SYR_BIFA0
ID SYR_BIFA0 Reviewed; 598 AA.
AC B8DWR0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=BLA_0618;
OS Bifidobacterium animalis subsp. lactis (strain AD011).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=442563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD011;
RX PubMed=19011029; DOI=10.1128/jb.01515-08;
RA Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT lactis AD011.";
RL J. Bacteriol. 191:678-679(2009).
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; CP001213; ACL28911.1; -; Genomic_DNA.
DR RefSeq; WP_004269231.1; NC_011835.1.
DR AlphaFoldDB; B8DWR0; -.
DR SMR; B8DWR0; -.
DR STRING; 442563.BLA_0618; -.
DR EnsemblBacteria; ACL28911; ACL28911; BLA_0618.
DR GeneID; 66533749; -.
DR KEGG; bla:BLA_0618; -.
DR HOGENOM; CLU_006406_0_1_11; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000002456; 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..598
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000198874"
FT REGION 229..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 135..145
FT /note="'HIGH' region"
SQ SEQUENCE 598 AA; 65586 MW; 7D962679DCF11F41 CRC64;
MSPEALQELI FTIANNLVSE GKAGTLTAEE LPDSAKFAVM RPKDRAHGDW ASNAAMQLAK
KAGMKPRDLA QLFADALNGT DGIAAVEVAG PGFINITLDS ASAAAVVDQV LDEGNRFGKN
NHLSGKTLNL EFVSANPTGP IHIGGTRWAA VGDSMARILQ ANGATVVREY YFNDHGEQIN
RFAKSLVAAA HDEPTPVDGY KGAYIDEIAR RVIVEANAEG IDILNLPRVD GGTDEKGEPL
GEGDSEQREE FRKRAVPMMF DEIRQSMKEF RVHFDVWFHE NSLYEDGEVE KAIADLRNAG
DIYEKDGATW FESTEHGDDK DRVIIKSDGT YAYFAADIAY YRNKRHRKTD PADVAIYMLG
ADHHGYIGRM MAMCAAFGDK PGENMQILIG QMVNVMKDGK PVRMSKRAGN IVTIDDLIDA
IGVDASRYSL ARTDYNSPVD IDLNLLASHS NDNPVYYVQY AHARSCNVDR NAEAAQINAA
DADLSLLDTE ADGEVIAALA QWPALLTLAG DLRAPHRIAH YLEDLAAAYH KWYNVERVVP
MPLTEAEERA DEQTRERTRI AKNPEPARAA ARLKLNDAVQ TVIAEGLDLL GVTAPDKM