ID   SYYC_ENCCU              Reviewed;         337 AA.
AC   Q8SRV7;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Probable tyrosine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.1;
DE   AltName: Full=Tyrosyl-tRNA synthetase;
DE            Short=TyrRS;
GN   OrderedLocusNames=ECU05_1120i;
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-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC         tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC         Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AL590445; CAD26632.1; -; Genomic_DNA.
DR   RefSeq; NP_597455.1; NM_001041321.1.
DR   AlphaFoldDB; Q8SRV7; -.
DR   SMR; Q8SRV7; -.
DR   STRING; 284813.Q8SRV7; -.
DR   GeneID; 859121; -.
DR   KEGG; ecu:ECU05_1120i; -.
DR   VEuPathDB; MicrosporidiaDB:ECU05_1120i; -.
DR   HOGENOM; CLU_035267_0_1_1; -.
DR   InParanoid; Q8SRV7; -.
DR   OMA; YIGFEIS; -.
DR   OrthoDB; 852081at2759; -.
DR   Proteomes; UP000000819; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00805; TyrRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR023617; Tyr-tRNA-ligase_arc/euk-type.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PIRSF; PIRSF006588; TyrRS_arch_euk; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..337
FT                   /note="Probable tyrosine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388399"
FT   MOTIF           40..48
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           218..222
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   337 AA;  39143 MW;  F36949226D26B983 CRC64;
     MSVEQKLYLI TRNLQEILGE EELKRIVSER ELNVYWGTAI TGKPHIAYLV PLMKIKDFVD
     AGCNVKILFA DIHGFLDNLK APIEKVQHRC AYYEKLIKSA LKMLCVDLDR IQFVKGSEFQ
     KSERYTMDLY RILSITSKHD AKKAGAEVVR QVENPMVSSL VYPSMQALDE VHLSVDAQFG
     GVDQRKIFTY ARKYLPLLNY EKRIHLMSPM LPGLNSDKMS SSDDLSKIDL MDSKEAIWRK
     IRKCFCEEGN KDNGLMMIFS HIVFPILQLK GECVRITDRD GREMAFEKYQ EFEEEFVRKS
     IHPGDLKSNA ARLIDEIIRP IREEMEKDLD MVREAYN