ID   KITH_AMEPV              Reviewed;         182 AA.
AC   P28852;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   22-FEB-2023, entry version 81.
DE   RecName: Full=Thymidine kinase;
DE            EC=2.7.1.21;
GN   Name=TK; OrderedLocusNames=AMV016; ORFNames=Q2;
OS   Amsacta moorei entomopoxvirus (AmEPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Entomopoxvirinae; Betaentomopoxvirus.
OX   NCBI_TaxID=28321;
OH   NCBI_TaxID=340055; Amsacta.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1733099; DOI=10.1016/0042-6822(92)90016-i;
RA   Gruidl M.E., Hall R.L., Moyer R.W.;
RT   "Mapping and molecular characterization of a functional thymidine kinase
RT   from Amsacta moorei entomopoxvirus.";
RL   Virology 186:507-516(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1469363; DOI=10.1099/0022-1317-73-12-3235;
RA   Lytvyn V., Fortin Y., Banville M., Arif B., Richardson C.;
RT   "Comparison of the thymidine kinase genes from three entomopoxviruses.";
RL   J. Gen. Virol. 73:3235-3240(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10936094; DOI=10.1006/viro.2000.0449;
RA   Bawden A.L., Glassberg K.J., Diggans J., Shaw R., Farmerie W., Moyer R.W.;
RT   "Complete genomic sequence of the Amsacta moorei entomopoxvirus: analysis
RT   and comparison with other poxviruses.";
RL   Virology 274:120-139(2000).
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; D10679; BAA01525.1; -; Genomic_DNA.
DR   EMBL; M80924; AAA42386.1; -; Genomic_DNA.
DR   EMBL; AF250284; AAG02722.1; -; Genomic_DNA.
DR   PIR; B40818; KIVZAM.
DR   RefSeq; NP_064798.1; NC_002520.1.
DR   SMR; P28852; -.
DR   GeneID; 1494606; -.
DR   KEGG; vg:1494606; -.
DR   OrthoDB; 9611at10239; -.
DR   Proteomes; UP000000872; Genome.
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; 3.30.60.20; -; 1.
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   InterPro; IPR020633; Thymidine_kinase_CS.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN           1..182
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000174942"
FT   ACT_SITE        85
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   182 AA;  21241 MW;  982719AFC0DF8D2D CRC64;
     MSIELIIGPM FSGKTTELMR KINRYILSNQ KCVIITHNID NRFINKNIIN HDGNILNKEY
     LYIKTNNLIN EINIVDNYDI IGIDECQFFE ENDLEQFCDK MANNKKKVIV AGLNCDFNRN
     IFNSISKLIP KVEKIKKLQA ICQFCYKDAS FTIKKHNKNQ IIEIGGQDLY VPVCRLCYNN
     SY
//