ID   SYH_BRUO2               Reviewed;         502 AA.
AC   A5VTT4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
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};
GN   OrderedLocusNames=BOV_A0169;
OS   Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=444178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX   PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA   Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA   de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA   Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA   Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT   "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT   range and tissue tropism.";
RL   PLoS ONE 4:E5519-E5519(2009).
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; CP000709; ABQ61997.1; -; Genomic_DNA.
DR   RefSeq; WP_006015175.1; NC_009504.1.
DR   AlphaFoldDB; A5VTT4; -.
DR   SMR; A5VTT4; -.
DR   GeneID; 45125586; -.
DR   KEGG; bov:BOV_A0169; -.
DR   HOGENOM; CLU_025113_3_2_5; -.
DR   PhylomeDB; A5VTT4; -.
DR   Proteomes; UP000006383; 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; 3.40.50.800; Anticodon-binding domain; 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   NCBIfam; TIGR00442; hisS; 1.
DR   PANTHER; PTHR11476:SF7; HISTIDINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR11476; HISTIDYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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_1000016318"
SQ   SEQUENCE   502 AA;  55149 MW;  BD9DC3BA3B405833 CRC64;
     MADKADKMKA RLPRGFVDRV PDDLRAAEKM MATIREVYDL YGFEPVETPL VEYTDALGKF
     LPDQDRPNEG VFSFQDDDEQ WLSLRYDLTA PLARYVAENF ETLPKPYRSY RNGWVFRNEK
     PGPGRFRQFM QFDADTVGAP NVSADAEMCM MMADALERLG IQRGDYAIRV NNRKVLDGVL
     DAIGLEGEGN AAKRLNVLRA IDKLDKFGPE GVRLLLGKGR LDESGDFTKG AQLPEAAIEK
     VLAFTAAGGA DGAQTIANLQ AVVAGNAKGE EGVQELADMQ ALFFAGGYEG RVKIDPSVVR
     GLEYYTGPVF EAELLFDVTN EDGQKVVFGS VGGGGRYDGL VSRFRGEPVP ATGFSIGVSR
     LMTALKNLGK LDVSDTVGPV VVLVMDKDTQ NLGRYQKMVS DLRKAGIRAE MYVGGSGMKA
     QMKYADRRAA PCVVIQGSQE REAGEVQIKD LVEGKRLSAE IEDNVTWRES RPAQITVRED
     GLVDAVREIL DAQARDRAEQ SK
//