ID   SYR_ALKMQ               Reviewed;         566 AA.
AC   A6TNX2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=Amet_1714;
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF;
RX   PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
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; CP000724; ABR47890.1; -; Genomic_DNA.
DR   RefSeq; WP_012062928.1; NC_009633.1.
DR   AlphaFoldDB; A6TNX2; -.
DR   SMR; A6TNX2; -.
DR   STRING; 293826.Amet_1714; -.
DR   EnsemblBacteria; ABR47890; ABR47890; Amet_1714.
DR   KEGG; amt:Amet_1714; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_9; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000001572; 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..566
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000198868"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   566 AA;  64448 MW;  F9D4CEF14B37CAB2 CRC64;
     MSDFKQKVSE LLGTQIEGIG QRELLEMIEV PPNSEMGDFA FPCFRLAKTF RKAPQVIAEE
     LVAKIQLTDD FEKVDNTGGY LNFFVNRNTY AKAVIQEVLS KGDQYGSRNL GEGKNICIDY
     SAPNVAKPFH VGHLRSTVIG NSLYRIYDFL GYNCIGINHL GDWGTQFGKV IVAYKNWGDK
     AEIEKEPINT LLALYVKFHD EAEKNPDLED EARGWFTKME KGDEEALSLW KWFSSETIKE
     LKKIYALLDV HFDHYSGESF YNDKMDVVID ELNKQNLLKE SQGANIVDLE EYNMPPCLVQ
     KKDGSTLYAT RDIAAAIYRK NTFNFEKCLY VTDYSQNLHF AQWFKVIELM GYDWAKDIEH
     ISFGRVTHEG RRIQSRKGSV VLLEEVLNGA VERISEIIEE KNPNVENKEQ VAKDVGIGAI
     VFNDLSNNRI KDISFSWDTA FSFEGETGPY VQYTHARASS VLRKAEVAIT DHINAAHLTD
     DVTMNVIKTI EQFPQVIVDA QRKNEPSIIT RHIVNIAQAF NRFYHDHPIL VEDEELKMAR
     LAVVQAVKQV LSVGLSLIGI KAPEKM