Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P24425 (KITH_EHV4) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 67. 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
OrganismEquine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus)
Taxonomic identifier10333 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeVaricellovirus
Virus hostEquus caballus (Horse) [TaxID: 9796]

Protein attributes

Sequence length352 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. Ref.2

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the herpesviridae thymidine kinase family.

Ontologies

Keywords
   Biological processDNA synthesis
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
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 – 352352Thymidine kinase
PRO_0000175067

Regions

Nucleotide binding32 – 398ATP

Sites

Active site601Proton acceptor Potential
Binding site781Substrate
Binding site1021Substrate
Binding site1051Substrate
Binding site1481Substrate
Binding site1921ATP

Secondary structure

..................................................... 352
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24425 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: F925ACF592077456

FASTA35238,784
        10         20         30         40         50         60 
MAACVPPGEA PRSASGTPTR RQVTIVRIYL DGVYGIGKST TGRVMASAAS GGSPTLYFPE 

        70         80         90        100        110        120 
PMAYWRTLFE TDVISGIYDT QNRKQQGNLA VDDAALITAH YQSRFTTPYL ILHDHTCTLF 

       130        140        150        160        170        180 
GGNSLQRGTQ PDLTLVFDRH PVASTVCFPA ARYLLGDMSM CALMAMVATL PREPQGGNIV 

       190        200        210        220        230        240 
VTTLNVEEHI RRLRTRARIG EQIDITLIAT LRNVYFMLVN TCHFLRSGRV WRDGWGELPT 

       250        260        270        280        290        300 
SCGAYKHRAT QMDAFQERVS PELGDTLFAL FKTQELLDDR GVILEVHAWA LDALMLKLRN 

       310        320        330        340        350 
LNVFSADLSG TPRQCAAVVE SLLPLMSSTL SDFDSASALE RAARTFNAEM GV 

« Hide

References

[1]"The nucleotide sequence of the equine herpesvirus 4 thymidine kinase gene."
Nicolson L., Cullinane A.A., Onions D.E.
J. Gen. Virol. 71:1801-1805(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structural basis for the dual thymidine and thymidylate kinase activity of herpes thymidine kinases."
Gardberg A., Shuvalova L., Monnerjahn C., Konrad M., Lavie A.
Structure 11:1265-1277(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-352 IN COMPLEXES WITH THYMIDINE; ADP AND BISUBSTRATE ANALOGS, ACTIVE SITE, CATALYTIC ACTIVITY, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14486 Genomic DNA. Translation: BAA03378.1.
PIRKIBEE4. A36657.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P6XX-ray2.00A/B23-352[»]
1P72X-ray2.10A/B23-352[»]
1P73X-ray2.70A/B/C/D23-352[»]
1P75X-ray3.02A/B/C/D23-352[»]
ProteinModelPortalP24425.
SMRP24425. Positions 23-352.
ModBaseSearch...
MobiDBSearch...

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

EvolutionaryTraceP24425.

Entry information

Entry nameKITH_EHV4
AccessionPrimary (citable) accession number: P24425
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: April 16, 2014
This is version 67 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