ID   SYR_CHLL3               Reviewed;         552 AA.
AC   Q3B147;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Plut_2092;
OS   Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS   luteolum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=319225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 273 / BCRC 81028 / 2530;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelodictyon luteolum DSM 273.";
RL   Submitted (AUG-2005) 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; CP000096; ABB24934.1; -; Genomic_DNA.
DR   RefSeq; WP_011358804.1; NC_007512.1.
DR   AlphaFoldDB; Q3B147; -.
DR   SMR; Q3B147; -.
DR   STRING; 319225.Plut_2092; -.
DR   PRIDE; Q3B147; -.
DR   EnsemblBacteria; ABB24934; ABB24934; Plut_2092.
DR   KEGG; plt:Plut_2092; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_10; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000002709; 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.
FT   CHAIN           1..552
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242063"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   552 AA;  61921 MW;  3D51F4B30957F30F CRC64;
     MQSFLVAEIQ NALRSASVTT GQSIIIEKPT SPKFGDYATN IAFLAAKELK RNPRQLAEEL
     TGHFRFPEGT VTKTEVAGPG FINFFMEPAF IMQSAERVFR EGAEYGKGRE GQGKTAIVEY
     VSANPTGPLT IGRGRGGVLG DCIANLAEAQ GYHVNREYYF NDAGRQMQIL GESVRYRYME
     LCGRTIDFPD THYKGGYIGE IAEKIHSEHG EDLLHVESIE PFRSEAESII FSSIQKTLGR
     LGIVHDSFFN EHTLYTADLN GISPNQNVID RLREKGFIGE YDGATWFLTT KLGQEKDKVL
     IKSSGEPSYR LPDIAYHVTK YARGFDMIIN VFGADHIDEY PDVLEALKIL GHDTAHVRIA
     INQFVTTTVN GETVKMSTRK GNADLLDDLI DDVGPDATRL FFIMRSKDSH LNFDVELAKK
     QSKDNPVFYL QYAHARICSL LRLAWSEIGF DAAKRPEPGV LMRLTTPEEL QLAFGILDFG
     EASRSAFRML EPQKMVDYMH SIAELFHRFY QECPILKAEP EIAEARLFLA VAVRQVLQNG
     FRILGISAPE SM