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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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