ID   SYR_COXBU               Reviewed;         592 AA.
AC   Q83A98;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
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};
GN   OrderedLocusNames=CBU_2008;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016828; AAO91497.1; -; Genomic_DNA.
DR   RefSeq; NP_820983.1; NC_002971.3.
DR   RefSeq; WP_010958595.1; NC_002971.4.
DR   AlphaFoldDB; Q83A98; -.
DR   SMR; Q83A98; -.
DR   STRING; 227377.CBU_2008; -.
DR   EnsemblBacteria; AAO91497; AAO91497; CBU_2008.
DR   GeneID; 1209921; -.
DR   KEGG; cbu:CBU_2008; -.
DR   PATRIC; fig|227377.7.peg.1997; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_6; -.
DR   OrthoDB; 9803211at2; -.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07956; Anticodon_Ia_Arg; 1.
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..592
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151555"
FT   MOTIF           134..144
FT                   /note="'HIGH' region"
SQ   SEQUENCE   592 AA;  66765 MW;  6C0E9C27FCE8DCA4 CRC64;
     MIDLSTMKQQ IETLLNQAIE RLKTKGVLKP EVTPVIKITH TTDPQHGDFA TNLALTLSKA
     AGMSPHALAE KIVEALPPSG QITEVEIAGP GFINFFVTEG SYQTVVSSIL KAGKDYGRSE
     MGKGQRVHME YVSANPTGPL HVGHGRGAAY GACVANLLNA AGFEVHREYY VNDAGRQMGI
     LALSVWVRYL QGYEASIELP KNAYQGEYII DIAEALKAKY GKQFYHSVES IQAKIPEEID
     SNADPEAYLD VWVTAQKDLL GPKDFECVFQ AALDSILNDI KNDLEEFGVT YDDWFPESRL
     VREGLIQEGL DLLTKHGYVY EKNGAQWFRA TALGDEKDRV LIRKNGLPTY FAADVAYHLH
     KFNQGYDQII DIFGADHHGY IPRIRGFLKG LGKAPEKLHI LLVQFAILYR GNEKVSMSTR
     GGTFVTLREL RHEVGNDAAR FFYIMRKPDQ HLDFDLELAK SQSNENPVYY IQYAHARICS
     VFRQLKTTQK NWDRPRGMEN LSLLSTNYEK ELLATLGRYP EVIKRAAMNY APHLLAHYLQ
     TLANQFHTYY NAERFLIEDD NLRNARLNLI NAVQQIIRNG LTLLGVSAPE EM
//