SYR_BORHD
ID SYR_BORHD Reviewed; 584 AA.
AC B2S0U2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=BH0594;
OS Borrelia hermsii (strain HS1 / DAH).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=314723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 / DAH;
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; CP000048; AAX17098.1; -; Genomic_DNA.
DR RefSeq; WP_012422349.1; NC_010673.1.
DR AlphaFoldDB; B2S0U2; -.
DR SMR; B2S0U2; -.
DR KEGG; bhr:BH0594; -.
DR HOGENOM; CLU_006406_6_1_12; -.
DR OMA; NKPLHLG; -.
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_1000095336"
FT MOTIF 127..137
FT /note="'HIGH' region"
SQ SEQUENCE 584 AA; 67429 MW; 4536CDFA4D5D8658 CRC64;
MNSKIKKDLK DIISKTIKEL ALRESIKLEE INIIMQKPPK SELGDLSILI FEFSKILKLN
TSIITEEIIK QIGDKYATKA MGPYLNIKFN RKEYIKDTIK KVNEQKEKYG INNVLKNKRI
IIEFSSPNTN KPLHIGHLRN DIIGESLSRI LKASGAQVTK INLINDRGTH ICKSMLAYKK
FGNNTTPELS LKKGDHLIGD FYVKYNEYAK NNEMAEDEIQ QLLCKWEEGD EKTVQLWKKL
NQWAIEGIKA TYKLTNITFD KIYLESEIFK IGREIILKGL EEGLCYKRED GAICIDIPTE
KNEISEQQFK QKVLLRANGT SIYLTQDLGN IVTRKNEFDF DEMIYVVGSE QIHHFKTLFY
VANKLGITKE NNLVHLSYGM VNLPEGKMKS REGNVIDADN LIHDLSESII LEIKKRNSDK
KDYQEIALNI SLGAIHYYLL KTAIHKDILF NKEESLSFTG NSGPYIQYVG ARINSILEKY
DELNLSNETI NFDLLVNENE WEIIKIISEF EEHIIKASKD RNPSVIANYS YLLAKSFSTY
YQDTKIIDKN KPELTHARID LSKAVLQTIK NCMHLLNIPY MKKM