ID   SYR_CLAMS               Reviewed;         554 AA.
AC   B0RAP7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=CMS1474;
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS   / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=31964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX   PubMed=18192393; DOI=10.1128/jb.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
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; AM849034; CAQ01585.1; -; Genomic_DNA.
DR   RefSeq; WP_012298852.1; NZ_MZMN01000003.1.
DR   AlphaFoldDB; B0RAP7; -.
DR   SMR; B0RAP7; -.
DR   STRING; 31964.CMS1474; -.
DR   PRIDE; B0RAP7; -.
DR   EnsemblBacteria; CAQ01585; CAQ01585; CMS1474.
DR   KEGG; cms:CMS1474; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_11; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000001318; 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; Reference proteome.
FT   CHAIN           1..554
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000076208"
FT   MOTIF           132..142
FT                   /note="'HIGH' region"
SQ   SEQUENCE   554 AA;  60487 MW;  C6272609C2F4A7BA CRC64;
     MTTPDLTGAL FEIVARTAGR RPGGDAIALS PDMVVLERPR NRDHGDWATN IAMRIAKPLG
     ESPRTIAADI AKALGELPQV AKVDVAGPGF INITLEAAAA GALAHTIVES GPAYGRGHSL
     EGIRINLEFV SANPTGPIHL GGVRWAAVGD SLARILQAEG ADVTREYYFN DHGSQIDRFA
     RSLLASHLGE ETPEDGYGGA YIGEIAERVV EGYEGDIDAL TREAQQEVFR KSGTELMFGE
     IKQKLHDFGV DFDVFFHEDS LHESGAVDRA IARLTELGHV FEEDGAIWLR TTTFGDDRDR
     VVIRSTGEPA YISGDLGYYL DKRERGFEQN IIMLGADHHG YVGRMMAMVE AFGDTPGVNL
     QILIGQMVNL LRDGEPVRMS KRAGTIVTLD DLVDAVGVDA GRYALVRSSA DQNLDIDLAV
     LGKRTNDNPV FYVQYAHART CAVDRNAAAS GVDRSAFAPE LLTHPTESAL LGLLQEFPRI
     VAQAAELREP HRVARYVEEL AGSYHRWYDS CRVVPRGDEE VTDLHRTRLW LNDAVRQVVA
     NGLNLVGVSA PERM