ID   SYH_TROWT               Reviewed;         426 AA.
AC   Q83FF5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Probable histidine--tRNA ligase;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidyl-tRNA synthetase;
DE            Short=HisRS;
GN   Name=hisS; OrderedLocusNames=TWT_785;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014184; AAO44882.1; -; Genomic_DNA.
DR   RefSeq; WP_011096731.1; NC_004572.3.
DR   AlphaFoldDB; Q83FF5; -.
DR   SMR; Q83FF5; -.
DR   STRING; 203267.TWT_785; -.
DR   EnsemblBacteria; AAO44882; AAO44882; TWT_785.
DR   GeneID; 67388575; -.
DR   KEGG; twh:TWT_785; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_3_0_11; -.
DR   OMA; YQIQKVW; -.
DR   OrthoDB; 277998at2; -.
DR   Proteomes; UP000002200; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR015807; His-tRNA-ligase.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR004516; HisRS/HisZ.
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..426
FT                   /note="Probable histidine--tRNA ligase"
FT                   /id="PRO_0000136288"
SQ   SEQUENCE   426 AA;  48039 MW;  399623321706F64B CRC64;
     MKIVPPRGMQ DFLPHEKEHR DRITEVIYKS YISHGFNPIE TPSLENIERL ACGVGQENEK
     LTYKIIRRGL TGAQTVQHPD ELIDLGLRFD LTIPLVRFWN TNRARLPKIF RSLQIGHVWR
     AEKPQKGRRR QFIQCDIDII GQPEILAEIE LLVATLSTLE QLGIRTPKLH INDRRILFSM
     LNNLGVPHSC HVYVSIVLDK LRKIGLDLVK QELCEFPALV AYLASSVNSN TGSTDLCFDV
     SSTKDITHIR RTIQSALPHG CKFDCEDLCR IIASVNEFTQ TGVFFDPLLV RGMGYYTGPI
     FEILHDDYSI AGGGRYDGLV ERLGGLPTPA CGFSIGFERV LGLIKESVSL DPKKMILLYD
     PKVDPNLVVS VKLEFISKGF IVRPELASRS RRNQIELAKR EGFGAFLYLD PLSPPDGLLA
     KVKPIL