ID   SYR_CHLTA               Reviewed;         563 AA.
AC   Q3KLP4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   04-NOV-2026, entry version 102.
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=CTA_0496;
OS   Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC   Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
OC   Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX   PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Arg) + L-arginine + ATP = L-arginyl-tRNA(Arg) + AMP +
CC         diphosphate; 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; CP000051; AAX50728.1; -; Genomic_DNA.
DR   RefSeq; WP_011324741.1; NC_007429.1.
DR   AlphaFoldDB; Q3KLP4; -.
DR   SMR; Q3KLP4; -.
DR   KEGG; cta:CTA_0496; -.
DR   HOGENOM; CLU_006406_5_1_0; -.
DR   OMA; AAAYHKW; -.
DR   Proteomes; UP000002532; 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   FunFam; 3.40.50.620:FF:000030; Arginine--tRNA ligase; 1.
DR   FunFam; 3.30.1360.70:FF:000002; arginine--tRNA ligase, cytoplasmic; 1.
DR   FunFam; 1.10.730.10:FF:000006; Arginyl-tRNA synthetase 2, mitochondrial; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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; 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..563
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242004"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   563 AA;  63071 MW;  F322C9CBE2E4A63C CRC64;
     MTTLLSFLTS LCSAAIHQAF PELEELTLDI TPSTKEHFGH YQCNDAMKLA RVLRKSPRAI
     AESIVAHIPP APFSSIEIAG AGFINFTFSK EFLASQLQTF SKELANGFRA ASPQKVIIDF
     SSPNIAKDMH VGHLRSTIIG DCLARCFSFV GHDVLRLNHI GDWGTAFGML ITYLQETSQE
     AIHQLEDLTA LYKKAHARFA EDSEFKKRSQ HNVVALQSGD AQALALWKQI CSVSEKSFQT
     IYSILDVELH TRGESFYNPF LAEVVADLES KNLVTLSDGA KCVFHEAFSI PLMIQKSDGG
     YNYATTDVAA MRYRIQQDQA DRILIVTDSG QSLHFQLLEA TCLAAGYLPS KGIFSHVGFG
     LVLDTQGRKF KTRSGENIKL RELLDTAVEK AKESLKAHRP DISEEELAYQ GPILGINAIK
     YADLSSHRIN DYVFSFEKML RFEGNTAMSL LYAYVRIQGI KRRMGLESLP QEEPLAIHEP
     AEEALALTLL RFPEILDLTL RELCPHFLTD YLYALTNKFN AFFRDCHIEG SDSQQERLYL
     CGLTERTLST GMHLLGLKTL NHL
//