ID SYH_BRUSI Reviewed; 502 AA. AC A9WXP3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 16-JUN-2009, entry version 13. 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=BSUIS_B0190; OS Brucella suis (strain ATCC 23445 / NCTC 10510). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=470137; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., RA Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., RA Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., RA Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W., RA Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., RA Munk C., Brettin T.S.; RT "Brucella suis ATCC 23445 whole genome shotgun sequencing project."; RL Submitted (DEC-2007) 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000912; ABY39209.1; -; Genomic_DNA. DR RefSeq; YP_001622031.1; -. DR GeneID; 5836564; -. DR GenomeReviews; CP000912_GR; BSUIS_B0190. DR KEGG; bmt:BSUIS_B0190; -. DR OMA; A9WXP3; RYDLTIP. 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 1 502 Histidyl-tRNA synthetase. FT /FTId=PRO_1000076263. SQ SEQUENCE 502 AA; 55179 MW; 2A41AFD402EE687F CRC64; MADKADKMKA RLPRGFVDRV PDDLRAAEKM MATIREVYDL YGFEPVETPL VEYTDALGKF LPDQDRPNEG VFSFQDDDEQ WLSLRYDLTA PLARYVAENF ETLPKPYRSY RNGWVFRNEK PGPGRFRQFM QFDADTVGAP NVSADAEMCM MMADTLERLG IQRGDYAIRV NNRKVLDGVL DAIGLEGEGN AAKRLNVLRA IDKLDKFGPE GVRLLLGKGR LDESGDFTKG AQLPEAAIEK VLAFTAAGGA DGAQTIANLQ AVVAGNAKGE EGVQELADMQ ALFFAGGYEG RVKIDPSVVR GLEYYTGPVF EAELLFDVTN EDGQKVVFGS VGGGGRYDGL VSRFRGEPVP ATGFSIGVSR LMTALKNLGK LDVSDTVGPV VVLVMDKDTQ NLGRYQKMVS DLRKAGIRAE MYVGGSGMKA QMKYADRRAA PCVVIQGSQE REAGEVQIKD LVEGKRLSAE IEDNVTWRES RPAQITVRED GLVDAVREIL DAQARDRAEQ SK //