KITH_AMEPV
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 03-AUG-2022, entry version 79.
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 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; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001267; Thymidine_kinase.
DR InterPro; IPR020633; Thymidine_kinase_CS.
DR PANTHER; PTHR11441; PTHR11441; 1.
DR Pfam; PF00265; TK; 1.
DR PIRSF; PIRSF035805; TK_cell; 1.
DR SUPFAM; SSF52540; SSF52540; 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
