ID   SYH_BORAP               Reviewed;         456 AA.
AC   Q0SP28;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=BAPKO_0137;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(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; CP000395; ABH01400.1; -; Genomic_DNA.
DR   RefSeq; YP_709576.1; -.
DR   GeneID; 4227378; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0137.
DR   KEGG; baf:BAPKO_0137; -.
DR   NMPDR; fig|390236.5.peg.201; -.
DR   HOGENOM; Q0SP28; -.
DR   OMA; Q0SP28; RYDLTIP.
DR   BioCyc; BAFZ390236:BAPKO_0137-MON; -.
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    456       Histidyl-tRNA synthetase.
FT                                /FTId=PRO_1000016316.
SQ   SEQUENCE   456 AA;  52781 MW;  89BF2C1B86106692 CRC64;
     MDIKTLKGFK DYLPKDSLIR IHIVRQIFSV LNSYNFDLID TPVLEYSELL LKKSGDEAEK
     QIYRFKDNGG RDVSMRFDLT VPFARFIATN ASNLKFPFRR SQFGKVFRGE NSQKGRYREF
     MQFDFDIVGE DSFRGDAEIL SVVYYGLEEI FLNFIEGINK KFIIHYSHLG ILNSFFEKLG
     IKEKSLFILR NIDKIDKIGV DKVKEALLLK IEKEVVDSIL NLVNLQGTFK EKIQALKSIL
     GDNESVKRVE DVFQHLSLLK IQDSFNLNLK ISRGLDYYTG IVFESEVFDS NMGSVCSGGR
     YDNLVSSFSS SIQKISGVGG SFGVDRIKDI IDLEKFSYVK IFVTKARSKV LIVNLDSALQ
     DYYYELATRF RNHDYSKVKN ISCEVYFKNK NGKNIKEQIE YALSKEIRFL VFVGQEEYKE
     NKMKVRDLTK KEELLLSFEE SINVIKCSEK LLCTPF
//