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