ID   SYR_BIFLD               Reviewed;         620 AA.
AC   B3DPJ1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   10-JUN-2026, entry version 76.
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};
GN   OrderedLocusNames=BLD_1605;
OS   Bifidobacterium longum (strain DJO10A).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=205913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A;
RX   PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA   Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA   Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA   Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT   "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT   reveals loci susceptible to deletion during pure culture growth.";
RL   BMC Genomics 9:247-247(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Arg) + L-arginine + ATP = L-arginyl-tRNA(Arg) + AMP +
CC         diphosphate; 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; CP000605; ACD99050.1; -; Genomic_DNA.
DR   RefSeq; WP_010081268.1; NC_010816.1.
DR   AlphaFoldDB; B3DPJ1; -.
DR   SMR; B3DPJ1; -.
DR   KEGG; blj:BLD_1605; -.
DR   HOGENOM; CLU_006406_0_1_11; -.
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   FunFam; 3.40.50.620:FF:000062; Arginine--tRNA ligase; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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; 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..620
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000095334"
FT   MOTIF           147..157
FT                   /note="'HIGH' region"
SQ   SEQUENCE   620 AA;  67292 MW;  14953760A3126BEC CRC64;
     MSPEALSELI SSIAHNLVAA GQAGALTDEL IPPVDKLAVM RPKDRAHGDW ASNIAMQLAK
     KAGMKPRDLA EPFAAALAEA DGIAKVEVAG PGFINITLDS ASAAAVVDTV LAAGAMTDTD
     KHLNKVNEYG RNAHLGGQTL NLEFVSANPT GPIHIGGTRW AAVGDAMARV LEANGAKVVR
     EYYFNDHGEQ INRFAKSLVA AWAEANNLGE AGYQTETPCD GYKGAYINEI AARVQAEAES
     DGVDLTALAH QDQGLNDDGE PLGEADTEVR EEFRKRAVPM MFDEIQKSMK DFRVNFDVWF
     HENSLYADGK VDAAIEELKS RGDIFDKDGA TWFESTKHGD DKDRVIIKSN GEFAYFAADI
     AYYWDKRHRA ENPADVAIYM LGADHHGYIG RMMAMCAAFG DEPGKNMQIL IGQLVNVMKD
     GKPVRMSKRA GNVVTIDDLV SVVGVDAARY SLARSDYNQN FDIDLALLAS HTNDNPVYYV
     QYAHARSKNV DRNAAVAGIS YEGADLALLD TEADGEVLAA LAQFPSVLAT AADDRQPHKV
     ARYLEELAAT YHKWYNVERV VPMALTDPET RGDDEARKAL EIAKNPEPAR AAARLKLNDA
     VQQVIANGLD LLGVTAPEKM
//