ID   SYR_BIFLO               Reviewed;         620 AA.
AC   Q8G4V2;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=BL1272;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN25073.1; -; Genomic_DNA.
DR   RefSeq; NP_696437.1; NC_004307.2.
DR   RefSeq; WP_011068711.1; NC_004307.2.
DR   AlphaFoldDB; Q8G4V2; -.
DR   SMR; Q8G4V2; -.
DR   STRING; 206672.BL1272; -.
DR   EnsemblBacteria; AAN25073; AAN25073; BL1272.
DR   KEGG; blo:BL1272; -.
DR   PATRIC; fig|206672.9.peg.1559; -.
DR   HOGENOM; CLU_006406_0_1_11; -.
DR   OMA; NKPLHLG; -.
DR   PhylomeDB; Q8G4V2; -.
DR   Proteomes; UP000000439; 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; Reference proteome.
FT   CHAIN           1..620
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151532"
FT   MOTIF           147..157
FT                   /note="'HIGH' region"
SQ   SEQUENCE   620 AA;  67206 MW;  F51C3C0C8CD9AB06 CRC64;
     MSPEALSELI SSIAHNLVAA GQAGALTDEL IPPVDKLAVM RPKDRAHGDW ASNIAMQLAK
     KAGMKPRDLA EPFAAALAEA DGIAKVEVAG PGFINITLDS ASAAAVVDAV LAAGAVTDAD
     KHLNKVNEYG RNDHLGGQTL NLEFVSANPT GPIHIGGTRW AAVGDAMARV LEANGAKVVR
     EYYFNDHGEQ INRFAKSLVA AWAEANNLGE AGYQTETPCD GYKGAYINEI AARVQAEAES
     DGVDLTALAH QDQGLNDDGE PLGEADTEVR EEFRKRAVPM MFDEIQKSMK DFRVNFDVWF
     HENSLYADGK VDAAIEELKS RGDIFDKDGA TWFESTKHGD DKDRVIIKSN GEFAYFAADI
     AYYWDKRHRA ENSADVAIYM LGADHHGYIG RMMAMCAAFG DEPGKNMQIL IGQLVNVMKD
     GKPVRMSKRA GNVVTIDDLV SVVGVDAARY SLARSDYNQN FDIDLALLAS HTNDNPVYYV
     QYAHARSKNV DRNAAAAGIS YEGADLALLD TEADGEVLAA LAQFPSVLAT AADDRQPHKV
     ARYLEELAAT YHKWYNVERV VPMALTDPET RGDDEARKAL EIAKNPEPAR AAARLKLNDA
     VQQVIANGLD LLGVTAPEKM