ID   SYR_HALSA               Reviewed;         631 AA.
AC   Q9HHN2;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 125.
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=VNG_6312G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OG   Plasmid pNRC200.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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   -!- 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; AE004438; AAG20944.1; -; Genomic_DNA.
DR   RefSeq; WP_010904157.1; NZ_BK010831.1.
DR   AlphaFoldDB; Q9HHN2; -.
DR   SMR; Q9HHN2; -.
DR   EnsemblBacteria; AAG20944; AAG20944; VNG_6312G.
DR   GeneID; 5954981; -.
DR   GeneID; 62888212; -.
DR   KEGG; hal:VNG_6312G; -.
DR   PATRIC; fig|64091.14.peg.2290; -.
DR   HOGENOM; CLU_006406_6_1_2; -.
DR   InParanoid; Q9HHN2; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 7046at2157; -.
DR   PhylomeDB; Q9HHN2; -.
DR   Proteomes; UP000000554; Plasmid pNRC200.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
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   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Plasmid; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..631
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151644"
FT   MOTIF           132..142
FT                   /note="'HIGH' region"
SQ   SEQUENCE   631 AA;  70471 MW;  1BF5F0A47AF1B30E CRC64;
     MLYNLRQELL AGIRAATSDA GYDYEVDQSA IELEDITDEE KGEFSSPISF SIAAAAGAPP
     VDVAAAIADA HRSNGLPAEV EAVTVEGGHI NYHADTTDLA DATLSTILRD GSEYGTRTDA
     DPDTILADVS SPNIAKPLHV GHLRNTILSD AVMNILEARG HDVTRDNHLG DWGVQFGNLM
     HEYTEFGDEA TLEDDAIEHL LDLYQQFEQR DSMLADLEDD ETVTDQFADA VTEERDYHAD
     SGKEWFTRLE QGDEDATALW ERFRTVSIDR FKQTYDDLDV AFDVWNGESF YAQEGWNDVI
     IEKAIENDVA MRGEGESVYI PVYPDDYENV GDPQAADVDA SLDRARQMRE ANDDLEDADF
     DPFYIVKSDG STLYGTRDLA TIEYRIEEYD ADQSVYVVAN EQNQYFQQLF VAARKMGYND
     IKLKHIDYGL ISLPEGSMST RKGQIITARE VLDRAQDRAE EIIAEKGRID DAEAQSVATK
     IALATIKYEM VAAKRERDTT FDIDESVALE GDTGPYVQYA ATRGYSILDG ADAAPEIDDL
     DPSVFNDTDV ELLFELARYP LVLERCEERY DAAPLAHYLL QLAHVFNSFY HKNAVLDAEN
     ARTERLLLTK ATTQIFDNGL GLLGIDVLEE M