ID KITH_ILTVT Reviewed; 364 AA.
AC P23983;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_04029};
DE EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_04029};
GN Name=TK {ECO:0000255|HAMAP-Rule:MF_04029};
OS Infectious laryngotracheitis virus (strain Thorne V882) (ILTV) (Gallid
OS herpesvirus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Iltovirus;
OC Iltovirus gallidalpha1; Infectious laryngotracheitis virus.
OX NCBI_TaxID=10344;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2157797; DOI=10.1099/0022-1317-71-4-841;
RA Griffin A.M., Boursnell M.E.;
RT "Analysis of the nucleotide sequence of DNA from the region of the
RT thymidine kinase gene of infectious laryngotracheitis virus; potential
RT evolutionary relationships between the herpesvirus subfamilies.";
RL J. Gen. Virol. 71:841-850(1990).
CC -!- FUNCTION: Catalyzes the transfer of the gamma-phospho group of ATP to
CC thymidine to generate dTMP in the salvage pathway of pyrimidine
CC synthesis. The dTMP serves as a substrate for DNA polymerase during
CC viral DNA replication. Allows the virus to be reactivated and to grow
CC in non-proliferative cells lacking a high concentration of
CC phosphorylated nucleic acid precursors. {ECO:0000255|HAMAP-
CC Rule:MF_04029}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_04029};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_04029}.
CC -!- SIMILARITY: Belongs to the herpesviridae thymidine kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_04029}.
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DR EMBL; D00565; BAA00442.1; -; Genomic_DNA.
DR PIR; D43675; D43675.
DR RefSeq; YP_182352.1; NC_006623.1.
DR SMR; P23983; -.
DR GeneID; 3239035; -.
DR KEGG; vg:3239035; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006230; P:TMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_04029; HSV_KITH; 1.
DR InterPro; IPR001889; Herpes_TK.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00693; Herpes_TK; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA synthesis; Early protein; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..364
FT /note="Thymidine kinase"
FT /id="PRO_0000175081"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ SEQUENCE 364 AA; 40215 MW; C1C04A7342ECCF7E CRC64;
MAVAGAVKTS GGVQFCSEFE NDDSDFRRVV LLYVDGPFGV GKTVTAKTLM QMPNWRGCRL
YLAEPMQAWR QWFGGADMIK EINEIQTLKA SGKLECREAS PVAVAEVQMT IAAPLRIMNH
VIYNYLGSER CYSAAASGPD DVLFLVDRHP LAACLCFPVA QYLSGALEFG DLITLLSGIP
DIPTHSNIVL MDLDICEQAR RIIQRGRPGE TVDWTYLCAL RNSYICLMNT TTYLQRTSYP
ALLKEQEALT SATLLKFKRE CLETATVPEI NPSIDQTLFA ILAFDQQNVH GERLKTVLSF
VVQKLATVLK NLCIFYLPAH GLTPEACALK CLEFAETASS LTTKRAAIAS LIDAVERYNA
DMGS
//
