SYR_HALWD
ID SYR_HALWD Reviewed; 596 AA.
AC Q18FC1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=HQ_3239A;
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001;
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA Pfeiffer F., Oesterhelt D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
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; AM180088; CAJ53337.1; -; Genomic_DNA.
DR RefSeq; WP_011572442.1; NC_008212.1.
DR AlphaFoldDB; Q18FC1; -.
DR SMR; Q18FC1; -.
DR STRING; 362976.HQ_3239A; -.
DR EnsemblBacteria; CAJ53337; CAJ53337; HQ_3239A.
DR GeneID; 4193716; -.
DR KEGG; hwa:HQ_3239A; -.
DR eggNOG; arCOG00487; Archaea.
DR HOGENOM; CLU_006406_6_1_2; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000001975; 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; 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..596
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018039"
FT MOTIF 127..137
FT /note="'HIGH' region"
SQ SEQUENCE 596 AA; 66431 MW; E71008C8B1183ED6 CRC64;
MFRPFRSEVE HAVESALQTL ALPTDDLGVE TPPEDVPATL ASSVAFRLAR SAKDSPPRVA
DDIAAAIDLE PDSQTYEYID HVDTRGPYIN FHVNDAYYMD TLTAAQDPGY GHLPNTGQSV
VVEHTSANPT GPVHVGRGRN TIFGDAVARL LEYNGDTVDR HYYLNDAGRQ VGVFTWAYEK
FDADSLPDPE RDRPDYDLVR YYRRGNEFLE NADADAVESA EDEIASIING LEAGNTETYE
RVQTVVDQVI DGMQHSFDRL SAIFDEFIKE TRFIQNGDAD AVVERLKSAD CAVYEDDAWQ
IDLSAYDIEK NLVFLRSDGT TLYTTRDLAH HEWKFDNYDA SVTILGEDHK LQAEQLDATL
QILGNDTDQL RQPFYSWVNL PEGGMSTRKG TGVDLDDLLD EAIARAREEV HDRLGSRVRD
DSLSSDDIDR IARQVGVGAV RYDIVSKQPT KGITFEWDRA LDFEAQSAPY IQYVHARCCG
IETEVNSNTD LDIDALTSDS IPDITMLRTD AERALLQEIA RFPAVVESAA ADLEPHVIAT
FARSFAEQFN TFYRECSVLN AESEIMTAAR VSLVRAARHT VANALDIVGV EAPQSM