KITH_ELHVK
ID KITH_ELHVK Reviewed; 356 AA.
AC Q18LE8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 34.
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 Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS (Elephant endotheliotropic herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Proboscivirus.
OX NCBI_TaxID=654902;
OH NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA Bennett M., Stewart J.P., Ulrich R.G.;
RT "Identification of novel rodent herpesviruses, including the first
RT gammaherpesvirus of Mus musculus.";
RL J. Virol. 81:8091-8100(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA Hentschke J.;
RT "Genetic and ultrastructural characterization of a European isolate of the
RT fatal endotheliotropic elephant herpesvirus.";
RL J. Gen. Virol. 82:475-482(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16963736; DOI=10.1099/vir.0.81977-0;
RA Ehlers B., Dural G., Marschall M., Schregel V., Goltz M., Hentschke J.;
RT "Endotheliotropic elephant herpesvirus, the first betaherpesvirus with a
RT thymidine kinase gene.";
RL J. Gen. Virol. 87:2781-2789(2006).
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; AF322977; ABG36571.1; -; Genomic_DNA.
DR SMR; Q18LE8; -.
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..356
FT /note="Thymidine kinase"
FT /id="PRO_0000408156"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 86
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 61..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ SEQUENCE 356 AA; 40857 MW; 243F25646927F3D1 CRC64;
MMDSRATYVP PKKISESNSN AEEDPTDCSK PITLKVPTVS ETVLATIPHK PQRHLTVYLE
GCVGVGKTTM FKYVVDNMFV HTAYDEPMDH WTKWFPENIL QTIHEAVNLP TQEQHAYVFS
CQNLIATSFL ARESGIVKTH PAPFDPSVDV ISIADRHALA AYVAFPIHHF LQGRFTYMEL
QCMLWAFKQD SVDTIFLLQG CSEETLRRVK RRNRKVEHGV TIEYINSLQA AYTVILSTWY
RATEYQYSAK RTVSEEISFF IAGPRRTLFY ILYDKRPITL PEIEILKLFR KISNDLKKLV
LIPVNFQRLV YSSALRRLQD LLIVTPGVTS YIHNENVDTA TCAVADNPHF NHHDVS