ID   SYR_SYNJA               Reviewed;         598 AA.
AC   Q2JRC3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   28-JAN-2026, entry version 94.
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=CYA_2732;
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS   A-Prime).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=321327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-3-3Ab;
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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; CP000239; ABD00836.1; -; Genomic_DNA.
DR   RefSeq; WP_011431507.1; NC_007775.1.
DR   AlphaFoldDB; Q2JRC3; -.
DR   SMR; Q2JRC3; -.
DR   STRING; 321327.CYA_2732; -.
DR   KEGG; cya:CYA_2732; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_3; -.
DR   OrthoDB; 9805987at2; -.
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   FunFam; 3.40.50.620:FF:000062; 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.
FT   CHAIN           1..598
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242107"
FT   MOTIF           140..150
FT                   /note="'HIGH' region"
SQ   SEQUENCE   598 AA;  66889 MW;  C22447499B99F9B9 CRC64;
     MATQPLSTSL VRFLTAAVSE SIRRASEAGQ LGSLTLEQAA GVAPTIQIPS DPRYGDYACP
     TPLGMAKLCR MAPAQIAQTL QKHLDLPGIA TEVAGGGYLN FRLGDSFLAE RLQELLRLGE
     DFGKTAAPHP ERILLEYVSA NPTGPLHVGH GRWAAVGSTL ANLLRWTGHQ VEREFYINDA
     GNQMRLLGQS LEVRVRQLQG EEVALPEDAY HGSYLVDIAR RLLDQVKAGI RPLPTTPEEY
     TDFAYAEMLA WQKQTLQQLR TEFDHWFSER RLHAPDPQTG LSAIQQALQE LQERGFLYRA
     KAPRGEDPKP GAEEAVYFKT QEFGDDKDRV VQKADGSFTY LAADIAYHRD KVRRGYQRLI
     NILGSDHHGY IGRLHAAVGA FSPDVKLEIL IGQFVKLFKT DPETGEKTEV RMSKRTGNFV
     SLNDLIDDPE IGVGVDAARW FLLSSSMDSP INFDLDLAVK QTFDNPVVYV HYSHARCCTL
     LRRLQEEEKV ELTNKVTLTE QQKLPYQEPE ERALLLRLLA LPDELIAAAE ERAPHKIIRY
     AEAIAADFNK FYDNCRILPL LKEDPLLAQA RIQLVQATRQ VLFNVLTGIL GLSAPESM
//