SYTC_ENTBH
ID SYTC_ENTBH Reviewed; 634 AA.
AC B7XIA1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Probable threonine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.3;
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
GN ORFNames=EBI_22768;
OS Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Enterocytozoon.
OX NCBI_TaxID=481877;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348;
RX PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S.,
RA Keeling P.J.;
RT "Patterns of genome evolution among the microsporidian parasites
RT Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT bieneusi.";
RL PLoS ONE 2:E1277-E1277(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348;
RX PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT Enterocytozoon bieneusi.";
RL PLoS Pathog. 5:E1000261-E1000261(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABGB01000017; EED44394.1; -; Genomic_DNA.
DR RefSeq; XP_002649729.1; XM_002649683.1.
DR AlphaFoldDB; B7XIA1; -.
DR SMR; B7XIA1; -.
DR STRING; 481877.B7XIA1; -.
DR PRIDE; B7XIA1; -.
DR EnsemblFungi; EED44394; EED44394; EBI_22768.
DR VEuPathDB; MicrosporidiaDB:EBI_22768; -.
DR HOGENOM; CLU_008554_0_1_1; -.
DR InParanoid; B7XIA1; -.
DR Proteomes; UP000001742; 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: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; 3.30.930.10; -; 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; 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..634
FT /note="Probable threonine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000388385"
FT DOMAIN 1..61
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
SQ SEQUENCE 634 AA; 74069 MW; D4209979C67FB8E1 CRC64;
MSIYVTFKGQ VQKICISSGT ILQELISTHY PNKNIIACAI DGIMADINTE INENQKIELY
DFDSKEGQHV YWHSSAHILG NALVNLYQCK LVNGPALDEG FYYDIDIERP IREEDFADIE
KEMQRIINKN IDFRKKMIKK DDLLKMYKDN DYKVHFINNI PDNLISVYYN DEFYDMCQGP
HIQSTGLVKA FKILKSSSCY FLNSADNQIL QRIYGISFPN KTLLKEYEEK VQKAKEMDHR
KIGKELNLYF FHEYSPGSCF WLPDGVVIYN RLMEFLRKEY IKRGFKEVIT PNIFHIDLWK
ESGHYQNYKE NIYGISGEDF ALKPMNCPGH CIIFKSVERS YKELPLRYAD FGVLHRNECS
GSLTGLTRVR RFQQDDAHIF TSKSSIKEEI ENAIGFLKTV YSIFNFKYEL FLSTRPTKFL
GTIEEWDVAE KSLKDAIIDS GHTYTLNEGD GAFYGPKIDI ILHDILNRKI QCATIQLDFQ
LPQRFDLKFK NELGMYETPV IIHRAILGSF ERFIAILIES YGKHLPFWLH PRQVGLVTID
CKHENYMYTV EKSMLNVVLD LGIRKYTDPK DTLNKKIRKA TLDGCKIICI LGDKEMEKNE
VNVRIGNKTR TYKIEELLEK IKVSIETKKE FIFN