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P0C0E6 (KITH_VZVO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thymidine kinase

EC=2.7.1.21
Gene names
ORF Names:ORF36
OrganismVaricella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3) [Complete proteome]
Taxonomic identifier341980 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeVaricellovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In latent infection, may allow the virus to be reactivated and to grow in cells lacking a high concentration of phosphorylated nucleic acid precursors, such as nerve cells that do not replicate their genome By similarity.

Catalytic activity

ATP + thymidine = ADP + thymidine 5'-phosphate.

Subunit structure

Homodimer By similarity.

Miscellaneous

Phosphorylates and thereby activates certain drugs like acyclovir (ACV), valacyclovir, and famciclovir to a toxic form, that leads to successful suppression of the infection, while the uninfected cell does not have this ability because it lacks TK. Mutations in thymidine kinase may induce HSV resistance to antiviral therapies in immunocompromised patients. The most frequently observed resistant strains are unable to express TK and are avirulent in animal models of disease. Resistance may be acquired less frequently by selecting variants which no longer recognize ACV or ACV triphosphate as substrates but which retain normal functions By similarity.

Sequence similarities

Belongs to the herpesviridae thymidine kinase family.

Ontologies

Keywords
   Biological processDNA synthesis
   Developmental stageEarly protein
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

TMP biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

thymidine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341Thymidine kinase
PRO_0000175087

Regions

Nucleotide binding19 – 268ATP

Sites

Active site481Proton acceptor Potential
Binding site661Substrate
Binding site901Substrate
Binding site1391Substrate By similarity
Binding site1831ATP By similarity

Secondary structure

..................................................... 341
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C0E6 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: F38ACC39751C076A

FASTA34137,843
        10         20         30         40         50         60 
MSTDKTDVKM GVLRIYLDGA YGIGKTTAAE EFLHHFAITP NRILLIGEPL SYWRNLAGED 

        70         80         90        100        110        120 
AICGIYGTQT RRLNGDVSPE DAQRLTAHFQ SLFCSPHAIM HAKISALMDT STSDLVQVNK 

       130        140        150        160        170        180 
EPYKIMLSDR HPIASTICFP LSRYLVGDMS PAALPGLLFT LPAEPPGTNL VVCTVSLPSH 

       190        200        210        220        230        240 
LSRVSKRARP GETVNLPFVM VLRNVYIMLI NTIIFLKTNN WHAGWNTLSF CNDVFKQKLQ 

       250        260        270        280        290        300 
KSECIKLREV PGIEDTLFAV LKLPELCGEF GNILPLWAWG METLSNCLRS MSPFVLSLEQ 

       310        320        330        340 
TPQHAAQELK TLLPQMTPAN MSSGAWNILK ELVNAVQDNT S 

« Hide

References

« Hide 'large scale' references
[1]"Molecular analysis of the pyrimidine deoxyribonucleoside kinase gene of wild-type and acyclovir-resistant strains of varicella-zoster virus."
Sawyer M.H., Inchauspe G., Biron K.K., Waters D.J., Straus S.E., Ostrove J.M.
J. Gen. Virol. 69:2585-2593(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular analysis of the thymidine kinase gene of thymidine kinase-deficient mutants of varicella-zoster virus."
Mori H., Shiraki K., Kato T., Hayakawa Y., Yamanishi K., Takahashi M.
Intervirology 29:301-310(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Analysis of mutations in the thymidine kinase genes of drug-resistant varicella-zoster virus populations using the polymerase chain reaction."
Lacey S.F., Suzutani T., Powell K.L., Purifoy D.J., Honess R.W.
J. Gen. Virol. 72:623-630(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 9883 and YS.
[4]"Comparison of the complete DNA sequences of the Oka varicella vaccine and its parental virus."
Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.
J. Virol. 76:11447-11459(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Isolate Human/Japan/P-Oka/1970 and Oka varicella vaccine Biken (V-Oka-Biken).
[5]"Complete DNA sequences of two oka strain varicella-zoster virus genomes."
Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M., Vassilev V.
J. Virol. 82:11023-11044(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Oka varicella vaccine VarilRix (V-Oka-GSK) and Oka varicella vaccine Varivax V-Oka-Merk).
[6]"Crystal structure of varicella zoster virus thymidine kinase."
Bird L.E., Ren J., Wright A., Leslie K.D., Degreve B., Balzarini J., Stammers D.K.
J. Biol. Chem. 278:24680-24687(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH ADP AND BROMOVINYL-DEOXYURIDINE-MONOPHOSPHATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36160 Genomic DNA. Translation: AAA45865.1.
AB009252 Genomic DNA. Translation: BAA23727.2.
AB009253 Genomic DNA. Translation: BAA23728.2.
AB097932 Genomic DNA. No translation available.
AB097933 Genomic DNA. No translation available.
DQ008354 Genomic DNA. Translation: AAY57648.1.
DQ008355 Genomic DNA. Translation: AAY57719.1.
PIRKIBEEL. A28930.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OSNX-ray3.20A/B/C/D1-341[»]
ProteinModelPortalP0C0E6.
SMRP0C0E6. Positions 8-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0C0E6. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR001889. Herpes_TK.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00693. Herpes_TK. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0C0E6.

Entry information

Entry nameKITH_VZVO
AccessionPrimary (citable) accession number: P0C0E6
Secondary accession number(s): O57298, P14344, Q4JQT9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: April 16, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references