ID   SYH_BURCM               Reviewed;         446 AA.
AC   Q0BEW8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=Bamb_1749;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000440; ABI87305.1; -; Genomic_DNA.
DR   RefSeq; YP_773639.1; -.
DR   GeneID; 4309831; -.
DR   GenomeReviews; CP000440_GR; Bamb_1749.
DR   KEGG; bam:Bamb_1749; -.
DR   NMPDR; fig|339670.3.peg.5218; -.
DR   OMA; Q0BEW8; 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    446       Histidyl-tRNA synthetase.
FT                                /FTId=PRO_1000016321.
SQ   SEQUENCE   446 AA;  49671 MW;  1CC4717FC0CC2265 CRC64;
     MTEQKRKIEK LTGVKGMNDI LPQDAGLWEF FEATVKSLLR AYGYQNIRTP IVEHTQLFTR
     GIGEVTDIVE KEMYSFTDAL NGENLTMRPE NTAAVVRASI EHNMLYDGPK RLWYIGPMFR
     HERPQRGRYR QFHQVGVEAL GFAGPDADAE IIMMCQRLWD DLGLTGIKLE INSLGLAEER
     AAHRVELIKY LEQFADVLDE DAKRRLYTNP LRVLDTKNPA LQEIAQNAPK LIDFLGDESR
     AHFEGLQRLL LANNIPFKIN PRLVRGLDYY NLTVFEWVTD KLGAQGTVAA GGRYDPLIEQ
     LGGKPTAACG WAMGIERILE LLKEEDLAPE QEGVDVYVVH QGETAREQAF IAAERLRDTG
     LDVIFHCSAD GAPASFKSQM KRADASGAAF AVIFGEEEVA NGTVGVKALR GAGEEGEKNV
     QQTVPVESLT EFLINAMVAS AEDGDD
//