ID   SYH_HALWD               Reviewed;         434 AA.
AC   Q18DQ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Histidine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00127};
DE            EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE   AltName: Full=Histidyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00127};
DE            Short=HisRS {ECO:0000255|HAMAP-Rule:MF_00127};
GN   Name=hisS {ECO:0000255|HAMAP-Rule:MF_00127}; OrderedLocusNames=HQ_1107A;
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-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-
CC         histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665,
CC         Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00127};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00127}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00127}.
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DR   EMBL; AM180088; CAJ51237.1; -; Genomic_DNA.
DR   RefSeq; WP_011570403.1; NC_008212.1.
DR   AlphaFoldDB; Q18DQ2; -.
DR   SMR; Q18DQ2; -.
DR   STRING; 362976.HQ_1107A; -.
DR   EnsemblBacteria; CAJ51237; CAJ51237; HQ_1107A.
DR   GeneID; 4194126; -.
DR   KEGG; hwa:HQ_1107A; -.
DR   eggNOG; arCOG00404; Archaea.
DR   HOGENOM; CLU_025113_3_1_2; -.
DR   OMA; CDFDFIG; -.
DR   Proteomes; UP000001975; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   CDD; cd00859; HisRS_anticodon; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_00127; His_tRNA_synth; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR015807; His-tRNA-ligase.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR004516; HisRS/HisZ.
DR   InterPro; IPR033656; HisRS_anticodon.
DR   PANTHER; PTHR43707; PTHR43707; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00442; hisS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..434
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_1000016371"
FT   REGION          412..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  47812 MW;  9EC36562551E054C CRC64;
     MYDRLKGFRD FYPPEMTARR QVIDILETTA TQYGFREVGT PTLEQTQMYV DKSGEGIEEE
     LYAFSDDGGR DVTLIPELTP TVARMVVDKQ QALSKPIKWV STRPFWRYEQ VQQGRFREFY
     QTNVDIFGTA DPIADAEILA FAADALRNLG LTASDFEFRV SHRDILSGLL ASITNDDADI
     DTRAAIRAVD KRAKIEQAEY HGLLTDAGLS YDQAQSFDDL LTTADLDEIA TVGNDIVTTA
     VQNLRSVLAA VDDLGVGEFC DISLTTARGL DYYTGVVFEC FDATGEVSRS VFGGGRYDNL
     IESFGGQPTP AVGVAPGLAP LSLLCQRAGV WPTEELTTDY YILTVGDTRS VATRIARELR
     VNKNTVEIDI ADRSFGAQMG YADSINAETV IIVGERDLEN DEITIKDMNS GDQTTVPVEA
     FPGDHDAPTY EDVV