ID   SYR_METS3               Reviewed;         575 AA.
AC   A5UMK8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=Msm_1231;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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   -!- 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; CP000678; ABQ87436.1; -; Genomic_DNA.
DR   RefSeq; WP_011954371.1; NC_009515.1.
DR   AlphaFoldDB; A5UMK8; -.
DR   SMR; A5UMK8; -.
DR   STRING; 420247.Msm_1231; -.
DR   EnsemblBacteria; ABQ87436; ABQ87436; Msm_1231.
DR   GeneID; 5216015; -.
DR   KEGG; msi:Msm_1231; -.
DR   PATRIC; fig|420247.28.peg.1230; -.
DR   eggNOG; arCOG00487; Archaea.
DR   HOGENOM; CLU_006406_6_1_2; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000001992; 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..575
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000018065"
FT   MOTIF           131..141
FT                   /note="'HIGH' region"
SQ   SEQUENCE   575 AA;  65338 MW;  AA478897DDF6F514 CRC64;
     MYFEIEKQAI DAISDALDKF EVDNTLENFQ VEDEKNFRLE FPPNPDMGDL ASTIAFSLAK
     KLRKAPNLIA SEIVEKLEIP EIFEKVEAIG PYVNFFIDYS NFSKKLLEYV GKDYGHLPKA
     DEKIILEHTS ANPNGPLHIG HVRNSIFGDS LNRLLKVAGR EVETQYYVND MGRQIAIIVF
     GITELGLKIE DQEGDKIDHK IGRLYFKANQ KLNEDESLVS HVDNLIERYE GGAEPELNKI
     FEEVVESCLL GIKETLHRIN INHDDFVWEG QFVRSGEVDD MIKYFDHEGF VSYGDVTYID
     LTCFQIEKEF VLRRSDGTSL YSTRDLAYHR YKATQGDVVL DILGSDHKLA AQQINVIFKE
     ILREIPPEVI FYEFITLPSG SMSTRKGVFV SVDELVDEAV KRAADEIKSR NPDLTDEEIK
     PMAEDIGVGA IRFFIAKLSP EKHLTFKWDE ALSFERGCAS IQYAHARACK LLKKSGKDVS
     SLAVSDDWVP NENEKDLIRT IAKFPQVIED CANKKRIHNI TQYCQDLAGA FNKFYKAEQV
     IGSDVEDTRL VLVDRAKTTL KNALDILGVP APQKM