ID   SYH_STREQ               Reviewed;         426 AA.
AC   P30053;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Histidine--tRNA ligase;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidyl-tRNA synthetase;
DE            Short=HisRS;
GN   Name=hisS;
OS   Streptococcus dysgalactiae subsp. equisimilis (Streptococcus equisimilis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=119602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=D181;
RX   PubMed=8441673; DOI=10.1093/nar/21.3.615;
RA   Menguito C.A., Keherly M.J., Tang C.-Y., Papaconstantinou J., Weigel P.H.;
RT   "Molecular cloning, sequence, structural analysis and expression of the
RT   histidyl-tRNA synthetase gene from Streptococcus equisimilis.";
RL   Nucleic Acids Res. 21:615-620(1993).
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.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA78919.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z17214; CAA78919.1; ALT_INIT; Genomic_DNA.
DR   PIR; S30233; S30233.
DR   AlphaFoldDB; P30053; -.
DR   SMR; P30053; -.
DR   BRENDA; 6.1.1.21; 5928.
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   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..426
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136262"
FT   CONFLICT        229
FT                   /note="Q -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   426 AA;  47932 MW;  DC902A63BFF5EBA8 CRC64;
     MKLQKPKGTQ DILSVAAAKW QYVEGVARET FKQYHYGEIR TPMFEHYEVI SRSVGDTTDI
     VTKEMYDFYD KGDRHITLRP EGTAPVVRSY VENKLFAPEV QKPVKLYYIG SMFRYERPQA
     GRLREFHQIG VECFGSANPA TDVETIAMAY HLFERLGIKG VTLHLNSLGN AASRAAYRQA
     LIDYLSPMRD TLSKDSQRRL DENPLRVLDS KEKEDKIAVA NAPSILDYQD EESQAHFDAV
     RSMLEALAIP YVIDTNMVRG LDYYNHTIFE FITEVDQSEL TICAGGRYDG LVEYFGGPAT
     PGFGFGLGLE RLLLILDKQG VELPVEEGLD VYIAVLGADA NVAALALTQA IRRQGFTVER
     DYLGRKIKAQ FKSADTFKAK VVITLGESEI KAGQAVLKHN QTRQEMTVSF DQIQTDFASI
     FAECVQ