SYR_BORT9
ID SYR_BORT9 Reviewed; 584 AA.
AC A1R025;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 25-MAY-2022, 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=BT0594;
OS Borrelia turicatae (strain 91E135).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=314724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91E135;
RA Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA Schwan T.G.;
RT "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT comparative analysis of two agents of endemic N. America relapsing fever.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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; CP000049; AAX17917.1; -; Genomic_DNA.
DR RefSeq; WP_011772535.1; NC_008710.1.
DR AlphaFoldDB; A1R025; -.
DR SMR; A1R025; -.
DR STRING; 314724.BT0594; -.
DR KEGG; btu:BT0594; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_6_1_12; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000001205; 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; 1.
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.
FT CHAIN 1..584
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000198876"
FT MOTIF 127..137
FT /note="'HIGH' region"
SQ SEQUENCE 584 AA; 67356 MW; 566B4123FB1BD2EE CRC64;
MISKIKKDLE NKISKTIKEL ALKQNITLDK INIIMKKPPK SELGDLSILI FEFSKILKLS
TSVIIEEIIK QIGKKYTTKS MGAYLNIKFN RKEYIKDIIK KVNEQKEKYG INNVLKNKRI
IIEFSSPNTN KPLHVGHLRN DIIGESLSRI LKASGGQVTK INLINDRGTH ICKTMLAYKK
FGNNTTPELS LKKGDHLIGD FYVKYNEYAK NNKMAEDEIQ QLLCKWEEGD EETVKLWKKL
NKWAIEGIKE TYKLTNITFD KIYLESEIFK IGREIILQGL EKGLCYKRED GAICINIPIE
TNEMTDQKFK QKVLLRANGT SIYLTQDLGN ILTRKNEFDF DEMIYVVGSE QIHHFKTLFY
VADKLGITKE NNLVHLSYGM VNLPTGKMKS REGHVIDADN LIHDLSESTM IEIKKRHSNE
QDSKKIALNI SLGAIHYYLL KTAIHKDILF NKEESLSFTG NSGPYIQYVG ARINSILDKY
DELNLPSKNI NFDLLINENE WAIIKIISEF EEYIIKAAKD RNPSIIVNYS YLLAKSFSAY
YQDTKIIDKD NPELTHARTD LSKAVLQTIK NCMHLLNIPY MKKM