SYH_BRUA2
ID SYH_BRUA2 Reviewed; 502 AA.
AC Q2YIH9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Histidine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00127};
DE EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00127};
DE Short=HisRS {ECO:0000255|HAMAP-Rule:MF_00127};
GN Name=hisS {ECO:0000255|HAMAP-Rule:MF_00127}; OrderedLocusNames=BAB2_0181;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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; AM040265; CAJ12347.1; -; Genomic_DNA.
DR RefSeq; WP_002968826.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YIH9; -.
DR SMR; Q2YIH9; -.
DR STRING; 359391.BAB2_0181; -.
DR EnsemblBacteria; CAJ12347; CAJ12347; BAB2_0181.
DR GeneID; 3827165; -.
DR KEGG; bmf:BAB2_0181; -.
DR PATRIC; fig|359391.11.peg.2131; -.
DR HOGENOM; CLU_025113_3_2_5; -.
DR OMA; CDFDFIG; -.
DR PhylomeDB; Q2YIH9; -.
DR Proteomes; UP000002719; Chromosome II.
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; Reference proteome.
FT CHAIN 1..502
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000016317"
SQ SEQUENCE 502 AA; 55136 MW; 2A41BDC723CE687F CRC64;
MADKADKMKA RLPRGFVDRV PDDLRAAEKM MATIREVYDL YGFEPVETPL VEYTDALGKF
LPDQDRPNEG VFSFQDDDEQ WLSLRYDLTA PLARYVAENF ETLPKPYRSY RNGWVFRNEK
PGPGRFRQFM QFDADTVGAP NVSADAEMCM MMADTLERLG IQRGDYAIRV NNRKVLDGVL
DAIGLEGEGN AAKRLNVLRA IDKLDKFGPE GVRLLLGKGR LDESGDFTKG AQLPEAAIEK
VLAFTAAGGA DGAQTIANLQ AVVAGNAKGE EGVQELADMQ ALFFAGGYEG RVKIDPSVVR
GLEYYTGPVF EAELLFDVTN EDGQKVVFGS VGGGGRYDGL VSRFRGEPVP ATGFSIGVSR
LMTALKNLGK LDVSDTVGPV VVLVMDKDTQ NLGRYQKMVS DLRKAGIRAE MYVGGSGMKA
QMKYADRRAA PCVVIQGSQE REAGEVQIKD LVEGKRLSAE IEDNVTWLES RPAQITVRED
GLVDAVREIL DAQARDRAEQ SK