ID   SYR_BACTN               Reviewed;         597 AA.
AC   Q8A3X5;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 119.
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=BT_2829;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(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; AE015928; AAO77935.1; -; Genomic_DNA.
DR   RefSeq; NP_811741.1; NC_004663.1.
DR   RefSeq; WP_008765307.1; NC_004663.1.
DR   AlphaFoldDB; Q8A3X5; -.
DR   SMR; Q8A3X5; -.
DR   STRING; 226186.BT_2829; -.
DR   PaxDb; 226186-BT_2829; -.
DR   EnsemblBacteria; AAO77935; AAO77935; BT_2829.
DR   GeneID; 60924010; -.
DR   KEGG; bth:BT_2829; -.
DR   PATRIC; fig|226186.12.peg.2876; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_10; -.
DR   InParanoid; Q8A3X5; -.
DR   OrthoDB; 9805987at2; -.
DR   Proteomes; UP000001414; 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   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..597
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151531"
FT   MOTIF           125..135
FT                   /note="'HIGH' region"
SQ   SEQUENCE   597 AA;  66954 MW;  14983726E8F617B0 CRC64;
     MKIEDKLVAS VINGLKALYG QEVPEKMVQL QKTKKEFEGH LTLVVFPFLK MSRKGPEQTA
     QEIGEYLKAN EPAVAAFNVI KGFLNLTIAS ATWIELLNEI QSDEEYGLVK ATETSPLVMI
     EYSSPNTNKP LHLGHVRNNL LGNALANIVA ANGNRVVKTN IVNDRGIHIC KSMLAWKKYG
     NGETPESTGK KGDHLVGDYY VSFDKHYKAE LAELMEKGMT KEEAEAASPL MQEAREMLVK
     WEAGDPEVRA LWEMMNNWVY AGFDETYRKM GVGFDKIYYE SNTYLEGKEK VMEGLEKGFF
     FKKEDGSVWV DLTAEGLDHK LLLRGDGTSV YMTQDIGTAK LRFADYPIDK MIYVVGNEQN
     YHFQVLSILL DKLGFEWGKG LVHFSYGMVE LPEGKMKSRE GTVVDADDLM EEMVSTAKET
     SQELGKLDGL TQEEADDIAR IVGLGALKYF ILKVDARKNM TFNPKESIDF NGNTGPFIQY
     TYARIQSVLR KAAESGIVIP EQIPAGIELS EKEEGLIQLV ADFAAVVKQA GEDYSPSIIA
     NYTYDLVKEY NQFYHDFSIL REENEAVKVF RIALSANVAK VVRLGMGLLG IEVPSRM
//