KITH_VACCC
ID KITH_VACCC Reviewed; 177 AA.
AC P68564; P03297;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Thymidine kinase;
DE EC=2.7.1.21;
GN Name=TK; ORFNames=J2R;
OS Vaccinia virus (strain Copenhagen) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10249;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "The complete DNA sequence of vaccinia virus.";
RL Virology 179:247-266(1990).
RN [2]
RP COMPLETE GENOME.
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL Virology 179:517-563(1990).
CC -!- FUNCTION: Phosphorylates thymidine and thymidine analogs, such as
CC azidothymidine (AZT). Part of the salvage pathway for pyrimidine
CC deoxyribonucleotide synthesis (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Homotetramer. Two molecules of substrate bind to each enzyme
CC tetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
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DR EMBL; M35027; AAA48082.1; -; Genomic_DNA.
DR PIR; A00609; KIVZ.
DR SMR; P68564; -.
DR Proteomes; UP000008269; 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..177
FT /note="Thymidine kinase"
FT /id="PRO_0000174938"
FT ACT_SITE 83
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 157..161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 177 AA; 20100 MW; 57E3595EBE6F3C54 CRC64;
MNGGHIQLII GPMFSGKSTE LIRRVRRYQI AQYKCVTIKY SNDNRYGTGL WTHDKNNFEA
LEATKLCDVL ESITDFSVIG IDEGQFFPDI VEFCERMANE GKIVIVAALD GTFQRKPFNN
ILNLIPLSEM VVKLTAVCMK CFKEASFSKR LGEETEIEII GGNDMYQSVC RKCYIDS