ID   SYR_METM5               Reviewed;         566 AA.
AC   A4FXF3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, 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}; OrderedLocusNames=MmarC5_0568;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000609; ABO34882.1; -; Genomic_DNA.
DR   RefSeq; WP_011868336.1; NC_009135.1.
DR   AlphaFoldDB; A4FXF3; -.
DR   SMR; A4FXF3; -.
DR   STRING; 402880.MmarC5_0568; -.
DR   PRIDE; A4FXF3; -.
DR   EnsemblBacteria; ABO34882; ABO34882; MmarC5_0568.
DR   GeneID; 4929211; -.
DR   KEGG; mmq:MmarC5_0568; -.
DR   eggNOG; arCOG00487; Archaea.
DR   HOGENOM; CLU_006406_6_1_2; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 7046at2157; -.
DR   Proteomes; UP000000253; 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..566
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000018062"
FT   MOTIF           121..131
FT                   /note="'HIGH' region"
SQ   SEQUENCE   566 AA;  64359 MW;  EE6D53DB813E91F3 CRC64;
     MDVENLIITT LKDKVRELTG NEMDIRLDEP PAINMGDYST NISFRLAKDL KKAPKMIAED
     IANSLSILGI EKIEAVNGYI NFFMNYSDFS KETVSKISAE KENFGKLEKR DEKVILEHTS
     ANPNGPFHIG HGRNMVIGDS LKRILIASGY DVETQYYVND MGRQEAIVVF GNERFELDKS
     KKADHAIGEV YVETNKLLAE NEELEQEILN LMKNYEEACE AGIENELTEK FKNAVDYSLG
     GFKETLSTLN IYHDKFVWES EFVKSGMVRD VIKRLMDTGK VVEDEVFRLD LSDYGLEKKL
     VLARLNGTSL YSTRDIVYHI NKMENCDFAV NLLGADHKLT AVMVNKTLAL LGYNEAEVVF
     YEFISLPEGS MSTRRGRFIS MDELFEEAKS RAAEEVRKRG VAENEEEIEE IAKRIAVGAV
     RYNIVRIAPE KPMVFRWDEA LDFEKVGCPV IQYAHARCSR ILENVETISN DNLFAYEMNE
     NEKTIVKLLS KLPKIVEKAA EVRKPQIVAN YVLDVAQGFN KFYANCPVLK EENETIKNSR
     LAIVNTTKTV LENTLDLLGI EMPGKM