ID   SYR_BDEBA               Reviewed;         580 AA.
AC   Q6MLI2;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=Bd2027;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(2004).
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; BX842651; CAE79875.1; -; Genomic_DNA.
DR   RefSeq; WP_011164477.1; NC_005363.1.
DR   AlphaFoldDB; Q6MLI2; -.
DR   SMR; Q6MLI2; -.
DR   STRING; 264462.Bd2027; -.
DR   PRIDE; Q6MLI2; -.
DR   EnsemblBacteria; CAE79875; CAE79875; Bd2027.
DR   KEGG; bba:Bd2027; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_7; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000008080; 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   Gene3D; 3.30.1360.70; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..580
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000241990"
FT   MOTIF           127..137
FT                   /note="'HIGH' region"
SQ   SEQUENCE   580 AA;  65364 MW;  F4A9AA2260E1B08D CRC64;
     MIKHDSIRLL ATNLLKDAIG RAYPDFSASE DDIYKALVNP PKSDLGDLAF GCFILAKALK
     TAPPQVATAV AAQMKGATAV AAGPYINIRF DEQTHGEQVL ATILDGSYFK KPLMEKSPKT
     MIEYSQPNTH KELHVGHMRN LCLGDAIVRM LRYSGREIVS STFPGDMGTH VAKCLWYMKK
     HNQEPVPETE KGEWLGRMYS KANLLLEDQN GTPQEDINRQ ELTAILHQLE GKTGPYYDLW
     LETREWSIEL MKKVYAWADV TFDEWYFESE MDSPSAAWVK QLYAEGKLEM SQGAIGKDLE
     SEKLGFCMLL KSDGTGLYAT KDLLLAKHKF EDVKIEKSVY VVDMRQALHF KQVFRVLEIL
     GFEQAKNCFH LQYNYVELPD GAMSSRKGNI VPLRELVHRM EDHVKTTYLS RYKGEWSEED
     VEKIAGQVAK GAIFYGMLRM DTNKKIVFDM NEWLKLDGES GPFVQYSYAR ISSLGRKFPR
     TAGAKIDWSR LNHASERQLM QSLGGFNTAV AAAAENFKPS AICTYLYDLA KSFNVFYHEC
     PIGTEADVAT REARLALSEA VGLTLKNGLA VLGMPAPEKM