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Q65DU6 (KITH_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:tdk
Ordered Locus Names:BLi03954, BL03975
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + thymidine = ADP + thymidine 5'-phosphate. HAMAP-Rule MF_00124

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00124

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00124.

Sequence similarities

Belongs to the thymidine kinase family.

Ontologies

Keywords
   Biological processDNA synthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

thymidine kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194Thymidine kinase HAMAP-Rule MF_00124
PRO_0000174961

Regions

Nucleotide binding15 – 228ATP By similarity
Nucleotide binding88 – 914ATP By similarity

Sites

Active site891Proton acceptor Potential
Metal binding1451Zinc By similarity
Metal binding1481Zinc By similarity
Metal binding1831Zinc By similarity
Metal binding1861Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65DU6 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: CF99EAE939FD14A1

FASTA19421,298
        10         20         30         40         50         60 
MYIMKQSGWL ELICGSMFSG KSEELIRRIK RATFAKQEVK VFKPAIDNRY SSESVVSHNG 

        70         80         90        100        110        120 
TSIVCHAIAS PEEIFQYISK ETDVIGVDEV QFFDETIVGT LTSLADQGYR VIAAGLDLDF 

       130        140        150        160        170        180 
RGEPFGVVPD LMALAETVTK LQAVCSVCGS PASRTQRLIN GKPASYDDPV ILVGASEAYE 

       190 
ARCRHHHEVP GNPK 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU42768.1.
CP000002 Genomic DNA. Translation: AAU25393.1.
RefSeqYP_006715231.1. NC_006322.1.
YP_081031.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65DU6.
SMRQ65DU6. Positions 1-191.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL03975.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU25393; AAU25393; BL03975.
AAU42768; AAU42768; BLi03954.
GeneID3027778.
3101344.
KEGGbld:BLi03954.
bli:BL03975.
PATRIC18953702. VBIBacLic203714_4026.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1435.
HOGENOMHOG000076390.
KOK00857.
OMAELICGSM.
OrthoDBEOG69D3J2.
ProtClustDBPRK04296.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-3907-MONOMER.

Family and domain databases

HAMAPMF_00124. Thymidine_kinase.
InterProIPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
IPR020634. Thymidine_kinase_subgr.
[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...

Entry information

Entry nameKITH_BACLD
AccessionPrimary (citable) accession number: Q65DU6
Secondary accession number(s): Q62PB8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: October 25, 2004
Last modified: April 16, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families