ID KITH_ENCCU Reviewed; 232 AA.
AC O96720; Q8SSL4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 3.
DT 28-JUN-2023, entry version 93.
DE RecName: Full=Thymidine kinase;
DE EC=2.7.1.21;
GN Name=TK; OrderedLocusNames=ECU01_0740i;
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=11157783; DOI=10.1101/gr.164301;
RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA Weissenbach J., Saurin W., Vivares C.P.;
RT "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT parasite Encephalitozoon cuniculi (Microspora).";
RL Genome Res. 11:198-207(2001).
RN [2]
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).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=GB-M1;
RX PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT "Identification of transcriptional signals in Encephalitozoon cuniculi
RT widespread among Microsporidia phylum: support for accurate structural
RT genome annotation.";
RL BMC Genomics 10:607-607(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-232.
RA Duffieux F., Peyret P., Roe B.A., Vivares C.P.;
RT "Putative thymidine kinase of Encephalitozoon cuniculi (Microspora) from
RT the chromosome I.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
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DR EMBL; AL391737; CAD24944.2; -; Genomic_DNA.
DR EMBL; AJ006824; CAA07261.1; -; Genomic_DNA.
DR RefSeq; XP_965909.1; XM_960816.1.
DR AlphaFoldDB; O96720; -.
DR SMR; O96720; -.
DR STRING; 284813.O96720; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_0740i; -.
DR HOGENOM; CLU_064400_2_2_1; -.
DR InParanoid; O96720; -.
DR OrthoDB; 196566at2759; -.
DR Proteomes; UP000000819; Chromosome I.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001267; Thymidine_kinase.
DR PANTHER; PTHR11441; THYMIDINE KINASE; 1.
DR PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1.
DR Pfam; PF00265; TK; 1.
DR PIRSF; PIRSF035805; TK_cell; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..232
FT /note="Thymidine kinase"
FT /id="PRO_0000174951"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 63..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 106..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 232 AA; 25958 MW; 3017360E71AF9BBA CRC64;
MDLAVLEWKS IKRRNAPTAE MTRGTLNFVT SPMNAGKTAN MLLRARHAAT LGRRVLLAKP
LSDTRHESSV IRSRCGIEMK CDLCAGPEFS FTKDVLYGDV DILLVDEAQF LSSRQIDELR
EVADVHGIPV WCYGLLTDFK KNLFEGSKRL VELCDKMIEL DIVCYFCKAD GRFHLKYANG
KAVVEGPSID ISIPGDGKFV AVCHMCWTEK TSTSEEVQDP RVLCAKVIPV DR
//
