ID   SYHC_ENCCU              Reviewed;         435 AA.
AC   Q8SRR3;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Probable histidine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidyl-tRNA synthetase;
DE            Short=HisRS;
GN   OrderedLocusNames=ECU06_0620;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AL590446; CAD25422.1; -; Genomic_DNA.
DR   RefSeq; NP_585818.1; NM_001041440.1.
DR   AlphaFoldDB; Q8SRR3; -.
DR   SMR; Q8SRR3; -.
DR   STRING; 284813.Q8SRR3; -.
DR   GeneID; 859242; -.
DR   KEGG; ecu:ECU06_0620; -.
DR   VEuPathDB; MicrosporidiaDB:ECU06_0620; -.
DR   HOGENOM; CLU_025113_4_2_1; -.
DR   InParanoid; Q8SRR3; -.
DR   OMA; YQIQKVW; -.
DR   OrthoDB; 1065556at2759; -.
DR   Proteomes; UP000000819; Chromosome VI.
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   CDD; cd00859; HisRS_anticodon; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 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   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="Probable histidine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388403"
SQ   SEQUENCE   435 AA;  49035 MW;  CC9DFF63EF442CAD CRC64;
     MTSLKTPKGT MDESPRQCFL HEEIIERIRR VFVLYGAVPI STPTFEMKSI LTNKYGEDTK
     LIYDLKDQGG EICALRYDLT VPFARYLASN KIRRMKRYQI GRVYRRDQPS IARGRLREFV
     QADFDIAGEC IQMMADAEVV SCVDRILSMF GIGEYRIKVN DRRILTSILE VVGVSCESYG
     TVCSTIDKIE KMSWEDIGRE LVLKGLSEEQ VRTTKKYMTM GGKEDVLGLL KADPVYGIER
     CKAAVHDMEE LFRLCRILGC SGSLVMDISL ARGLDYYTGM ILEAEYVGKS VGSVIGGGRY
     DNLTENLGER CVSTPCVGFS VGVSRIFSLL YEEYDKESST MVYVGASGGL FLDERLSVLR
     ILQDANICSE TFYTRRSSFE SQQKYVAKKK IPFIVVVGES EIAAGSVQVI NALTRKKEIV
     KVEQMVSYLL DPENQ