ID   SYH_SULIL               Reviewed;         426 AA.
AC   C3MRE4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=LS215_1962;
OS   Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=429572;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.S.2.15 / Lassen #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001399; ACP35957.1; -; Genomic_DNA.
DR   RefSeq; WP_012711827.1; NC_012589.1.
DR   AlphaFoldDB; C3MRE4; -.
DR   SMR; C3MRE4; -.
DR   PRIDE; C3MRE4; -.
DR   EnsemblBacteria; ACP35957; ACP35957; LS215_1962.
DR   GeneID; 7799608; -.
DR   GeneID; 7941891; -.
DR   KEGG; sis:LS215_1962; -.
DR   HOGENOM; CLU_025113_3_1_2; -.
DR   OMA; CDFDFIG; -.
DR   OrthoDB; 47919at2157; -.
DR   Proteomes; UP000001747; Chromosome.
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:0000105; P:histidine biosynthetic process; IEA:InterPro.
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   HAMAP; MF_00125; HisZ; 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; IPR004517; 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.
FT   CHAIN           1..426
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_1000203150"
SQ   SEQUENCE   426 AA;  49284 MW;  C7E36F16077911D0 CRC64;
     MTKFETVRGM KDYIGIDAEK IRYLESTFRD LAIKYGYSEI ITPVVEEFKL FALKGGEELR
     ETMYVFKDKA DRELSLRPEI TPSVARAYIQ NLQSSPKPIR LFYFGTVYRY DEPQYGRYRE
     FRQAGIEMIG DSSILADLEV LDLLYNFYDK LNLSNDITIK INNIGIFRKI MDKYNIEDNL
     QEHILHLIDK NKINEALDIL EKNLKNKDII DFFNKILTKK DTKLEDIESL AELEEVSRLD
     IKSEFLYLFR LSRILSNLNI KFKIDLGFVR GLAYYTGLIF EVLHPSVQFS IAGGGRYDKL
     IELYGGLPSP AIGFAIGVER TLLVIKDLKV EEPVNVIVIG MSEDTIPSMF MVSRILRKEE
     YKVVINTKDQ PLSKLLPYYA SQGFKVAIII GKQELEKNMI TVRNLITRKQ ISVPLENIED
     AIKQTL