ID   SYR_METVS               Reviewed;         569 AA.
AC   A6UP37;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=Mevan_0350;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-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; CP000742; ABR54259.1; -; Genomic_DNA.
DR   RefSeq; WP_011972162.1; NC_009634.1.
DR   AlphaFoldDB; A6UP37; -.
DR   SMR; A6UP37; -.
DR   STRING; 406327.Mevan_0350; -.
DR   PRIDE; A6UP37; -.
DR   EnsemblBacteria; ABR54259; ABR54259; Mevan_0350.
DR   GeneID; 5325871; -.
DR   KEGG; mvn:Mevan_0350; -.
DR   eggNOG; arCOG00487; Archaea.
DR   HOGENOM; CLU_006406_6_1_2; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 7046at2157; -.
DR   Proteomes; UP000001107; 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..569
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000018067"
FT   MOTIF           121..131
FT                   /note="'HIGH' region"
SQ   SEQUENCE   569 AA;  64914 MW;  240BB70466A8A880 CRC64;
     MDVKKLIVVA IEKKVLDLTG KQIEIRLDEP PSINMGDYST NIAFRLSKEL KKAPKIIAEE
     ITSSLSIPGI EKIESLNGYI NFFMDYSVFS KETTLEINSK QENFGKSDLK NKKVILEHTS
     ANPNGPFHIG HGRNMVIGDS LKRILNAAGY TVETQYYVND MGRQEAIVVF GNDRFKLDKS
     KKSDHAIGQT YVEANKLLNE NEELEQEILN LMKNYEEAME NGIENEITEK FKNAVEYALT
     GFKETLSTLN IHHDKFVWES EFVRSGLVRN VINRLMETGK VTEEDVYRLD LSEFGIEKKL
     VLARLNGTSL YSTRDVAYHM TKMENCDFAV NLLGADHKLT GIMVNKTLAL LGYNEAEIVF
     YEFISLPEGS MSTRQGRFIS MDELFEEAKL RAREEVKKRE VAKTEEEIEE IAKKIAVGAV
     RYNIVRISPE KPMVFRWDEA LDFEKVGCPV IQYAHARCSR ILENCEPSGL VNSKNLFEYE
     MAENEKIIVK LISKLPEIVE KSAEVRKPQI LANYALELAQ GFNKFYGNCR ILKEENETVR
     NSRIMIVNST KLVLENSLDL LGIEMPGKM