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Protein

Thymidine kinase

Gene

tdk

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei89 – 891Proton acceptorUniRule annotation
Binding sitei120 – 1201Substrate; via amide nitrogen
Metal bindingi145 – 1451Zinc
Metal bindingi148 – 1481Zinc
Binding sitei179 – 1791SubstrateBy similarity
Metal bindingi183 – 1831Zinc
Metal bindingi186 – 1861Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 228ATPUniRule annotation
Nucleotide bindingi88 – 914ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. thymidine kinase activity Source: UniProtKB-HAMAP
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. DNA biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

DNA synthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciBCER226900:GJEU-5322-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidine kinaseUniRule annotation (EC:2.7.1.21UniRule annotation)
Gene namesi
Name:tdkUniRule annotation
Ordered Locus Names:BC_5330
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001417 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 195195Thymidine kinasePRO_0000174955Add
BLAST

Proteomic databases

PRIDEiQ814U0.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi226900.BC5330.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JA1X-ray2.80A1-195[»]
ProteinModelPortaliQ814U0.
SMRiQ814U0. Positions 1-191.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ814U0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni170 – 1745Substrate binding

Sequence similaritiesi

Belongs to the thymidine kinase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1435.
KOiK00857.
OMAiVITGPMY.
OrthoDBiEOG69D3J2.

Family and domain databases

HAMAPiMF_00124. Thymidine_kinase.
InterProiIPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
[Graphical view]
PANTHERiPTHR11441. PTHR11441. 1 hit.
PfamiPF00265. TK. 1 hit.
[Graphical view]
PIRSFiPIRSF035805. TK_cell. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00603. TK_CELLULAR_TYPE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q814U0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYLINQNGWI EVICGSMFSG KSEELIRRVR RTQFAKQHAI VFKPCIDNRY
60 70 80 90 100
SEEDVVSHNG LKVKAVPVSA SKDIFEHITE ELDVIAIDEV QFFDGDIVEV
110 120 130 140 150
VQVLANRGYR VIVAGLDQDF RGLPFGQVPQ LMAIAEHVTK LQAVCSVCGS
160 170 180 190
PASRTQRLID GEPAAFDDPI ILVGASESYE PRCRHCHAVP ANKDK
Length:195
Mass (Da):21,696
Last modified:June 1, 2003 - v1
Checksum:i937F6D890890302E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP12193.1.
RefSeqiNP_834992.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP12193; AAP12193; BC_5330.
GeneIDi1207670.
KEGGibce:BC5330.
PATRICi32606864. VBIBacCer54481_5503.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP12193.1.
RefSeqiNP_834992.1. NC_004722.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JA1X-ray2.80A1-195[»]
ProteinModelPortaliQ814U0.
SMRiQ814U0. Positions 1-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC5330.

Proteomic databases

PRIDEiQ814U0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP12193; AAP12193; BC_5330.
GeneIDi1207670.
KEGGibce:BC5330.
PATRICi32606864. VBIBacCer54481_5503.

Phylogenomic databases

eggNOGiCOG1435.
KOiK00857.
OMAiVITGPMY.
OrthoDBiEOG69D3J2.

Enzyme and pathway databases

BioCyciBCER226900:GJEU-5322-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ814U0.

Family and domain databases

HAMAPiMF_00124. Thymidine_kinase.
InterProiIPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
[Graphical view]
PANTHERiPTHR11441. PTHR11441. 1 hit.
PfamiPF00265. TK. 1 hit.
[Graphical view]
PIRSFiPIRSF035805. TK_cell. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00603. TK_CELLULAR_TYPE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711.
  2. "Structural studies of thymidine kinases from Bacillus anthracis and Bacillus cereus provide insights into quaternary structure and conformational changes upon substrate binding."
    Kosinska U., Carnrot C., Sandrini M.P., Clausen A.R., Wang L., Piskur J., Eriksson S., Eklund H.
    FEBS J. 274:727-737(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND TTP, SUBUNIT.

Entry informationi

Entry nameiKITH_BACCR
AccessioniPrimary (citable) accession number: Q814U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: June 1, 2003
Last modified: April 29, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.