ID   SYH_AQUAE               Reviewed;         403 AA.
AC   O66522;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Histidine--tRNA ligase;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidyl-tRNA synthetase;
DE            Short=HisRS;
GN   Name=hisS; OrderedLocusNames=aq_122;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000657; AAC06477.1; -; Genomic_DNA.
DR   PIR; G70311; G70311.
DR   RefSeq; NP_213082.1; NC_000918.1.
DR   RefSeq; WP_010880020.1; NC_000918.1.
DR   AlphaFoldDB; O66522; -.
DR   SMR; O66522; -.
DR   STRING; 224324.aq_122; -.
DR   PRIDE; O66522; -.
DR   EnsemblBacteria; AAC06477; AAC06477; aq_122.
DR   KEGG; aae:aq_122; -.
DR   PATRIC; fig|224324.8.peg.105; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_1_1_0; -.
DR   InParanoid; O66522; -.
DR   OMA; CDFDFIG; -.
DR   OrthoDB; 277998at2; -.
DR   Proteomes; UP000000798; 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; IBA:GO_Central.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
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..403
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136091"
SQ   SEQUENCE   403 AA;  46411 MW;  2ECE1B92857E01D0 CRC64;
     MNIQSVRGFH DILGKDAKKF RKISDTARKI LKLYNFEEII LPVVEYAELF QRSVGETTDI
     VQKEMFVFED RKGRKLALRP EGTAGTVRAF IQHKLYALRP YVKLFYEGPM FRYERPQAGR
     YRQFHQIGAE VFGVAEPHAD AEIIKIVYDI LQALGIKGVV VEINSLGCKK DREAYREALL
     NYLTGVKEEL CSDCISRMDR NPLRVLDCKV ETCKVAVREA PKMIDFLCDE CREHYEKLKN
     YLKALDIPFR ENYNLVRGLD YYTRTVFEAV SDELGLTLIA GGRYDYLVEE LGGPPTPALG
     FALGVERLML LLPDEEEKEE VYFVIPFGDV HEYALRVADI LRKKGKVVEY SYRKGGLKKQ
     LEFADKLGVK YAVIIGEDEV KNQEVTIKDM ETGEQRRVKL SEL