ID   SYR_PARUW               Reviewed;         584 AA.
AC   Q6MEP4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=pc0231;
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC   Candidatus Protochlamydia.
OX   NCBI_TaxID=264201;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25;
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA   Mewes H.-W., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(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; BX908798; CAF22955.1; -; Genomic_DNA.
DR   RefSeq; WP_011174781.1; NC_005861.1.
DR   AlphaFoldDB; Q6MEP4; -.
DR   SMR; Q6MEP4; -.
DR   STRING; 264201.pc0231; -.
DR   PRIDE; Q6MEP4; -.
DR   EnsemblBacteria; CAF22955; CAF22955; PC_RS01120.
DR   KEGG; pcu:PC_RS01120; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_0; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000000529; 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; Reference proteome.
FT   CHAIN           1..584
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242060"
FT   MOTIF           130..140
FT                   /note="'HIGH' region"
SQ   SEQUENCE   584 AA;  66381 MW;  D71B63069ED04EED CRC64;
     MNTLLSVLAN LFQQATANAF PDLSVLDPNF QPEITPSTQE KFGHYQFNSA MKLAKLLKKN
     PRQVAEAIVN QLTDSLPPLS KIEIAGPGFI NMTFSTDFLS KNLDILLRDA HFGIPFPEKP
     EKIIIDFSSP NVAKEMHVGH LRSTVIGDSL ARLFEFLGHH VIRLNHLGDW GTAFGMLIAY
     MKEEAPNVLS GEQKTDLTHL VSWYRSSKKK FDEEPEFKRR AQLEVVALQQ GEQKAREAWQ
     MICEISQKAY QEIYQLLDVK IIDRGESFYN PFLPNIVSDL EKKGLVKISD GAKCIFLEGF
     QNREGENLPL MIQKSDGGYN YDTTDMAAIY HRIYHEKGDR LIYITDAGQA THFQMIFKAA
     EKAKYLDTTQ IRVDHVPFGL VLGTDGKKFR TRSGETEKLI DLLRTAINCA DKILSEKNPE
     MEESERRHLA KSLGIGAIKY ADLSCNRVGD YTFSYDRMLR FEGNTAAFLM YAYVRIAGIK
     RRLKANLPAV LENTHINLEH STEIELGLHI LRFHETLNLM ANDLLPNRLT DYLYTLAEKF
     NAFFRDCRVE GTPQQNTRLL LCEATAKVLK QGLTILGLTT VDKM