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
//
