ID   SYR_AGARV               Reviewed;         597 AA.
AC   C4ZD15;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
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=EUBREC_2239;
OS   Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS   / VPI 0990) (Eubacterium rectale).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Agathobacter.
OX   NCBI_TaxID=515619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC   0990;
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001107; ACR75978.1; -; Genomic_DNA.
DR   RefSeq; WP_012743073.1; NC_012781.1.
DR   AlphaFoldDB; C4ZD15; -.
DR   SMR; C4ZD15; -.
DR   STRING; 515619.EUBREC_2239; -.
DR   PaxDb; 515619-EUBREC_2239; -.
DR   KEGG; ere:EUBREC_2239; -.
DR   HOGENOM; CLU_006406_5_1_9; -.
DR   Proteomes; UP000001477; 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; 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.
FT   CHAIN           1..597
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000203094"
FT   MOTIF           124..134
FT                   /note="'HIGH' region"
SQ   SEQUENCE   597 AA;  66744 MW;  C0B7B15F19EABD3A CRC64;
     MKKLINLISE EVTKAFVSAG YDEKYGKVTL SNRPDLCEFQ CNGAMAAAKE YKCAPFMISD
     KVAALLESDE MFESVESVKP GFLNIKMDTA FLAKYMNDMK DDEGRYGLEK AKKPLTIVVD
     YGGPNVAKPL HVGHLRSAVI GESVKRIAKF MGHNVIGDVH LGDWGLQMGL IITELRERKP
     DLVYFDESYT GEYPKEAPFT ISELEDIYPT ASGKSKSDES FKEAALLATK ELQGGRRGYQ
     ALLSHIMNVS VTDLKRNYEN LNVHFELWKG ESDAQPYVPG MVEMMKEKGF AHMSEGALVV
     DVKEDTDTKE IPPCIILKSD GASLYSTTDL ATLVMRMKEN NPDRVIYLAD ARQSMHFIQV
     FRCARKTGIV PDTTELVHIG FGTMNGKDGK PFKTRDGGVM RLEYLLKEID DEMLNKIKEN
     QKEKENLNID EAEAEQTAKT VALAAVKYGD LSNQASKDYI FDIDRFTSFE GNTGPYILYT
     IVRIKSILSK YEAKGGDISA LKDAIMPAVN AGQKNLMLSL AKFNATIESA YEESAPHKIC
     AYIYELANAF NGFYHDTKIL SEENEELKKS YISLLVLTKE ILEACIDMLG FSAPDRM
//