ID SYH_AYWBP Reviewed; 427 AA. AC Q2NIN2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 16-JUN-2009, entry version 30. 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=AYWB_594; OS Aster yellows witches'-broom phytoplasma (strain AYWB). OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; OC Acholeplasmataceae; Candidatus Phytoplasma; OC Candidatus Phytoplasma asteris. OX NCBI_TaxID=322098; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16672622; DOI=10.1128/JB.188.10.3682-3696.2006; RA Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., RA Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W., RA Hogenhout S.A.; RT "Living with genome instability: the adaptation of phytoplasmas to RT diverse environments of their insect and plant hosts."; RL J. Bacteriol. 188:3682-3696(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. 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; CP000061; ABC65711.1; -; Genomic_DNA. DR RefSeq; YP_456790.1; -. DR GeneID; 3866087; -. DR GenomeReviews; CP000061_GR; AYWB_594. DR KEGG; ayw:AYWB_594; -. DR HOGENOM; Q2NIN2; -. DR OMA; Q2NIN2; 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 1 427 Histidyl-tRNA synthetase. FT /FTId=PRO_1000016311. SQ SEQUENCE 427 AA; 49715 MW; 8A750EA3CDD3AD3D CRC64; MFSKIKGTHD LMLDKMVCWQ KVENHIRTLF AKYHLQEIRT PIIEYRGVFD RAAQHSEMVS KETYTFTDKK GRFITLRPEG TAGVIRSYVE NKLDKTSQLH KFFYYGPFFR YERPQKGRYR QFHQVGVEIL GQSSPFLDVE VIFLAYKTLK SLGICDITVK INSLGCKTTY NNYLQVFKNY LQTHYQQLCP LCQERFEKNI LRIWDCKNCN NEPFLKQAPR IFDHLVEDAK VRFLQVLEGL KQMNVNFELC HDLVRGLDYY TNSVFEIVYN NEQGHQAVLG GGGCYDNLVT LFRGSPSPGI GFALGMERLM SILATRSFCN KNILPSLDAF ILVSEPQFFY QGLELATTLR HQGFSADLNY KFLSFSKSLK QALKKQPLYL LILGPKEFAN NQITIKNTYT QQQTTILQKD VVSYLQNNKE LNYIHEN //