SYH_VIBA3
ID SYH_VIBA3 Reviewed; 422 AA.
AC B7VJT9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=VS_0620;
OS Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=575788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LGP32;
RA Mazel D., Le Roux F.;
RT "Vibrio splendidus str. LGP32 complete genome.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; FM954972; CAV17615.1; -; Genomic_DNA.
DR RefSeq; WP_012603314.1; NC_011753.2.
DR AlphaFoldDB; B7VJT9; -.
DR SMR; B7VJT9; -.
DR STRING; 575788.VS_0620; -.
DR EnsemblBacteria; CAV17615; CAV17615; VS_0620.
DR KEGG; vsp:VS_0620; -.
DR PATRIC; fig|575788.5.peg.1972; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_1_6; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 277998at2; -.
DR Proteomes; UP000009100; Chromosome 1.
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 PANTHER; PTHR43707; PTHR43707; 1.
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..422
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000199165"
SQ SEQUENCE 422 AA; 47092 MW; 7F9F7F697330B161 CRC64;
MAKNIQAIRG MNDCLPTQSP LWQKVESAVK SVVSAYGYNE VRMPIVEETN LFSRAVGEET
DVVSKEMYTF DDRNGDSLTL RPEGTAGCVR SCIQNSLINR DEQRLWYMGP MFRHERPQKG
RYRQFHQCGV EVFGLDGPDV DAELIMMTAR LWRELGIDKH VRLELNSIGS QEDRVSYRTA
LVAFLEQHID VLDEDCKRRM HTNPLRVLDT KNPDVQAILG DAPRLSEYLG EESKQHFAGL
CELLDAVGIE YQVNERLVRG LDYYNRTVFE WITDSLGAQG TVCGGGRYDG LVEQLGGKAT
NAVGFAMGLE RLVLMMETLE LTEVRRSVDV YMVAAGEGTM IAGMQLANQL RDTVEGVRVM
NHFGGGNFKK QFKRADKVGA VVALVLGENE VADNTVVLKD LVGGEQQTVS QTEVAEKVAA
LI