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SYH_CLOAB
ID   SYH_CLOAB               Reviewed;         430 AA.
AC   Q97FJ7;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 110.
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=CA_C2740;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80686.1; -; Genomic_DNA.
DR   PIR; C97237; C97237.
DR   RefSeq; NP_349346.1; NC_003030.1.
DR   RefSeq; WP_010966027.1; NC_003030.1.
DR   AlphaFoldDB; Q97FJ7; -.
DR   SMR; Q97FJ7; -.
DR   STRING; 272562.CA_C2740; -.
DR   PRIDE; Q97FJ7; -.
DR   DNASU; 1118923; -.
DR   EnsemblBacteria; AAK80686; AAK80686; CA_C2740.
DR   GeneID; 44999228; -.
DR   KEGG; cac:CA_C2740; -.
DR   PATRIC; fig|272562.8.peg.2929; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_3_0_9; -.
DR   OMA; YQIQKVW; -.
DR   OrthoDB; 277998at2; -.
DR   Proteomes; UP000000814; 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   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; Reference proteome.
FT   CHAIN           1..430
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136141"
SQ   SEQUENCE   430 AA;  49246 MW;  D7B034BD474297F3 CRC64;
     MNNKIKPSIL PGFMELLPKE QLVFNDIVSK ITGVYEQNGF LPMDTPIIEK EEVLLAKSAG
     ETEKQVYRID NEDRKQVLRF DLTVPFSRFA AQYMSDLTFP FKRYQLGKVY RGERNQKGRY
     REFYQCDVDV VGNGNLSIKN DAFIINMASK ALRKIGLDSY KFQISNRKIL TGVLEGLNIT
     NMQEVMILID KYDKITEEQF LSELNKLIGE EKAKVISKVI KISGSSDEVV ENLKKVEIKN
     EMLEKGIEEV EEVIKYLKLF GVEDSEYAIN LKIIRGLDYY TGTVFETLLT GNESYGSICS
     GGRYDNLAQN YTENVLPGVG MSIGITRLFF VLREIGFIEN YNSSLNEKYL IVPIGDTFEY
     CTKILNKLLV NGKSAEIYFE EGKLKKKLTY ANKLDIKYVI LIGEDEVTNK ELVIKDMITG
     EQKKLNIEEI
 
 
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