ID   SYR_YERPS               Reviewed;         576 AA.
AC   Q66AV1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=YPTB2029;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(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; BX936398; CAH21267.1; -; Genomic_DNA.
DR   RefSeq; WP_011192408.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66AV1; -.
DR   SMR; Q66AV1; -.
DR   EnsemblBacteria; CAH21267; CAH21267; YPTB2029.
DR   GeneID; 66841538; -.
DR   KEGG; ypo:BZ17_436; -.
DR   KEGG; yps:YPTB2029; -.
DR   PATRIC; fig|273123.14.peg.466; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000001011; 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.
FT   CHAIN           1..576
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242127"
FT   MOTIF           122..132
FT                   /note="'HIGH' region"
SQ   SEQUENCE   576 AA;  64126 MW;  F92649F54B4602B8 CRC64;
     MNIQALLSDK VSQALIAAGA PADCEAQVRQ SAKAQFGDYQ ANGVMAVAKK LGMQPRQLAE
     RVVELLDLTG IASKIEIAGP GFINIFLDRQ WVAEKVEYAL TAPKLGVAPV EPQTIVVDYS
     APNVAKQMHV GHLRSTIIGD AAVRTLAFLG HNVIRANHVG DWGTQFGMLI AYLEKMQNEN
     ASDMGLSDLE LFYQQAKKTY DEDEEFALRA RAYVVKLQSG DEYCRQMWRK LVDITMAQNQ
     VAYDRLNVTL TKDDVMGESL YNAMLPEIVA DLKAKGLAVE SEGATVVYLD EYKNKDGEPM
     GVIIQKKDGG YLYTTTDIAC AKYRYETLGA DRILYYIDSR QHQHLMQAWT IVRKAGYVPE
     SVPLEHHMFG MMLGKDGKPF KTRSGGTVKL SDLLDEAVER AGKLIAEKNP DMPADELKQV
     INAVGIGAVK YADLSKSRTT DYIFDWDNML ALDGNTAPYM QYAYTRVVSV FRRAGVDETS
     LTLPLVITED REAALATRLL QFEEIITTVA REGTPHVMCS YLYDLAGLFS SFYEHCQILN
     AESEEIRQSR LKLAMLTAKT LKQGLDTLGI QTVERM