ID   SYH_THEFY               Reviewed;         438 AA.
AC   Q47RX0;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=Tfu_0759;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/jb.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA   Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA   Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ54797.1; -; Genomic_DNA.
DR   RefSeq; WP_011291206.1; NC_007333.1.
DR   AlphaFoldDB; Q47RX0; -.
DR   SMR; Q47RX0; -.
DR   STRING; 269800.Tfu_0759; -.
DR   PRIDE; Q47RX0; -.
DR   EnsemblBacteria; AAZ54797; AAZ54797; Tfu_0759.
DR   KEGG; tfu:Tfu_0759; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_3_0_11; -.
DR   OMA; YQIQKVW; -.
DR   OrthoDB; 277998at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 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   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.
FT   CHAIN           1..438
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136281"
SQ   SEQUENCE   438 AA;  48660 MW;  FDD26DA4C5A814F3 CRC64;
     MSEQRIIRPT PISGFPEWTP RIRSVELRWL DHIRRGFERY GFSSVETPSV EVLDVLLSKG
     ETSQEIYTLQ RLQADADDSS DARLGLHFDL TVPFARYVAQ HFNDLVFPFK RYQIQRVWRG
     ERPQEGRFRE FTQCDIDVIN VDRIPLHFDA ELPRIVHEVL TGLDIPAWTL NINNRKVLQG
     FYEGLGITDP LAVIRAVDKL HKIGADAVRE ILIDQAGLSS DQAAACLELA EIRGSDTTVV
     DAVAKLGVSH PTLTAGLDEL GEVLDELSDL PSGSVVADLS IARGLDYYTG TVYEATFNDD
     PGYGSICAGG RYENLAGQFI RRSLPGVGIS IGLTRIFAKL VSEGRITGGR FCPTDVLVVL
     PSDERRSAAL AVAAQLRERG FNTEVYHQAA KIGKQIQYAV KKDIPFVWFP PFDDGRPHEV
     KNLATGEQVE ADPASWNG