ID SYR_CLOBH Reviewed; 563 AA. AC A5I0R5; A7G2H6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 91. 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=CBO1072, CLC_1124; OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441771; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A; RX PubMed=17519437; DOI=10.1101/gr.6282807; RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A., RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., RA White B., Whithead S., Parkhill J.; RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain RT Hall A and comparative analysis of the clostridial genomes."; RL Genome Res. 17:1082-1092(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A; RX PubMed=18060065; DOI=10.1371/journal.pone.0001271; RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.; RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within RT plasmids."; RL PLoS ONE 2:E1271-E1271(2007). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000727; ABS36212.1; -; Genomic_DNA. DR EMBL; AM412317; CAL82626.1; -; Genomic_DNA. DR RefSeq; WP_011948742.1; NC_009698.1. DR RefSeq; YP_001253603.1; NC_009495.1. DR RefSeq; YP_001386991.1; NC_009698.1. DR AlphaFoldDB; A5I0R5; -. DR SMR; A5I0R5; -. DR GeneID; 5185327; -. DR KEGG; cbh:CLC_1124; -. DR KEGG; cbo:CBO1072; -. DR PATRIC; fig|413999.7.peg.1067; -. DR HOGENOM; CLU_006406_6_1_9; -. DR PRO; PR:A5I0R5; -. DR Proteomes; UP000001986; 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; cd07956; Anticodon_Ia_Arg; 1. 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_1000018016" FT MOTIF 120..130 FT /note="'HIGH' region" SQ SEQUENCE 563 AA; 63868 MW; 4BEF19B952256D83 CRC64; MDYKNLVAER IKENTELEVD LIEKLIEIPP KKEMGDYAFP CFQLAKTFRK APNLIAEELK EKINKEGFEK VVTVGPYLNF FVDKTILIKD VLEKVLSEKE KYGSSKVGEG KNVVVEYSSP NIAKPFHIGH LFTTAIGNAL YKILSFEGYN CIGINHLGDW GTQFGKLISA YRRWVDEEAL EKDAIGELLR IYVKFHGEAE KDPELEKEAR LNFKRLEEGS EEETELWNRF KDLSLKEFNK VYDMLGIKFD SLAGESFYSD KMDAVVQEID DKGLLVDSNG AKVVMLDEYN MPPCMIKKSD GATIYATRDL AAAIYRKKTY DFHKCIYVVG TPQALHFKQV FTTLKLMGHD WADDCKHVGF GLVKLANKKL STRNGDVVFL EDLLNQSVEE TLKIINEKNP NLKNKGDVAK KLGIGAVVFT YLKNNRERDI VFDWKEILSF DGETGPYVEY SYARGKSILR KAGELTGEAD YSKLSSKEEF ELAKLLGGFN DAIMNAIDKL EPAMVTRYVI EVAKAFNKFY NAHGILNAED NDVKLARVKL VEATCQVIKN ALNLLGIDVV EEM //