ID   SYH_BACFR               Reviewed;         454 AA.
AC   Q64QS2;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=BF3416;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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   -!- SUBUNIT: Homodimer. {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; AP006841; BAD50159.1; -; Genomic_DNA.
DR   RefSeq; WP_011203280.1; NC_006347.1.
DR   RefSeq; YP_100693.1; NC_006347.1.
DR   AlphaFoldDB; Q64QS2; -.
DR   SMR; Q64QS2; -.
DR   STRING; 295405.BF3416; -.
DR   EnsemblBacteria; BAD50159; BAD50159; BF3416.
DR   KEGG; bfr:BF3416; -.
DR   PATRIC; fig|295405.11.peg.3283; -.
DR   HOGENOM; CLU_025113_3_0_10; -.
DR   OMA; YQIQKVW; -.
DR   Proteomes; UP000002197; 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   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.
FT   CHAIN           1..454
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136108"
SQ   SEQUENCE   454 AA;  50385 MW;  2528978FA60AE02E CRC64;
     MAAKPGIPKG TRDFSPVEMA KRNYIFNTIR DVYHLYGFQQ IETPSMEMLS TLMGKYGEEG
     DKLLFKIQNS GDYFSGITDE ELLSRNAAKL ASKFCEKGLR YDLTVPFARY VVMHRDEITF
     PFKRYQIQPV WRADRPQKGR YREFYQCDAD VVGSDSLLNE VELMQIVDTV FTRFGIRVCI
     KINNRKILTG IAEIIGEADK IVDITVAIDK LDKIGLDNVN KELAEKGISE EAIAKLQPII
     LLSGTNTEKL ATLKTVLSDS ETGLKGVEES EFILNTLQTM GLKNEIELDL TLARGLNYYT
     GAIFEVKALD VQIGSITGGG RYDNLTGVFG MAGVSGVGIS FGADRIFDVL NQLELYPKEA
     VNGTQLLFIN FGEKEAAFSM GILSKARAAG IRAEIFPDAA KMKKQMSYAN VKNIPFVAIV
     GENEMNEGKA MLKNMESGEQ QLVTAEELIG ALTK