ID   SYR_HALMA               Reviewed;         579 AA.
AC   Q5UXX8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=rrnAC3169;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(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   -!- 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY596297; AAV47875.1; -; Genomic_DNA.
DR   RefSeq; WP_011224649.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UXX8; -.
DR   SMR; Q5UXX8; -.
DR   STRING; 272569.rrnAC3169; -.
DR   EnsemblBacteria; AAV47875; AAV47875; rrnAC3169.
DR   GeneID; 40153977; -.
DR   KEGG; hma:rrnAC3169; -.
DR   PATRIC; fig|272569.17.peg.3709; -.
DR   eggNOG; arCOG00487; Archaea.
DR   HOGENOM; CLU_006406_6_1_2; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000001169; 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; 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..579
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242128"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   579 AA;  64318 MW;  9E99E129A6C5B57F CRC64;
     MFLQLRAEVE DALADALTTL DLPAEDLGIE EPPEDVDAVL ASSVAFRLAG EVGTAPPNVA
     SDIADAIAAD DLTYVSDVTT QGPYVNFLPS EAYFAETLQS VTESGFGRLP DRDTSVVVEH
     TSANPTGPVH VGRARNPIIG DAVARVLDYA GYDVDRHYYV NDAGRQIAVF TWAYETFDED
     DLPEPERESP EYEMVRYYRK GNTILEDGDP DEVEAAEAEV QSILQGLEDG DEETYERVAE
     VVDTVLGGMQ NTLGRLPAEF DEFVKETKFM RNGDTDDLVD RLKGLDCAVY EEDAWQLDLP
     DFEKNLVFLR SDGTSLYTTR DLAHHEWKFD TYDRAVTVLG EDHKLQADQL AAALELLDND
     TDQLRQVFYS WVNLPEGGMS TREGTGIDLD DLLDEAIDRA REEVESRLDD RTRGDLDEDD
     IDRIARQVGI GAVRYDIVSK QPTKGITFEW DRALDFEAQS APYVQYVHAR CCGILGDVET
     DIPDEPDLDP LSEPEERDLL RELARFPAVI EAAADDLTPH TVATYTRDLA ETFNAFYREC
     PVLDADPETR AARLALVDGT RTTIANALDA LGVEAPTSM