ID   SYR_EHRRG               Reviewed;         576 AA.
AC   Q5FH87;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 106.
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=ERGA_CDS_05040;
OS   Ehrlichia ruminantium (strain Gardel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=302409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gardel;
RX   PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(2006).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAI27956.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR925677; CAI27956.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_044157001.1; NC_006831.1.
DR   AlphaFoldDB; Q5FH87; -.
DR   SMR; Q5FH87; -.
DR   EnsemblBacteria; CAI27956; CAI27956; ERGA_CDS_05040.
DR   KEGG; erg:ERGA_CDS_05040; -.
DR   HOGENOM; CLU_006406_0_1_5; -.
DR   OrthoDB; 1146366at2; -.
DR   BioCyc; ERUM302409:ERGA_RS02615-MON; -.
DR   Proteomes; UP000000533; 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_0000242019"
FT   MOTIF           132..142
FT                   /note="'HIGH' region"
SQ   SEQUENCE   576 AA;  65365 MW;  DCB7B35A2B8AE584 CRC64;
     MSVACTIRRH IIEKLHVLNI DNFVVTNESI LAKLIVDYPN NPDHGDLYTN AALILSKYIK
     KNPMDIAKIL VDEFSSIKEI SDINVVKPGF INFNISLDVW YEIIISINRL KEKFGHVNFG
     NGKRVNIEFV SANPTGPMHI GHARGAIFGD VLANLLERVG YEVVREYYIN DAGAQVDVLV
     ESVYLRYKEV LGENIVIGSG LYPGLYLKDI GKLLYQEYGS GLLGMDYSQR RRIIRDVSLM
     YLMKLIKEDL ALLGIKHDIF TSESQLQKDN IVQKCVELLQ EKQLIYYGTL DQPKGTEGIN
     WKPRTQMLFK STDFGDDVDR ALQKADGSWT YFANDIAYHF YKISRGFQHM ILELGSDHIG
     YVKRLKAAVK ALSDGNATID IKLHSIVNFL DNGAQVKMSK RSGEFLTIKD VIEKVGKDVV
     RFIMLTRKSD VVLDFDFAKV VEQSKNNPVF YVQYAHARVH SLIRNAPKIL EIELVDFSVL
     SSKEEILLIK LLAKWQDIVE ISAKTAEPHR ITFYLIEVAE AFHALWGYGN KSTDMRFIVD
     NNINLTSARI YLAKSVGYVI ASGLTIFSIV PLTEMK