ID   SYR_CHLTR               Reviewed;         563 AA.
AC   O84460;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 135.
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=CT_454;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 323-369.
RC   STRAIN=L2/434/Bu;
RA   Wang L., Steenburg S.D., Zheng Y., Larsen S.H.;
RT   "Gene identification of Chlamydia trachomatis by random DNA sequencing.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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; AE001273; AAC68054.1; -; Genomic_DNA.
DR   EMBL; AF087268; AAD04046.1; -; Genomic_DNA.
DR   PIR; A71513; A71513.
DR   RefSeq; NP_219967.1; NC_000117.1.
DR   RefSeq; WP_009871812.1; NC_000117.1.
DR   AlphaFoldDB; O84460; -.
DR   SMR; O84460; -.
DR   STRING; 272561.CT_454; -.
DR   EnsemblBacteria; AAC68054; AAC68054; CT_454.
DR   GeneID; 884196; -.
DR   KEGG; ctr:CT_454; -.
DR   PATRIC; fig|272561.5.peg.491; -.
DR   HOGENOM; CLU_006406_5_1_0; -.
DR   InParanoid; O84460; -.
DR   OrthoDB; 9805987at2; -.
DR   Proteomes; UP000000431; 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; 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..563
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151548"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   563 AA;  62980 MW;  335C9A0CF6E00553 CRC64;
     MTTLLSFLTS LCSAAIHQAF PELEELTLDI TPSTKEHFGH YQCNDAMKLA RVLHKSPRAI
     AESIVAHIPP TPFSSIEIAG 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 KRRMGLESPP QEGPLAVHEP
     AEEALALTLL RFPEILDLTL RELCPHFLTD YLYALTNKFN AFFRDCHIEG SDSQQERLYL
     CGLTERTLST GMHLLGLKTL NHL
//