ID   SYR_KINRD               Reviewed;         554 AA.
AC   A6W7E9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Krad_1250;
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; Kineococcus.
OX   NCBI_TaxID=266940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RX   PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA   Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA   Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT   "Survival in nuclear waste, extreme resistance, and potential applications
RT   gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL   PLoS ONE 3:e3878-e3878(2008).
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; CP000750; ABS02738.1; -; Genomic_DNA.
DR   RefSeq; WP_012084406.1; NC_009664.2.
DR   AlphaFoldDB; A6W7E9; -.
DR   SMR; A6W7E9; -.
DR   STRING; 266940.Krad_1250; -.
DR   EnsemblBacteria; ABS02738; ABS02738; Krad_1250.
DR   KEGG; kra:Krad_1250; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_11; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000001116; 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; -; 1.
DR   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR11956; PTHR11956; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 2.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM01016; Arg_tRNA_synt_N; 1.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF55190; SSF55190; 1.
DR   TIGRFAMs; TIGR00456; argS; 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..554
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000076218"
FT   MOTIF           132..142
FT                   /note="'HIGH' region"
SQ   SEQUENCE   554 AA;  60028 MW;  572FFB65CF17E283 CRC64;
     MTPAELSAAL RDALTAAVAA GELTLDPADV PAEVRVERPK NRDHGDWATS VALQLAKKAG
     LPPREVAALV QRRLLEVEGV RAVDIAGPGF LNVTLDAAAA GELARSVVEA GPAFGRSATP
     TGERINLEFV SANPTGPIHL GGTRWAAVGD SLARVLEAAG ATVTREYYFN DHGAQIDRFA
     RSLLARANDE PAPEDGYGGD YVTDIAAAVL AEAPGLLDLP REEQQEVFRR EGVELMFAEI
     RQSLAEFGVE FDVYFHEDSL HTSGAVGRAV QKLRDLGRIY EADGATWLRT SDFGDDKDRV
     VIKSDGHPAY ISGDLAYYLD KRERGFDRCV LMLGADHHGY VPRMMAMCAA FGDTPGVNLE
     ILIGQMVNLL KDGVPVRMSK RAGTVVTMED LVEAVGVDAA RYSLVRSSVD SSIDIDLDLL
     TRRSNDNPVF YVQYAHARTA NVAVNAAAAG VRREDAFDPS LLTEETESLL LAALAEFPAV
     VARAGELREP HRVARYLEEL AGRFHKFYDA CRVTPRAGEE VTDVHRTRLW LNDATRQVLA
     NGLGLLGVSS PDRM