ID   SYH_BACTN               Reviewed;         454 AA.
AC   Q8A6N7;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=BT_1840;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO76947.1; -; Genomic_DNA.
DR   RefSeq; NP_810753.1; NC_004663.1.
DR   RefSeq; WP_008767712.1; NZ_UYXG01000014.1.
DR   AlphaFoldDB; Q8A6N7; -.
DR   SMR; Q8A6N7; -.
DR   STRING; 226186.BT_1840; -.
DR   PaxDb; Q8A6N7; -.
DR   PRIDE; Q8A6N7; -.
DR   EnsemblBacteria; AAO76947; AAO76947; BT_1840.
DR   GeneID; 60927829; -.
DR   KEGG; bth:BT_1840; -.
DR   PATRIC; fig|226186.12.peg.1889; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_3_0_10; -.
DR   InParanoid; Q8A6N7; -.
DR   OMA; YQIQKVW; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF13393; tRNA-synt_His; 2.
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..454
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136110"
SQ   SEQUENCE   454 AA;  50397 MW;  8EEE5279CFAA5C92 CRC64;
     MAAKPSIPKG TRDFSPVEMA KRNYIFNTIR DVYHLYGFQQ IETPSMEMLS TLMGKYGDEG
     DKLLFKIQNS GDYFSGITDE ELLSRNAVKL ASKFCEKGLR YDLTVPFARY VVMHRDEITF
     PFKRYQIQPV WRADRPQKGR YREFYQCDAD VVGSDSLLNE VELMQIVDTV FSRFNIRVCI
     KINNRKILSG IAEIIGEADK IVDITVAIDK LDKIGLENVN AELKEKGISD EAIAKLQPII
     LLSGTNTEKL ATLKSVLAAS ETGMKGVEES EFILGTLETM GLKNEIELDL TLARGLNYYT
     GAIFEVKALD VQIGSITGGG RYDNLTGVFG MAGVSGVGIS FGADRIFDVL NQLELYPKEA
     VNGTELMFVN FGDKEAAFSM SMLAKVRAAG IRAEIFPDAA KMKKQMSYAN AKSVPFVAIV
     GENEMNEGKA MLKNMETGEQ NLVSVEELIA ALRN