ID SYR_BORDL Reviewed; 585 AA.
AC B5RME6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=BDU_595;
OS Borrelia duttonii (strain Ly).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borrelia.
OX NCBI_TaxID=412419;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ly;
RX PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL PLoS Genet. 4:E1000185-E1000185(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; CP000976; ACH93532.1; -; Genomic_DNA.
DR AlphaFoldDB; B5RME6; -.
DR SMR; B5RME6; -.
DR STRING; 412419.BDU_595; -.
DR KEGG; bdu:BDU_595; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_6_1_12; -.
DR OrthoDB; 9805987at2; -.
DR Proteomes; UP000000611; 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.
FT CHAIN 1..585
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000095335"
FT MOTIF 127..137
FT /note="'HIGH' region"
SQ SEQUENCE 585 AA; 67249 MW; CE96893EF201D2AE CRC64;
MIKTIKADLK NKIQKTIKEL ALSSNIKLDK INIVMQKPPK SEMGDLSILI FEFSKILKLS
IPVITQEIIK QIGNEYKTKS MGPYLNIKFN RKEYIQNTIK KVNKEKENYG ANNSLQNKKT
IIEFSSPNTN KPLHVGHLRN DIIGESLSRI LKASGSKVTK INLINDRGTH ICKSMLAYKK
FGNNITPEIA QKKGDHLIGD FYVKYNEYAS QNSEIAENEI QQLLCQWEQG DEKTVQLWTK
LNKWAIDGIK ETYNTTNITF DKIYLESEIF KIGREVVING LKEGLCYKRE DGAICINIPT
EKNNIDNQNF KQKVLLRANG TSIYLTQDLG NIVARKNEFD FDEMIYVVGS EQIHHFKTLF
YVADKLGVTN ENNLIHLSYG MVNLPEGKMK SREGNIIDAD NLIHDLSQST MLELKKRYEN
EQNLQKLALN ISLGAIHYYL LKTAIHKDIL FNKTESLSFT GNSGPYIQYV GARINSILDK
YNNLNLANKN TNFDLLVNEN EWEIIKIISE FEEYIIKASK DRNPSIIANY SYLLAKNFST
YYQDTKIIDK DNLELTHARI DLAKAVLQTI KNCMHLLNIP YIQKM
//
