ID SYH_ALHEH Reviewed; 429 AA. AC Q0A986; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 22. 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=Mlg_1252; OS Alkalilimnicola ehrlichei (strain MLHE-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Alkalilimnicola. OX NCBI_TaxID=187272; 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., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., RA King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., RA Xie G., Stolz J.F., Richardson P.; RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1."; 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. 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; CP000453; ABI56601.1; -; Genomic_DNA. DR RefSeq; YP_742091.1; -. DR GeneID; 4269174; -. DR GenomeReviews; CP000453_GR; Mlg_1252. DR KEGG; aeh:Mlg_1252; -. DR NMPDR; fig|187272.6.peg.1200; -. DR HOGENOM; Q0A986; -. DR OMA; Q0A986; 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 1 429 Histidyl-tRNA synthetase. FT /FTId=PRO_1000016308. SQ SEQUENCE 429 AA; 47922 MW; DDE09E5CBB8133B9 CRC64; MAKGIRSIRG FSDILPEQTP LWQFVESNIQ ATLEAYGYRE IRLPIVEKTE LFSRSIGEVT DIVEKEMYTF EDRNGDSLTL RPEGTAGCVR CGIQNGLFHG GQPRVWYAGP MFRHERPQKG RYRQFHQIGA EVYGESGPGV DAEMILMTAR LLRCLGLEDV RLELNTLGTG EARAAHRAAL VEYLQAHEDR LDDDARRRLH SNPLRILDTK NPDMQALVEQ APRLMDYLDE DSRSHFQAVC RVLDQAGVAY RVNPRLVRGL DYYSRTVFEW ITDRLGAQGT VLAGGRYDTL VEQIGGKPTP AIGFALGLER LVSLLEESGI SGPQSGPHAF VVSADSLRAL PLVEGLRDRL PGLRLQMQTE GGSFRSQFKR ADRSGAALAL VLGEEELAEG RFGVKDLRGD AEQQRLDPEA LSDYLARRWP ELAATEVTD //