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Protein

Thymidylate kinase

Gene

TMK

Organism
Vaccinia virus (strain Copenhagen) (VACV)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Poxvirus TMP kinase is able to phosphorylate dTMP, dUMP and also dGMP from any purine and pyrimidine nucleoside triphosphate. The large substrate specificity is explained by the presence of a canal connecting the edge of the dimer interface to the TMP base binding pocket, canal not found in the human homolog (By similarity).By similarity

Catalytic activityi

ATP + dTMP = ADP + dTDP.

Pathwayi: dTTP biosynthesis

This protein is involved in the pathway dTTP biosynthesis, which is part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the pathway dTTP biosynthesis and in Pyrimidine metabolism.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 188ATPCurated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.4.9. 6591.
UniPathwayiUPA00575.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidylate kinase (EC:2.7.4.9)
Alternative name(s):
dTMP kinase
Gene namesi
Name:TMK
ORF Names:A48R
OrganismiVaccinia virus (strain Copenhagen) (VACV)
Taxonomic identifieri10249 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008269 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204Thymidylate kinasePRO_0000155217Add
BLAST

Interactioni

Subunit structurei

Homodimer; the dimer arrangement is orthogonal and not antiparallel as in human enzyme.By similarity

Protein-protein interaction databases

DIPiDIP-48617N.

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Helixi17 – 2610Combined sources
Helixi30 – 323Combined sources
Beta strandi33 – 397Combined sources
Helixi44 – 5310Combined sources
Helixi61 – 7313Combined sources
Helixi76 – 849Combined sources
Beta strandi88 – 936Combined sources
Helixi95 – 10410Combined sources
Helixi109 – 1168Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi123 – 1286Combined sources
Helixi132 – 1354Combined sources
Beta strandi140 – 1423Combined sources
Helixi148 – 16114Combined sources
Beta strandi168 – 1714Combined sources
Helixi177 – 19418Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V54X-ray2.40A/B1-204[»]
2W0SX-ray2.92A/B1-204[»]
ProteinModelPortaliP68693.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68693.

Family & Domainsi

Sequence similaritiesi

Belongs to the thymidylate kinase family.Curated

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR018095. Thymidylate_kin_CS.
IPR018094. Thymidylate_kinase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00041. DTMP_kinase. 1 hit.
PROSITEiPS01331. THYMIDYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P68693-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRGALIVFE GLDKSGKTTQ CMNIMESIPA NTIKYLNFPQ RSTVTGKMID
60 70 80 90 100
DYLTRKKTYN DHIVNLLFCA NRWEFASFIQ EQLEQGITLI VDRYAFSGVA
110 120 130 140 150
YAAAKGASMT LSKSYESGLP KPDLVIFLES GSKEINRNVG EEIYEDVTFQ
160 170 180 190 200
QKVLQEYKKM IEEGDIHWQI ISSEFEEDVK KELIKNIVIE AIHTVTGPVG

QLWM
Length:204
Mass (Da):23,219
Last modified:December 7, 2004 - v1
Checksum:i911DFD2C671CF6B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35027 Genomic DNA. Translation: AAA48180.1.
PIRiE42522. KIVZ5W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35027 Genomic DNA. Translation: AAA48180.1.
PIRiE42522. KIVZ5W.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V54X-ray2.40A/B1-204[»]
2W0SX-ray2.92A/B1-204[»]
ProteinModelPortaliP68693.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48617N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00575.
BRENDAi2.7.4.9. 6591.

Miscellaneous databases

EvolutionaryTraceiP68693.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR018095. Thymidylate_kin_CS.
IPR018094. Thymidylate_kinase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00041. DTMP_kinase. 1 hit.
PROSITEiPS01331. THYMIDYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Appendix to 'The complete DNA sequence of vaccinia virus'."
    Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P., Paoletti E.
    Virology 179:517-563(1990)
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Crystal structure of poxvirus thymidylate kinase: an unexpected dimerization has implications for antiviral therapy."
    Caillat C., Topalis D., Agrofoglio L.A., Pochet S., Balzarini J., Deville-Bonne D., Meyer P.
    Proc. Natl. Acad. Sci. U.S.A. 105:16900-16905(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Entry informationi

Entry nameiKTHY_VACCC
AccessioniPrimary (citable) accession number: P68693
Secondary accession number(s): P13410
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 7, 2004
Last modified: April 1, 2015
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.