ID   SYH_PASMU               Reviewed;         423 AA.
AC   P57988;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   25-MAY-2022, entry version 123.
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=PM2011;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK04095.1; -; Genomic_DNA.
DR   RefSeq; WP_010907448.1; NC_002663.1.
DR   AlphaFoldDB; P57988; -.
DR   SMR; P57988; -.
DR   STRING; 747.DR93_2089; -.
DR   EnsemblBacteria; AAK04095; AAK04095; PM2011.
DR   KEGG; pmu:PM2011; -.
DR   PATRIC; fig|272843.6.peg.2034; -.
DR   HOGENOM; CLU_025113_1_1_6; -.
DR   OMA; CDFDFIG; -.
DR   Proteomes; UP000000809; 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   PANTHER; PTHR43707; PTHR43707; 1.
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..423
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136216"
SQ   SEQUENCE   423 AA;  47530 MW;  F0E65E0CB851B2AD CRC64;
     MAKTIQAIRG MNDCSPTESP LWQWVEGKVR SVLQNYGYSE VRMPIVESTP LFARAIGEVT
     DVVSKEMYTF WDNDEQLTLR PEGTAGCVRA AIEHGWIYNQ EQRLWYMGPM FRHERPQKGR
     YRQFHQAGVE VFGIPNPEID AELIMLTARL WKELGIAEHV TLQLNSIGSL EARKNYRSAL
     VAFLQQHVDL LSEEEKERLE KNPLRILDTK NQALQEVLND APKLLAYLDD DSREHFAQLC
     ALLDAVGIQY EVNPKLVRGL DYYNKTVFEW VTSALGAQGT VCGGGRYDGL VEQLGGHATT
     GVGFAMGLER LVLLVQEVNQ SIRLPSAVDI YVVYQGEGTT LAAFQLAETL RTELPQLRVM
     THCSGGNFKK QFKRADKSGA TLALVIGESE VQNQQVVVKH LLGGAEQQTL ALDDIVDYIK
     NNF