SYH_HELPJ
ID SYH_HELPJ Reviewed; 442 AA.
AC Q9ZK27;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Histidine--tRNA ligase;
DE EC=6.1.1.21;
DE AltName: Full=Histidyl-tRNA synthetase;
DE Short=HisRS;
GN Name=hisS; OrderedLocusNames=jhp_1115;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE001439; AAD06696.1; -; Genomic_DNA.
DR PIR; D71847; D71847.
DR RefSeq; WP_000632487.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZK27; -.
DR SMR; Q9ZK27; -.
DR STRING; 85963.jhp_1115; -.
DR EnsemblBacteria; AAD06696; AAD06696; jhp_1115.
DR KEGG; hpj:jhp_1115; -.
DR PATRIC; fig|85963.30.peg.1463; -.
DR eggNOG; COG0124; Bacteria.
DR OMA; CDFDFIG; -.
DR Proteomes; UP000000804; 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 CDD; cd00859; HisRS_anticodon; 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 InterPro; IPR033656; HisRS_anticodon.
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..442
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136175"
SQ SEQUENCE 442 AA; 50246 MW; 4C650763A8BA53BC CRC64;
MITPKVLSGF KDRLPKDAIQ KAQLLAKVSV VFQSFGFVPI ETPHLEYAQT LLPDASSDIQ
KEIYRFKDHG DRDVALRFDL TVPLARFVSL HHQILGMPFK RYAIGNVFRG ERAQKGRYRE
FTQCDFDFIG SESLVCDAEI IQVIIASLKA LDLEDFCVSI NHRKILNGIC EYFGIAQVNE
VLRIVDKLEK IGLNGVEEEL KKECDLDSNT IKDLLEMVQI KQNDLSHAEF FEKIAYLKDY
NENLKKGIQD LERLYQLLGD LQISQNLYKI DFSIARGLGY YTGIVYETTL NDMKSLGSVC
SGGRYDHLTK NFSKENLQGV GASIGIDRLI VALSEMQLLD ERSTQAKVLI ACMHEEYFSY
ANRLAESLRQ SGIFSEVYPE AQKIKKPFSY ANHKGHEFVA VIGEEEFKSE TLSLKNMHSG
MQLNCLSFLK ALEIIGENDE DL