ID   SYH_BORA1               Reviewed;         428 AA.
AC   Q2KY92;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Histidyl-tRNA synthetase;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidine--tRNA ligase;
DE            Short=HisRS;
GN   Name=hisS; OrderedLocusNames=BAV2343;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + L-histidine + tRNA(His) = AMP +
CC       diphosphate + L-histidyl-tRNA(His).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; AM167904; CAJ49953.1; -; Genomic_DNA.
DR   RefSeq; YP_786857.1; -.
DR   GeneID; 6265925; -.
DR   GenomeReviews; AM167904_GR; BAV2343.
DR   KEGG; bav:BAV2343; -.
DR   NMPDR; fig|521.1.peg.108; -.
DR   HOGENOM; Q2KY92; -.
DR   OMA; Q2KY92; VFEWVTT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00127; -; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR004154; Anticodon_bd.
DR   InterPro; IPR015807; His-tRNA-synth_IIa_sub.
DR   InterPro; IPR004516; His-tRNA_synth_IIA.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   PANTHER; PTHR11476; His-tRNA_synth; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 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; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    428       Histidyl-tRNA synthetase.
FT                                /FTId=PRO_1000016315.
SQ   SEQUENCE   428 AA;  47191 MW;  914D6819BD979D53 CRC64;
     MTQAFQKVSA IRGMNDVLPG PSAQWERFEE IVRAWLQGYG YRNVRTPILE QTRLFTRGIG
     EVTDIVEKEM YTFTDALNGE SLTMRPEMTA GVVRAAIEHN MLYERPHRVY SIGPVFRHER
     PQRGRYRQFH QIDVEALGFA GPDIDAELIV MLGRLWNTLG LADIRLELNS LGQPAERAAH
     RAALIEYLEK HVDILDEDGK RRLYTNPLRV LDTKNPALQE MANAAPRLFD FLGEASRAHF
     DGVCQRLDDA GIGYSLNPRL VRGLDYYNLT VFEWVTDRLG SQGTVCGGGR YDGLIELLGG
     KPAPAVGFAI GVERLLDLWE QSAGQQTPPE CEVYVVHQGE GAQRLAARVG EDLRDAGLSV
     IVHAGAASFK SQFKRADASG ARVAVILGDD EVATKTASVK YLRADAAGEG AQDKVALATL
     ASVLKSKG
//