ID   SYR_CLOAB               Reviewed;         563 AA.
AC   Q97K78;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 120.
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=CA_C1041;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK79017.1; -; Genomic_DNA.
DR   PIR; F97028; F97028.
DR   RefSeq; NP_347677.1; NC_003030.1.
DR   RefSeq; WP_010964359.1; NC_003030.1.
DR   AlphaFoldDB; Q97K78; -.
DR   SMR; Q97K78; -.
DR   STRING; 272562.CA_C1041; -.
DR   GeneID; 44997554; -.
DR   KEGG; cac:CA_C1041; -.
DR   PATRIC; fig|272562.8.peg.1249; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_9; -.
DR   OrthoDB; 9805987at2; -.
DR   Proteomes; UP000000814; 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; 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_0000151550"
FT   MOTIF           120..130
FT                   /note="'HIGH' region"
SQ   SEQUENCE   563 AA;  64392 MW;  0BE96F3464904E21 CRC64;
     MDYKKVIAER INKIVDMDVE ALYKIIEIPP KKDMGDFALP CFQFAKVLRK APNAIAEEVC
     KKIDQSGFEK VENLGPYINF FVDKADFAKE TIESVLSERD NYGRSKVGEG KKVLIEYSSP
     NIAKPFHVGH LFGTVLGSSL YKIFSMEGYD CVRINHLGDW GTQFGKLISA YKRWCDEDAL
     YKDPIKELLR IYVKFHKEAE KDPLLEDEGR MYFKRLEDGE KEEVELWTKF KDLSLREFKK
     VYNQIGVEFD SYTGESFYSD KIDAIEEELN EKGLLTESNG AKVVMLDEYN MPPCIIKKAD
     GASIYATRDL AAAEYRKKTY NFDKSIYVVG LEQSLHFKQF LKTLELAGHE WSKDCIHVGY
     GLVRFAEGKL STRNGDVIFL EDLLKESVQK TSEIIEEKNP ELDNKEEVSR KVGIGAVIFT
     YLKNGRERDI IFDWKEMLSF EGETGPYVQY SYARAKSILR KLGEVKGNVS YDKLVSAEEF
     DLIKQLKGFN GAILNAIDRL EPSVITRYVI EVAKAFNKFY NAYNISNTSD EELKNARLAL
     VEAASIVIKN ALSLIGIDVV EEM
//