ID   SYH_BIFLO               Reviewed;         466 AA.
AC   Q8G864;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=BL0017;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN23884.1; -; Genomic_DNA.
DR   RefSeq; NP_695248.1; NC_004307.2.
DR   RefSeq; WP_008782706.1; NC_004307.2.
DR   AlphaFoldDB; Q8G864; -.
DR   SMR; Q8G864; -.
DR   STRING; 206672.BL0017; -.
DR   EnsemblBacteria; AAN23884; AAN23884; BL0017.
DR   KEGG; blo:BL0017; -.
DR   PATRIC; fig|206672.9.peg.18; -.
DR   HOGENOM; CLU_025113_3_0_11; -.
DR   OMA; YQIQKVW; -.
DR   PhylomeDB; Q8G864; -.
DR   Proteomes; UP000000439; 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   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   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..466
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136114"
SQ   SEQUENCE   466 AA;  50394 MW;  72729E0E6A7C06C9 CRC64;
     MAKGASISGF PEWLPSERVV EQRVIDTLRK VFELNGFIGI ETRAVETGAS LLKKGETSKE
     IYLLSRLQEV GHESDTPIEE RLGLHFDLTV PLSRYVVEHS GALAFPFKRW QIQKVWRGER
     PQEGRFREFV QADIDVIGAG DLPDHYEVEL PLVMVSALEE LRAYGLPKAT VHANNRKLSE
     GFYRGLGLTD VEGVLREIDK LDKIGADEVA RLLTETCGAT EAQARACLEL AELTASDGAE
     LAAKFDALCE AHGIVKDSEA YTLARQGLDT LAMIVDEAAA IRPGSVIADL KIARGLDYYT
     GSVYETFLDG AASLGSICSG GRYDNLASQG NRKYPGVGLS IGLSRLVSYM LHTAGAHANR
     VSPAAVLVAV WNEEDRPAAN RIANQLRARG IATDVAPTAA KLGKQIKYAD KLGIPYVWFP
     ATAAEGAEGA EPAGDEVKNI VTGEQVAADC TSWEPDTVVA QQTVEI