ID   SYR_PROA2               Reviewed;         551 AA.
AC   B4S6D8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Paes_2238;
OS   Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=290512;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 271 / SK 413;
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., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL   Submitted (JUN-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; CP001108; ACF47240.1; -; Genomic_DNA.
DR   RefSeq; WP_012506770.1; NC_011059.1.
DR   AlphaFoldDB; B4S6D8; -.
DR   SMR; B4S6D8; -.
DR   STRING; 290512.Paes_2238; -.
DR   EnsemblBacteria; ACF47240; ACF47240; Paes_2238.
DR   KEGG; paa:Paes_2238; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_10; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000002725; 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; 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_1000095391"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   551 AA;  61934 MW;  EBA1428DFEBA1912 CRC64;
     MQEYLIASIQ QALLASGIEP PKEITIEKPS NKQFGDFSTN IALTLAKECR KNPRQLAEEI
     SAKLEFRPET VDKTTIAGPG FINFYLTPAF IMQSVEQVLN EGDQFGKTCT GKGQKAIVEY
     VSANPTGPLT IGRGRGGVLG DCIANLLESQ GYKVTREYYF NDAGRQMTIL AESVRLRYLE
     CCGEAIAFPD THYQGDYISD IAAKLFEKHG VELKEVSQLD EFKQIAETYI FASIKNTLHR
     LNIHHDSFFN EHKLYQTGQN GKSPNEQVID ALDKAGYISN YDGAVWFTTT KLGQEKDKVL
     IKSTGEPSYR LPDIAYHVTK YERAFSEIIN VFGADHIDEY PDVIEALRIL GYDPGRIKVA
     INQFVTTTVN GETVKMSTRK GNADLLDDLI DDVGADATRL FFIMRSKDSH LNFDVELAKK
     QSRDNPVFYL QYAHARICSL VKLAEQEIGF TQSDIGVHLM QNLDSPHELQ LGLALLDFPE
     VISSAVRMLE PQKMVEYLHH VAELYHRFYQ ECPILKAEPD ICKARLFLSL ATRQVLQNGF
     RILGVTAPTA M