLGVDYE
     MEKLKKDLSD FNVHFDNWFS ETSLYENGAI KNTLSKMKEL GYTYEADGAT WLRTSDFKDD
     KDRVLIKKDG NYTYFTPDTA YHYNKINRGN DILIDLMGAD HHGYINRLKA SLETFGVDSD
     RLEIQIMQMV RLMQNGEEVK MSKRTGNAIT LREIMDEVGI DAARYFLTMR SPDSHFDFDL
     ELAKEQSQDN PIYYAQYAHA RICSILKQAK EQGIEVSTDA DFSKINNDKA IDLLKKVAEF
     ESTIESAAEH RAPHRLTNYI QDLAAAFHKF YNAEKVLTDD TEKTKAHVAM IEAVRITLHN
     ALALVGVTAP ESM