ID   SYR_RICPR               Reviewed;         576 AA.
AC   Q9ZE81;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   Name=argS; OrderedLocusNames=RP065;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ235270; CAA14536.1; -; Genomic_DNA.
DR   PIR; A71715; A71715.
DR   RefSeq; NP_220459.1; NC_000963.1.
DR   RefSeq; WP_004599723.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZE81; -.
DR   SMR; Q9ZE81; -.
DR   STRING; 272947.gene:17555148; -.
DR   EnsemblBacteria; CAA14536; CAA14536; CAA14536.
DR   GeneID; 57569193; -.
DR   KEGG; rpr:RP065; -.
DR   PATRIC; fig|272947.5.peg.66; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_5; -.
DR   OrthoDB; 9803211at2; -.
DR   Proteomes; UP000002480; 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; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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; Reference proteome.
FT   CHAIN           1..576
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151600"
FT   MOTIF           126..136
FT                   /note="'HIGH' region"
SQ   SEQUENCE   576 AA;  65204 MW;  ECBAEB63C456F1BF CRC64;
     MNIFNQLKQD IIAASQKLYN NKEIANTATI ETPKDSFNGD LSSNIAMIIA SKESIAPREV
     ALKFKEVLVT LPYIASIEIA GPGFINFTIK AESWQAAIKD ILQHEEKFFE IDIDKNSNIN
     IEYVSANPTG PMHIGHARGA VYGDVLARIL QKVGYSVTKE YYVNDAGSQI NDLVSTVLLR
     YKEALGEPIT IPVGLYPGEY LIPLGEILSK EYGNKLLTMN DVERFKIIKS FAVEKMLDLN
     RKDLADLGIK HDVFFSEQSL YDKGEIEKTV KLLERMGLIY EGTLPAPKGK VHEDWEYRVQ
     KLFKSTNYGD SQDRPIEKAD GSWSYFASDL AYAKDKIDRG ANHLIYVLGA DHSGYVKRIE
     AIVKALGQEK VKVDVKICQL VNFVENGVPI KMSKRLGSFA SVQDVNKEVG KDIIRFMMLT
     RQNDKPLDFD LVKVKEQSRE NPIFYVQYAH VRTKSILSKA RELMPEAYNS FKEGKYNLSL
     LSSEEEIEII KLLAAWTKTL EASVKYFEPH RIAFYLINLA SKFHSMWNFG KENSDYRFII
     ENNKELTLAR LALASVIQKI IASGLEVIGV EPMVTM
//