KITH_MEHVF
ID KITH_MEHVF Reviewed; 310 AA.
AC P13157;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Meleagrid herpesvirus 1 (strain FC126) (MeHV-1) (Turkey herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10391;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2724415; DOI=10.1128/jvi.63.6.2847-2852.1989;
RA Martin S.L., Aparisio D.I., Bandyopadhyay P.K.;
RT "Genetic and biochemical characterization of the thymidine kinase gene from
RT herpesvirus of turkeys.";
RL J. Virol. 63:2847-2852(1989).
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; M26659; AAA46109.1; -; Genomic_DNA.
DR SMR; P13157; -.
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; -; 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; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA synthesis; Early protein; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..310
FT /note="Thymidine kinase"
FT /id="PRO_0000175079"
FT ACT_SITE 45
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ SEQUENCE 310 AA; 35512 MW; 9F796BD643EB6F38 CRC64;
MALPRRPPTL TRVYLDGPFG IGKTSILNAM PDHTPDGAPI LKVYEPMKYW RCQSTDLVVA
ANETPERRRG GALSRFQSDM IMASIQARFA DPYLLFHERL SSKCRGKIEI CDTPAIILML
DRHPVAAILC FPITRYLLGE YSLEMLISSI IRLPLESPGC NLTVTILPDE KEHVNRICSR
DRPGETADRN MLRTLNAVYA SLVDTVKYAN LTCPYEKESW EMEWLGLPWF EESLLEEFIS
RPRPVICSRT RMPLDRTLLA IFKRKELCSE NGELLTQYSW ILWGLLTKLH TINVELFDIS
GMSRRECATL
