ID   SYH_VIBPA               Reviewed;         422 AA.
AC   Q87S15;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 1.
DT   25-MAY-2022, entry version 105.
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=VP0609;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC58872.1; -; Genomic_DNA.
DR   RefSeq; NP_796988.1; NC_004603.1.
DR   RefSeq; WP_005460225.1; NC_004603.1.
DR   AlphaFoldDB; Q87S15; -.
DR   SMR; Q87S15; -.
DR   STRING; 223926.28805595; -.
DR   PRIDE; Q87S15; -.
DR   EnsemblBacteria; BAC58872; BAC58872; BAC58872.
DR   GeneID; 1188084; -.
DR   KEGG; vpa:VP0609; -.
DR   PATRIC; fig|223926.6.peg.577; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_1_1_6; -.
DR   OMA; CDFDFIG; -.
DR   Proteomes; UP000002493; 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_0000136292"
SQ   SEQUENCE   422 AA;  47146 MW;  645FD62392F06A5D CRC64;
     MAKTIQAIRG MNDCLPTQSP LWQKLENTVK NVISAYGYNE VRMPIVEETN LFSRAVGEET
     DVVSKEMYTF DDRNGDSLTL RPEGTAGCVR SCIQNSLINR DEQRLWYMGP MFRHERPQKG
     RYRQFHQCGV EVFGLNGPDV DAELIMMTAR LWRELGIDKH VRLELNSIGS QEDRADYRTA
     LVAFLEQHID VLDEDCKRRM HTNPLRVLDT KNPDIQAILG DAPRLSEYLG EESKAHFAGL
     CELLDAAGIE YTVNERLVRG LDYYNRTVFE WITESLGAQG TVCGGGRYDG LVEQLGGKPT
     PAVGFAMGLE RLVLMLETLE LTDVRRSVDV YVVTAGEGTM MAGMKLAEQL REAISGVRVM
     NHFGGGNFKK QFKRADKVGA VVALVLGENE VADNTVVLKD LVGGEQETYN QAEVAEKIAA
     LI