KITH_GAHVR
ID KITH_GAHVR Reviewed; 352 AA.
AC P17653;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-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 Gallid herpesvirus 2 (strain RB-1b) (GaHV-2) (Marek's disease herpesvirus
OS type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=33707;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2555435; DOI=10.1099/0022-1317-70-11-3055;
RA Scott S.D., Ross N.L.J., Binns M.M.;
RT "Nucleotide and predicted amino acid sequences of the Marek's disease virus
RT and turkey herpesvirus thymidine kinase genes; comparison with thymidine
RT kinase genes of other herpesviruses.";
RL J. Gen. Virol. 70:3055-3065(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; D13956; BAA03049.1; -; Genomic_DNA.
DR PIR; B33375; KIBEMV.
DR SMR; P17653; -.
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..352
FT /note="Thymidine kinase"
FT /id="PRO_0000175076"
FT ACT_SITE 54
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ SEQUENCE 352 AA; 40366 MW; 34A65B16BB18D002 CRC64;
MSEPQSWSVM ASQMTSAQLI RVYLDGSMGI GKTSMLNEIP THSLMGVPVL KVFEPMKYWR
YYFTDLVTTV NDTCDRRRRG EFSLFQSSMI VTALQSKFAD PYLVFHERLS SKCHRITGTR
GNPSLILILD RHPISATVCF PIARHLTGDC SLEMLISMII RLPQEPPGCN LVIVDLHDEK
EHVSRLSSRN RTGEKTDLLM LRALNAVYSC LVDTIMYANH ICPYSKDEWE SEWLDLPWFD
TSLATTFINE PRTDYRGSRV SLHHTLLAIF KRRELCAEDG SLSTTHAWIL WGLLMKLRNI
NVERFNITGL STTKCVESFM DTMSERLVTH SSWNDAFEIE ADVLAYNKEM AM
