ID   SYTC_ENCCU              Reviewed;         640 AA.
AC   Q8SRH2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Probable threonine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.3;
DE   AltName: Full=Threonyl-tRNA synthetase;
DE            Short=ThrRS;
GN   OrderedLocusNames=ECU07_1570;
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-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-
CC         threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670,
CC         Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3;
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; AL590447; CAD25688.1; -; Genomic_DNA.
DR   RefSeq; NP_586084.1; NM_001041706.1.
DR   AlphaFoldDB; Q8SRH2; -.
DR   SMR; Q8SRH2; -.
DR   STRING; 284813.Q8SRH2; -.
DR   GeneID; 859518; -.
DR   KEGG; ecu:ECU07_1570; -.
DR   VEuPathDB; MicrosporidiaDB:ECU07_1570; -.
DR   HOGENOM; CLU_008554_0_1_1; -.
DR   InParanoid; Q8SRH2; -.
DR   OMA; IWDEAEK; -.
DR   OrthoDB; 813937at2759; -.
DR   Proteomes; UP000000819; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00771; ThrRS_core; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_00184; Thr_tRNA_synth; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
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; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR033728; ThrRS_core.
DR   InterPro; IPR012947; tRNA_SAD.
DR   PANTHER; PTHR11451; PTHR11451; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR01047; TRNASYNTHTHR.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF55186; SSF55186; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00418; thrS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..640
FT                   /note="Probable threonine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388384"
FT   DOMAIN          1..63
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
SQ   SEQUENCE   640 AA;  73945 MW;  6EF3BCF8641E2534 CRC64;
     MYEVKLKVEL EDKVLEVTQG TTPYDILCDY FKDRKDVISC RIDGVYSDMS SEILKDCKLE
     LMTFEDDGAR DIFWHSSAHV LGNALVNLYP DAKLVHGPPI EEGFFYDVDV TDPISSEDYE
     KIEEEMVKIM KKNYRFERVI KSKEELLEAY RDNPCKTHFI MKGVDKESSV YRNGDFFDMC
     LGPHIRSTGV IKAVKVLKNS SAYFLNDPNL KSLQRIYAIT FPSKGMMDEY LKRKEEAKER
     DHRKIGTELD LFFFSKYSPG SCFFLPNGTT MYNTLIEFLR EEYRKRGFKE VITPNIFCTQ
     LWEESGHLQN YKENMFIIEG DTFALKPMNC PGHCVMFRHQ DHSFRDLPLR LADFGVLHRN
     ELSGTLTGLT RVRRFQQDDA HIFCTKDQVK EEIKGCLEFL SFVYGVFGFR FELVLSTRPE
     KYLGSVDEWD RAEKALADAM DESNMPFKIN AGDGAFYGPK IDITLHDALG RRIQCATIQL
     DFQLPQRFEL KYRDSDGQCR TPVIIHRAIL GSIERMIAII LESFGKRLPF WISPRQIAIV
     NMGNPDYVGK VRSVLARFRL DVIDDGNTLS KRIRTAETSG YALVCVVGKK EAEANEINIR
     FNKSNRNIGL YELRDILDRM ADEKVELDSI LPIDKVSISK