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SYH1_BACC1
ID   SYH1_BACC1              Reviewed;         436 AA.
AC   P62367;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Histidine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00127};
DE            EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE   AltName: Full=Histidyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00127};
DE            Short=HisRS 1 {ECO:0000255|HAMAP-Rule:MF_00127};
GN   Name=hisS1 {ECO:0000255|HAMAP-Rule:MF_00127}; OrderedLocusNames=BCE_3348;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS42256.1; -; Genomic_DNA.
DR   RefSeq; WP_000425326.1; NC_003909.8.
DR   AlphaFoldDB; P62367; -.
DR   SMR; P62367; -.
DR   EnsemblBacteria; AAS42256; AAS42256; BCE_3348.
DR   GeneID; 59159793; -.
DR   KEGG; bca:BCE_3348; -.
DR   HOGENOM; CLU_025113_3_0_9; -.
DR   OMA; YQIQKVW; -.
DR   Proteomes; UP000002527; 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..436
FT                   /note="Histidine--tRNA ligase 1"
FT                   /id="PRO_0000136095"
SQ   SEQUENCE   436 AA;  49160 MW;  847FBA0FA029029C CRC64;
     MEMKNVKGTK DYLPEEQVLR NKIKRACEDT FERYGCKPLE TPTLNMYELM SYKYGGGDEI
     LKEIYTLQDQ GKRNLALRYD LTIPFAKVVA MNPNIRLPFK RYEIGKVFRD GPIKQGRFRE
     FIQCDVDIVG VESVMAEAEL MSMAFELFRT LNLEVTIQYN NRKLLNGILE SINIPTERTS
     DVILSLDKIE KIGIDGVRKD VLERGISEEM ADTICNTVLS CLKLTIADFK EAFNNPLVAD
     GVNELQQLQQ YLIALGINEN AIFNPFLARG LTMYTGTVYE IFLKDGSITS SIGSGGRYDN
     IIGAFRGDNM NYPTVGISFG LDVIYTALSQ KETISSTADV FIIPLGTELQ CLQIAQQLRS
     TTSLKVELEL AGRKLKRALN YANKENIPYV LIIGEDELST ETVVLRNMKE GSEVKVPLSS
     LKDNTFNNYC NIPIKL
 
 
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