ID   SYR_ACIAD               Reviewed;         596 AA.
AC   Q6FFM0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=ACIAD0164;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG67137.1; -; Genomic_DNA.
DR   RefSeq; WP_004930584.1; NC_005966.1.
DR   AlphaFoldDB; Q6FFM0; -.
DR   SMR; Q6FFM0; -.
DR   STRING; 62977.ACIAD0164; -.
DR   EnsemblBacteria; CAG67137; CAG67137; ACIAD0164.
DR   GeneID; 45232683; -.
DR   KEGG; aci:ACIAD0164; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_6; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   BioCyc; ASP62977:ACIAD_RS00765-MON; -.
DR   Proteomes; UP000000430; 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; 2.
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..596
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000241973"
FT   MOTIF           128..138
FT                   /note="'HIGH' region"
SQ   SEQUENCE   596 AA;  66918 MW;  5B541365535D241E CRC64;
     MNTAIQAALD HVVQSLQQEG ILPSDWNNNS TLTRTKDRSH GDFASNIAMV GSKAAGMKPR
     DLAEKILASL PEVADITKAE IAGPGFINFF LNADQRFAVL DQIQAQGQYY GQTQVNAEKK
     IQVEFVSANP TSSLHVGHGR GAAYGMTVAN LLEATGAQVD REYYVNDAGR QMDILATSTY
     LRYLELLGQP LVFPKNAYQG DYVKEIAQSI IDKDGDAYVR SVADVYRNVP EDVQYAEELD
     SEGNKVVLSG DKEKHIDGLI ANSQQLIGQG YRVFHQAALK AILDDIKDDL ADFGVTFDQW
     FSEASLTQKI DEALQTLDQR GYLYEKEGNI WFKSTKFGDE KDRVVKRRNG QTTYFASDIA
     YHLDKLQRGY THIVDIWGSD HHGYIARVKA AIDAMGYDSS KLTVLLVQFV SLWRGGEMVQ
     MSSRSGQFVT LRELRQEVGN DAARFYYVMR KSEQHIDFDL DLAVSQSKDN AVYYIQYAHA
     RICRMLEKAN STQMRFNQTQ ARQFANRLDL DAETEILAKL AAYPDILVRA ANAYEPHQIG
     NYLKELAALF HGWYNEHKVL TEDVELTQAR LLLSVNVQQV LRNGLDLLGV SAPEAM