ID   SYR_CLOK1               Reviewed;         566 AA.
AC   B9E1W5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 62.
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=CKR_1439;
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016;
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA   Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT   of Clostridia species.";
RL   Submitted (SEP-2005) 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; 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; AP009049; BAH06490.1; -; Genomic_DNA.
DR   RefSeq; WP_012101940.1; NC_011837.1.
DR   AlphaFoldDB; B9E1W5; -.
DR   SMR; B9E1W5; -.
DR   EnsemblBacteria; BAH06490; BAH06490; CKR_1439.
DR   KEGG; ckr:CKR_1439; -.
DR   HOGENOM; CLU_006406_6_1_9; -.
DR   Proteomes; UP000007969; 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..566
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000198888"
FT   MOTIF           120..130
FT                   /note="'HIGH' region"
SQ   SEQUENCE   566 AA;  65277 MW;  6FAE822C077322CC CRC64;
     MDFKKLAAEE IKKNIDLELN FIEGLIEVPP KPEMGDYAFP CFQLAKVLKK APNIISKELK
     DKLHSKYFEK IENLGPYVNF FVDKKIFTEY TLKEILLKGD SYGSSDMGEG KNVVVEYSSP
     NIAKPFHVGH LFSTSIGNAL YKMINFQGYN CTRINHLGDW GTQFGKLIAA YNRWCNAEEL
     NRDPIKELLR IYVKFHEEAE KDPSLNEEGR MYFKKLEDGS EEEIKLWKKF KDLSLREFKK
     VYDLLKVDFD SYAGESFYTD KMDAVVEEID KKGLLVESNG AKVVLLDEYN IPPCIVKKSD
     GTTIYATRDL AAAIYRKKTY DFYKSIYVVG LDQSLHFKQV FTTLKLMGKD WADSCKHVGF
     GLVRFANKKL STRKGDVIFL EELLNKSVER TLEIINEKNP KLENKEEAAK KIGIGAVIFT
     YLKNNREKDI VFDWNEMLSF EGETGPYVQY SYARGKSILR KSEEASYDEN QIDYSKLGSK
     EEFELVKILE NFNKSIINAI NRLEPFIVTR YVIDVAKAFN KFYNAHSIMN AADENIKKAR
     LYLVKCTCQV LKNGLNLMGI EVVEKM