ID   SYR_CLOB8               Reviewed;         563 AA.
AC   A6LS73;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   10-JUN-2026, entry version 93.
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=Cbei_1019;
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000721; ABR33203.1; -; Genomic_DNA.
DR   RefSeq; WP_011968362.1; NC_009617.1.
DR   AlphaFoldDB; A6LS73; -.
DR   SMR; A6LS73; -.
DR   KEGG; cbe:Cbei_1019; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_9; -.
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; cd07956; Anticodon_Ia_Arg; 1.
DR   CDD; cd00671; ArgRS_core; 1.
DR   FunFam; 1.10.730.10:FF:000008; Arginine--tRNA ligase; 1.
DR   FunFam; 3.40.50.620:FF:000116; Arginine--tRNA ligase; 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.
FT   CHAIN           1..563
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000076209"
FT   MOTIF           120..130
FT                   /note="'HIGH' region"
SQ   SEQUENCE   563 AA;  63629 MW;  B93B1A193F07C8BC CRC64;
     MDYKSKVAEL IKKHVELEIE AIEKLIEIPP KPEMGDYAFP CFQLSKVMRK APNMIAEELK
     NSMSTDGFER IENLGPYVNF FVDKGVFAEN TIKKALEDGE NYGASNIGEG KTVCVEYSSP
     NIAKPFHVGH LFTTAIGNSL YKMFKKEGYN TVGLNHLGDW GTQFGKLISA YDRWVDEEAL
     EKAPIDELLR IYVKFHEEAE KDPSLEDEAR ANFKALETGD EKATALWTRF RDLSLKEFER
     VYNILGVKFD SLAGEAFYND KMDVVVNELK EKGLLVESNG AQVVMLEEYN MPPCIVLKGD
     GASIYATRDL AAAMYRKKTY DFHKCVYVVG TPQALHFKQV FKVLELAGHE WAKDCVHVGF
     GLVKFADRKL STRNGSIVLL DDLLREAVEK TMEVINEKNP ELENKEEVAK KIGVGAVIFT
     YLKNSREKDI VFDWKEILSF DGETGPYVQY SYARGNSILN RGKECTGTVD YSKLSSKEEF
     ELVKSIANFN SVITLALDKL EPSILTRYVI EVAKGFNKFY NAHSVLNLED EDLKATRLNL
     VKASLQVIKN GLELLGIDVV EKM
//