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SYR_DEIRA
ID   SYR_DEIRA               Reviewed;         609 AA.
AC   Q9RRC4;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 117.
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=DR_2568;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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; AE000513; AAF12109.1; -; Genomic_DNA.
DR   PIR; B75257; B75257.
DR   RefSeq; NP_296288.1; NC_001263.1.
DR   RefSeq; WP_010889193.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RRC4; -.
DR   SMR; Q9RRC4; -.
DR   STRING; 243230.DR_2568; -.
DR   EnsemblBacteria; AAF12109; AAF12109; DR_2568.
DR   KEGG; dra:DR_2568; -.
DR   PATRIC; fig|243230.17.peg.2813; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_0; -.
DR   InParanoid; Q9RRC4; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
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   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..609
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151556"
FT   MOTIF           114..124
FT                   /note="'HIGH' region"
SQ   SEQUENCE   609 AA;  66604 MW;  5F482073018397BB CRC64;
     MDLKAQLKAA VEQAAHQMGM PVDAAIQETP ANKPGDYGTP AAFQMAKAAG GNPAQIAAQL
     AQTVVLPAGI RRVEATGPFL NFFLDAGAFV RGVVERPFEL PKREGKVVIE HTSVNPNKEL
     HVGHLRNVVL GDSMARILRA AGHTVEVQNY IDDTGRQAAE SLFATQHYGR VWDGVQKYDQ
     WLGEGYVQLN ADPQKPELES GIMEIMHKLE AGELRPLVEQ TVKAQLQTCF RLGARYDLLN
     WESDVVGSGF LAQAMNILEG SRYTSRPTEG KYAGAFIMDV SEFMPGLEEP NVVLVRSGGT
     AMYAAKDIGY QFWKFGLFEG MKFKPFMQDP EGNTIWTSAP DGQPDDERRF GHAQEVINVI
     DSRQDHPQTV VRSALGVAGE QEKEERSIHL SYAFVTLEGQ TISGRKGIAV SADDAMDEAQ
     KRALSVLQGI NPDLAAREDA AEIARRIGLG AIRFAMLKAE PTRKIDFRWE QALALNGDTA
     PYVQYAAVRA ANILKKAEEA GYATDGTGAD WDALPDIDLV LAKQIAKLPE VAAQAARIHS
     PHVVAQYALD LATSFNAWYN AKTKQGKPAT NVLQSEEGLR EARLALIVRL RKAFEDTLDL
     IGIEIPAAM
 
 
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