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Protein

Thymidine kinase

Gene

tdk

Organism
Bacillus anthracis
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

BioCyciANTHRA:TDK-MONOMER.
BANT260799:GJAJ-5254-MONOMER.
BANT261594:GJ7F-5433-MONOMER.
MetaCyc:MONOMER-17898.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidine kinaseUniRule annotation (EC:2.7.1.21UniRule annotation)
Gene namesi
Name:tdkUniRule annotation
Ordered Locus Names:BA_5573, GBAA_5573, BAS5179
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000000427: Chromosome, UP000000594: Chromosome, UP000005639: Chromosome

Subcellular locationi

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 – 194194Thymidine kinasePRO_0000174953Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 PublicationUniRule annotation

Protein-protein interaction databases

IntActiQ81JX0. 5 interactions.
STRINGi198094.BA_5573.

Structurei

Secondary structure

1
194
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 146Combined sources
Helixi21 – 3414Combined sources
Beta strandi39 – 435Combined sources
Beta strandi65 – 673Combined sources
Helixi71 – 777Combined sources
Beta strandi84 – 874Combined sources
Helixi90 – 923Combined sources
Helixi97 – 10610Combined sources
Beta strandi110 – 1156Combined sources
Helixi128 – 1347Combined sources
Beta strandi136 – 1405Combined sources
Turni146 – 1483Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi154 – 1596Combined sources
Turni176 – 1783Combined sources
Beta strandi179 – 1824Combined sources
Turni184 – 1863Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J9RX-ray2.70A1-194[»]
ProteinModelPortaliQ81JX0.
SMRiQ81JX0. Positions 1-190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ81JX0.

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.
HOGENOMiHOG000076390.
KOiK00857.
OMAiVITGPMY.
OrthoDBiEOG69D3J2.

Family and domain databases

HAMAPiMF_00124. Thymidine_kinase.
InterProiIPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
IPR020634. Thymidine_kinase_subgr.
[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.

Q81JX0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYLINQNGWI EVICGSMFSG KSEELIRRVR RTQFAKQHAI VFKPCIDNRY
60 70 80 90 100
SEEDVVSHNG LKVKAVPVSA SKDIFKHITE EMDVIAIDEV QFFDGDIVEV
110 120 130 140 150
VQVLANRGYR VIVAGLDQDF RGLPFGQVPQ LMAIAEHVTK LQAVCSACGS
160 170 180 190
PASRTQRLID GEPAAFDDPI ILVGASESYE PRCRHCHAVP TKQR
Length:194
Mass (Da):21,642
Last modified:June 1, 2003 - v1
Checksum:iD2A9B182355D9D13
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP29216.1.
AE017334 Genomic DNA. Translation: AAT34716.1.
AE017225 Genomic DNA. Translation: AAT57468.1.
RefSeqiNP_847730.1. NC_003997.3.
YP_022241.1. NC_007530.2.
YP_031418.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP29216; AAP29216; BA_5573.
AAT34716; AAT34716; GBAA_5573.
AAT57468; AAT57468; BAS5179.
GeneIDi1085264.
2819897.
2851937.
KEGGiban:BA_5573.
bar:GBAA_5573.
bat:BAS5179.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP29216.1.
AE017334 Genomic DNA. Translation: AAT34716.1.
AE017225 Genomic DNA. Translation: AAT57468.1.
RefSeqiNP_847730.1. NC_003997.3.
YP_022241.1. NC_007530.2.
YP_031418.1. NC_005945.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J9RX-ray2.70A1-194[»]
ProteinModelPortaliQ81JX0.
SMRiQ81JX0. Positions 1-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ81JX0. 5 interactions.
STRINGi198094.BA_5573.

Protocols and materials databases

DNASUi1085264.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP29216; AAP29216; BA_5573.
AAT34716; AAT34716; GBAA_5573.
AAT57468; AAT57468; BAS5179.
GeneIDi1085264.
2819897.
2851937.
KEGGiban:BA_5573.
bar:GBAA_5573.
bat:BAS5179.

Phylogenomic databases

eggNOGiCOG1435.
HOGENOMiHOG000076390.
KOiK00857.
OMAiVITGPMY.
OrthoDBiEOG69D3J2.

Enzyme and pathway databases

BioCyciANTHRA:TDK-MONOMER.
BANT260799:GJAJ-5254-MONOMER.
BANT261594:GJ7F-5433-MONOMER.
MetaCyc:MONOMER-17898.

Miscellaneous databases

EvolutionaryTraceiQ81JX0.

Family and domain databases

HAMAPiMF_00124. Thymidine_kinase.
InterProiIPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
IPR020634. Thymidine_kinase_subgr.
[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. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
    Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
    , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
    Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames / isolate Porton.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestor.
  3. "Complete genome sequence of Bacillus anthracis Sterne."
    Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sterne.
  4. "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 (2.70 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND DEOXYTHYMIDINE, SUBUNIT.

Entry informationi

Entry nameiKITH_BACAN
AccessioniPrimary (citable) accession number: Q81JX0
Secondary accession number(s): Q6HQH0, Q6KJU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: June 1, 2003
Last modified: January 7, 2015
This is version 87 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.