ID   SYR_CHLL2               Reviewed;         551 AA.
AC   B3EIJ1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=Clim_2484;
OS   Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 245 / NBRC 103803 / 6330;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium limicola DSM 245.";
RL   Submitted (MAY-2008) 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   -!- 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; CP001097; ACD91503.1; -; Genomic_DNA.
DR   RefSeq; WP_012467367.1; NC_010803.1.
DR   AlphaFoldDB; B3EIJ1; -.
DR   SMR; B3EIJ1; -.
DR   STRING; 290315.Clim_2484; -.
DR   EnsemblBacteria; ACD91503; ACD91503; Clim_2484.
DR   KEGG; cli:Clim_2484; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_10; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000008841; 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   Gene3D; 3.30.1360.70; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..551
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000095348"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   551 AA;  62064 MW;  3037D6B4C78809F9 CRC64;
     MQEFLLPVIK SALQSAAIET DKPVQIEKPT DKKNGDFSTN IALLLSKECR RNPRELAAEL
     IGQMIFPDGT VERIEIAGPG FINFYLTPLF IMQSVEHILL EGKGYGSSCA GKGKTAIVEY
     VSANPTGPLT IGRGRGGVLG DCIANLLATQ GYGLTREYYF NDAGRQMQIL GESVRYRYME
     RCGRDIVFPE SHYQGEYIRE IAEILFLEHE SSLIDSDNLS IFKDTAEAII FSSIKKTLAR
     IDIRHDSFFN EHTLYIAEGN GKSANDRVLE LLESKGFIDR YDGATWFLTT KLGQEKDKVL
     VKSSGEPSYR LPDIAYHLDK YRRKFDLIVN VFGADHIDEY PDVLEALRIL GHDTSKMRVA
     INQFVTTTVD GETVKMSTRK GNADLLDELI DDVGADATRL FFIMRSKDSH LNFDIELAKK
     QSKDNPVFYL QYAHARICSL LRIAAEEAGF KPDGSGAHLL QKLTLEPEIQ LGFTLLDYPE
     VIRTAIRLLE PQKMVEYLHS VAEQYHKFYQ ECPILKADPD IRTARLFLSL ATRQVLRNGF
     TILGISAPES M