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O57203 (KITH_VACCA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 64. 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
Name:TK
Ordered Locus Names:MVA086R, ACAM3000_MVA_086
ORF Names:J2R
OrganismVaccinia virus (strain Ankara) (VACV)
Taxonomic identifier126794 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylates thymidine and thymidine analogs, such as azidothymidine (AZT). Part of the salvage pathway for pyrimidine deoxyribonucleotide synthesis. Ref.3

Catalytic activity

ATP + thymidine = ADP + thymidine 5'-phosphate. Ref.3

Subunit structure

Homotetramer By similarity. Two molecules of substrate bind to each enzyme tetramer By similarity. Ref.3

Sequence similarities

Belongs to the thymidine kinase family.

Ontologies

Keywords
   Biological processDNA synthesis
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion 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 – 177177Thymidine kinase
PRO_0000174937

Regions

Nucleotide binding11 – 188ATP Probable
Region157 – 1615Substrate binding

Sites

Active site831Proton acceptor Potential
Metal binding1381Zinc
Metal binding1411Zinc
Metal binding1701Zinc
Metal binding1731Zinc
Binding site1131Substrate; via amide nitrogen

Secondary structure

.................................... 177
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O57203 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 57E19BCEBE6F3C54

FASTA17720,028
        10         20         30         40         50         60 
MNGGHIQLII GPMFSGKSTE LIRRVRRYQI AQYKCVTIKY SNDNRYGTGL WTHDKNNFEA 

        70         80         90        100        110        120 
LEATKLCDVL ESITDFSVIG IDEGQFFPDI VEFCERMANE GKIVIVAALD GTFQRKPFNN 

       130        140        150        160        170 
ILNLIPLSEM VVKLTAVCMK CFKEASFSKR LGEETEIEII GGNDMYQSVC RKCYVGS 

« Hide

References

« Hide 'large scale' references
[1]"The complete genomic sequence of the modified vaccinia Ankara strain: comparison with other orthopoxviruses."
Antoine G., Scheiflinger F., Dorner F., Falkner F.G.
Virology 244:365-396(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J., Khristova M., Wohlhueter R.M.
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Isolate Acambis 3000.
[3]"Structure of vaccinia virus thymidine kinase in complex with dTTP: insights for drug design."
El Omari K., Solaroli N., Karlsson A., Balzarini J., Stammers D.K.
BMC Struct. Biol. 6:22-22(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND TTP, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U94848 Genomic DNA. Translation: AAB96503.1.
AY603355 Genomic DNA. Translation: AAT10484.1.
PIRT37362.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J87X-ray3.10A/B/C/D1-177[»]
ProteinModelPortalO57203.
SMRO57203. Positions 4-176.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.7.1.21. 6591.

Family and domain databases

InterProIPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
[Graphical view]
PANTHERPTHR11441. PTHR11441. 1 hit.
PfamPF00265. TK. 1 hit.
[Graphical view]
PIRSFPIRSF035805. TK_cell. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00603. TK_CELLULAR_TYPE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO57203.

Entry information

Entry nameKITH_VACCA
AccessionPrimary (citable) accession number: O57203
Secondary accession number(s): Q6J3E4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 64 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