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