ID   SYH_BRUME               Reviewed;         502 AA.
AC   Q8YB45;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=BMEII1056;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(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         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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE008918; AAL54298.1; -; Genomic_DNA.
DR   PIR; AG3641; AG3641.
DR   RefSeq; WP_004681426.1; NZ_GG703779.1.
DR   AlphaFoldDB; Q8YB45; -.
DR   SMR; Q8YB45; -.
DR   STRING; 224914.BMEII1056; -.
DR   EnsemblBacteria; AAL54298; AAL54298; BMEII1056.
DR   GeneID; 29595934; -.
DR   KEGG; bme:BMEII1056; -.
DR   PATRIC; fig|224914.52.peg.2307; -.
DR   eggNOG; COG0124; Bacteria.
DR   OMA; CDFDFIG; -.
DR   PhylomeDB; Q8YB45; -.
DR   Proteomes; UP000000419; Chromosome II.
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; 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..502
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136124"
SQ   SEQUENCE   502 AA;  55209 MW;  5C9AC279B43E296B CRC64;
     MADKADKMKA RLPRGFVDRV PDDLRAAEKM MATIREVYDL YGFEPVETPL VEYTDALGKF
     LPDQDRPNEG VFSFQDDDEQ WLSLRYDLTA PLARYVAENF ETLPKPYRSY RNGWVFRNEK
     PGPGRFRQFM QFDADTVGAP NVSADAEMCM MMADTLERLG IQRGDYAIRV NNRKVLDGVL
     DAIGLEGEGN AAKRLNVLRA IDKLDKFGPE GVRLLLGKGR LDESGDFTKG AQLPEAAIEK
     VLAFTAAGGA DGAQTIANLQ AVVAGNAKGE EGVQELADMQ ALFFAGGYEG RVKIDPSVVR
     GLEYYTGPVF EAELLFDVTN EDGQKVVFGS VGGGGRYDGL VSRFRGEPVP ATGFSIGVSR
     LMTALKNLGK LDVSDTVGPV VVLVMDKDTQ NLSRYQKMVS DLRKAGIRAE MYVGGSGMKA
     QMKYADRRAA PCVVIQGSQE REAGEVQIKD LVEGKRLSAE IEDNVTWRES RPAQITVRED
     GLVDAVREIL DAQARDRAEQ SK