ID   SYR_CORJK               Reviewed;         556 AA.
AC   Q4JUI1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   27-MAR-2024, entry version 104.
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=jk1354;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAI37526.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR931997; CAI37526.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041626385.1; NC_007164.1.
DR   AlphaFoldDB; Q4JUI1; -.
DR   SMR; Q4JUI1; -.
DR   STRING; 306537.jk1354; -.
DR   GeneID; 3432219; -.
DR   KEGG; cjk:jk1354; -.
DR   PATRIC; fig|306537.10.peg.1374; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_11; -.
DR   OrthoDB; 9803211at2; -.
DR   Proteomes; UP000000545; 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; 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..556
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242010"
FT   MOTIF           130..140
FT                   /note="'HIGH' region"
SQ   SEQUENCE   556 AA;  60134 MW;  81C7B91329D71D1E CRC64;
     MTPAELSELI TETARTTLDA HGLDSSVVPE SATVERPRNP EHGDYATNIA MQVAKKAGTN
     PREFGTWLAE SLGAHEGIDE ATVAGPGFIN IRLAAAAQGK IVEDILTVGA NFGHGDELAG
     AAINLEFVSA NPTGPIHLGG TRWAAVGDSL GRVLNARGAK VTREYYFNDH GAQIDRFARS
     LVAAAKGEPT PEDGYGGDYI QDIASQIVEA NPDWQKLGAD EAQELFRSQG VELMFAHIKR
     TLAEFGTEFD VYFHENSLFE SGAVEAAIQK IKDNGNLYEA DGAWWLRSTN FGDDKDRVVI
     KSDGNAAYIA GDIAYVADKF DRGHNLCIYM LGADHHGYIA RLRAAAAAMG YDPQQVEVLI
     GQLVNLVKDG KAVRMSKRAG TVITLDDLVE AIGVDAARYA MIRSSVDSSL DIDMDLWASK
     SNDNPVFYVQ YAHARLCSLA RKAEDLGVTR EGADLSLLTH DREGDLIRTL GEFPAVVKTA
     AELREPHRVA RYAESLAGTF HRFYDACQIL PKPSDDEQTV AENKALFAAR LSLAAASRQT
     LANALELLGV AAPERM
//