SYH_AYWBP
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 03-AUG-2022, entry version 103.
DE RecName: Full=Histidine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00127};
DE EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00127};
DE Short=HisRS {ECO:0000255|HAMAP-Rule:MF_00127};
GN Name=hisS {ECO:0000255|HAMAP-Rule:MF_00127}; OrderedLocusNames=AYWB_594;
OS Aster yellows witches'-broom phytoplasma (strain AYWB).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=322098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYWB;
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., Shevchenko D.V.,
RA Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT "Living with genome instability: the adaptation of phytoplasmas to diverse
RT environments of their insect and plant hosts.";
RL J. Bacteriol. 188:3682-3696(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-
CC histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665,
CC Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00127};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00127}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00127}.
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DR EMBL; CP000061; ABC65711.1; -; Genomic_DNA.
DR RefSeq; WP_011412873.1; NC_007716.1.
DR AlphaFoldDB; Q2NIN2; -.
DR SMR; Q2NIN2; -.
DR STRING; 322098.AYWB_594; -.
DR PRIDE; Q2NIN2; -.
DR EnsemblBacteria; ABC65711; ABC65711; AYWB_594.
DR KEGG; ayw:AYWB_594; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_1_14; -.
DR OMA; YQIQKVW; -.
DR OrthoDB; 277998at2; -.
DR PhylomeDB; Q2NIN2; -.
DR Proteomes; UP000001934; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00127; His_tRNA_synth; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR015807; His-tRNA-ligase.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR PANTHER; PTHR43707; PTHR43707; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..427
FT /note="Histidine--tRNA ligase"
FT /id="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