ID   SYH_ALCBS               Reviewed;         422 AA.
AC   Q0VNE1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=ABO_1859;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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; AM286690; CAL17307.1; -; Genomic_DNA.
DR   RefSeq; YP_693579.1; -.
DR   GeneID; 4211474; -.
DR   GenomeReviews; AM286690_GR; ABO_1859.
DR   KEGG; abo:ABO_1859; -.
DR   NMPDR; fig|393595.12.peg.1864; -.
DR   HOGENOM; Q0VNE1; -.
DR   OMA; Q0VNE1; VFEWVTT.
DR   BioCyc; ABOR393595:ABO_1859-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    422       Histidyl-tRNA synthetase.
FT                                /FTId=PRO_1000016307.
SQ   SEQUENCE   422 AA;  46386 MW;  6A2B20E795997A88 CRC64;
     MSKKITSIRG MNDILPEQTG LWQWLEAKVG AVLASYGYQE IRMPIVEQTD LFKRSIGEVT
     DIVEKEMYTF DDRNGDSLTL RPEGTASCVR ACEQHGLLYN QTQRLWYAGP MFRHERPQAG
     RYRQFHQIGV ETFGMTGPDI DAEVILLTAR LWKALGLEDK VVLELNSLGD SADRARYRDA
     LVDYLKAHFD DLDGDSQKRL ERSPLRVLDS KDTGTREVLK GAPQLADYLN DEAVAHFEGL
     KALLDASGIA YKVNPYLVRG LDYYGKTVFE WVTDALGAQG TVCAGGRYDG LVEQLGGKPT
     PAVGFAMGIE RLILLIEQER PELSAPVDVY VMAMGDVLAP TMALSEHLRD ALPGRAIQLH
     CGGGSFKSQM KKADRSGAAV GLIMGEDELA SGVVTVKPLR GQGEQVQVAQ GDVANAVTSF
     LE
//