ID   SYR_CROS8               Reviewed;         577 AA.
AC   A7MEC0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   09-APR-2025, entry version 87.
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=ESA_01360;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU76620.1; -; Genomic_DNA.
DR   RefSeq; WP_004387403.1; NC_009778.1.
DR   AlphaFoldDB; A7MEC0; -.
DR   SMR; A7MEC0; -.
DR   GeneID; 56730216; -.
DR   KEGG; esa:ESA_01360; -.
DR   HOGENOM; CLU_006406_5_1_6; -.
DR   Proteomes; UP000000260; 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   FunFam; 1.10.730.10:FF:000001; Arginine--tRNA ligase; 1.
DR   FunFam; 3.30.1360.70:FF:000001; Arginine--tRNA ligase; 1.
DR   FunFam; 3.40.50.620:FF:000030; 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; Reference proteome.
FT   CHAIN           1..577
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000018026"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   577 AA;  63926 MW;  33EA0CB3C397DE56 CRC64;
     MNIQALLSEK VSQALIAAGA PADCEPQVRQ SAKAQFGDYQ ANGVMAIAKK LGMPPRQFAE
     QALAHLDLTG IAAKTEIAGP GFINIFLDPA FLAKNIEAAV ASDRAGVEKV SAPQTIVVDY
     SAPNVAKEMH VGHVRSTIIG DASVRTLEFL GHKVIRANHV GDWGTQFGML IAYLEKQQQE
     NAGEMALSDL EGFYREAKKH YDEDEAFAER ARSYVVKLQG GDEYCREMWR KLVDITMTQN
     QITYQRLNVT LTRDDVMGES LYNPMLPGIV ADLKAKGLAV ESEGATVVFL DEFKNKEGEP
     MGVIIQKKDG GYLYTTTDIA CAKYRYETLH ADRVLYYIDS RQHQHLMQAW TIVRKAGYVP
     ESVPLEHHMF GMMLGKDGKP FKTRAGGTIK LSELLDEALD RARRLVAGKN PDMPADELEK
     LANAVGIGAV KYADLSKSRT TDYIFDWDNM LAFEGNTAPY MQYAYTRVLS VFRKAGVKES
     ELTAPVVIQD DREAQLAARL LQFEETLGVV ARDGTPHVMC AYLYDLAGLF SGFYEHCPIL
     TAETDALRQS RLKLALLTAK TLKLGLDTLG IETVERM
//