ID   SYYC_NOSCE              Reviewed;         329 AA.
AC   C4V6W1;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Probable tyrosine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.1;
DE   AltName: Full=Tyrosyl-tRNA synthetase;
DE            Short=TyrRS;
GN   ORFNames=NCER_100158;
OS   Nosema ceranae (strain BRL01) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX   NCBI_TaxID=578460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRL01;
RX   PubMed=19503607; DOI=10.1371/journal.ppat.1000466;
RA   Cornman R.S., Chen Y.P., Schatz M.C., Street C., Zhao Y., Desany B.,
RA   Egholm M., Hutchison S., Pettis J.S., Lipkin W.I., Evans J.D.;
RT   "Genomic analyses of the microsporidian Nosema ceranae, an emergent
RT   pathogen of honey bees.";
RL   PLoS Pathog. 5:E1000466-E1000466(2009).
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; ACOL01000006; EEQ83027.1; -; Genomic_DNA.
DR   RefSeq; XP_002996698.1; XM_002996652.1.
DR   AlphaFoldDB; C4V6W1; -.
DR   SMR; C4V6W1; -.
DR   STRING; 578460.C4V6W1; -.
DR   EnsemblFungi; EEQ83027; EEQ83027; NCER_100158.
DR   KEGG; nce:NCER_100158; -.
DR   VEuPathDB; MicrosporidiaDB:NCER_100158; -.
DR   HOGENOM; CLU_035267_0_1_1; -.
DR   InParanoid; C4V6W1; -.
DR   OMA; PMVKIAE; -.
DR   Proteomes; UP000009082; Unassembled WGS sequence.
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   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..329
FT                   /note="Probable tyrosine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388401"
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   329 AA;  38145 MW;  27A1DA2CAA999925 CRC64;
     MDTTEKLKLI NRNLKEVIGG DIMEKIINKR DLNVYWGTAT TGKPHIAYFL PILKIKDFVD
     AGCNVTILLA DIHAFLDNLK APIEKIECRS QYYKKIITLM LKSIKVDVSK ISFIFGSEYQ
     KSNKYFTDIL RILNQTKKND ARRAGSEVVK QVKNSKLSSL VYPAMQALDE EYLNVDVQFG
     GIDQRKIFMY AREFLPLLKY KKRIHLMNPM IPGLNSDKMS SSDIDSKIDL LDTKLEIYKK
     IHNCSLENEG LIFLFKSIIY PYCSIFNLQI MISGKVYTFD KLYEDIKMKI IDETELKNIA
     SDMIERLICP IRDEMLRDLK LIENAYGNK