ID   SYR_ALIFM               Reviewed;         577 AA.
AC   B5FC42;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=VFMJ11_0877;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) 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; CP001139; ACH65193.1; -; Genomic_DNA.
DR   RefSeq; WP_012532885.1; NC_011184.1.
DR   AlphaFoldDB; B5FC42; -.
DR   SMR; B5FC42; -.
DR   EnsemblBacteria; ACH65193; ACH65193; VFMJ11_0877.
DR   KEGG; vfm:VFMJ11_0877; -.
DR   HOGENOM; CLU_006406_5_1_6; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000001857; Chromosome I.
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..577
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000095418"
FT   MOTIF           122..132
FT                   /note="'HIGH' region"
SQ   SEQUENCE   577 AA;  64080 MW;  BBF9496E3E7ADED3 CRC64;
     MNIQSLINDK VSQALEAAGA PAGSPAAVRQ SAKAQFGDYQ ANGVMGVAKR LGTNPREFAQ
     KVLDVLDLDG IASKTEIAGP GFINIFLSEE FLAKQAEAAL ADKRLGVAKE EQQNIVADYS
     APNVAKEMHV GHLRSTIIGD AVVRTLEFLG HNVTRANHIG DWGTQFGMLI ANLERIQKEK
     GEVSMELSDL EGFYRESKKL YDEDEEFAVT ARGYVVKLQS GDEFCAEMWK KLVDVTMVQN
     QRNYDRLNVS LTRDNVMGES MYNSMLAPIV ADLQKQGLAV ESEGAQVVFL DEYKNKDGEP
     MGVIVQKRDG GFLYTTTDIA CAKYRYEELN ADRVLYFIDS RQHQHLMQAW TIVRKAGYVP
     ESVSLEHHAF GMMLGKDGRP FKTRAGGTVR LADLLDEAEE RAAKLIEEKN KDLPAEEKAK
     IATTVAMAAV KYSDLSKHRT TDYIFDWDNM LAFEGNTAPY MQYAYTRVAS IFSKAGLSMD
     ELTGEVKITD EKEKALVAKL MQFEEAVQAV ASEGQPHLMC AYLFELAGQF SSFYEACPIL
     NNEDDAVKQS RLKLAALTAK TIKQGLELLG IETLERM