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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
 
 
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