ID   SYH_HALMA               Reviewed;         435 AA.
AC   Q5UXW4;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=rrnAC3183;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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   -!- 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; AY596297; AAV47889.1; -; Genomic_DNA.
DR   RefSeq; WP_011224659.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UXW4; -.
DR   SMR; Q5UXW4; -.
DR   STRING; 272569.rrnAC3183; -.
DR   EnsemblBacteria; AAV47889; AAV47889; rrnAC3183.
DR   GeneID; 40153990; -.
DR   KEGG; hma:rrnAC3183; -.
DR   PATRIC; fig|272569.17.peg.3723; -.
DR   eggNOG; arCOG00404; Archaea.
DR   HOGENOM; CLU_025113_3_1_2; -.
DR   OMA; CDFDFIG; -.
DR   Proteomes; UP000001169; Chromosome I.
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   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..435
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136309"
FT   REGION          415..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   435 AA;  48394 MW;  4EA8E8A4D1B02F0B CRC64;
     MYDSVKGFRD FYPKEMQARR WAMDTLEDVA QRYGFREIGT PALEPTEMYV DKSGEEIVEE
     LYSFEDKGGR KVALTPELTP TVARMFVAKQ QELSKPIKWV STRPFWRYEE PQQGRFREFY
     QTNVDIFGSA EPTADAEILA VAVDMLTDLG LTGEDFEIRV SHRDILSGVL ESFEADVDVP
     EAIRAVDKRA KVDHDEYLDA LAEAGLSYGQ ADTFDEMLQI DAEEIETLGD LTGSEDVRTA
     TDNLQAVLDA AEDFGVREHL TVSLTTARGL DYYTGVVFEC FDSTGEVSRS VFGGGRYDDL
     IEGFGGQPTP AVGFAPGHAT LQLLCQRAGV WPAEELSTDY YVLQVGDTRP TAARIARDLR
     ERGHVVESDV ADRSFGAQMG YADGINAETV VIVGEQDLEN DEVTLKEMDD GEQVSVPLSA
     FPGDYDRPTF EDFAE