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Protein

Thymidine kinase

Gene

tdk

Organism
Erysipelothrix rhusiopathiae (strain Fujisawa)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei90 – 901Proton acceptorUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 238ATPUniRule annotation
Nucleotide bindingi89 – 924ATPUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

KinaseUniRule annotation, Transferase

Keywords - Biological processi

DNA synthesisUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciERHU650150:GHGV-1689-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidine kinaseUniRule annotation (EC:2.7.1.21UniRule annotation)
Gene namesi
Name:tdkUniRule annotationImported
Ordered Locus Names:ERH_1613Imported
OrganismiErysipelothrix rhusiopathiae (strain Fujisawa)Imported
Taxonomic identifieri650150 [NCBI]
Taxonomic lineageiBacteriaFirmicutesErysipelotrichiaErysipelotrichalesErysipelotrichaceaeErysipelothrix
ProteomesiUP000007944 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliF5WV83.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thymidine kinase family.UniRule annotation

Phylogenomic databases

KOiK00857.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

F5WV83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMYHQYQEGY IEVITGCMFA GKTEELIRRI NVLKFAHKNI IVFKPAVDNR
60 70 80 90 100
YSDSKVVSHA GTSVQSVVVD KATDILKYVT KETDVVAIDE VQFFDEEIVK
110 120 130 140 150
VCDHLALEGK RVMVAGLDMD FRGEPFGVIP KLMTTAEFVT KLTAVCTECG
160 170 180 190 200
APATRTQRLV NGKPASYHDP VVMIGASESY EARCRHDHIV LDKPQINGNS

EGDK
Length:204
Mass (Da):22,728
Last modified:July 27, 2011 - v1
Checksum:i2641D86303AFE8A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP012027 Genomic DNA. Translation: BAK32665.1.
RefSeqiWP_003774317.1. NC_015601.1.
YP_004561706.1. NC_015601.1.

Genome annotation databases

EnsemblBacteriaiBAK32665; BAK32665; ERH_1613.
KEGGierh:ERH_1613.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP012027 Genomic DNA. Translation: BAK32665.1.
RefSeqiWP_003774317.1. NC_015601.1.
YP_004561706.1. NC_015601.1.

3D structure databases

ProteinModelPortaliF5WV83.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAK32665; BAK32665; ERH_1613.
KEGGierh:ERH_1613.

Phylogenomic databases

KOiK00857.

Enzyme and pathway databases

BioCyciERHU650150:GHGV-1689-MONOMER.

Family and domain databases

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

Publicationsi

  1. "The genome of Erysipelothrix rhusiopathiae, the causative agent of swine erysipelas, reveals new insights into the evolution of firmicutes and the organism's intracellular adaptations."
    Ogawa Y., Ooka T., Shi F., Ogura Y., Nakayama K., Hayashi T., Shimoji Y.
    J. Bacteriol. 193:2959-2971(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FujisawaImported.

Entry informationi

Entry nameiF5WV83_ERYRF
AccessioniPrimary (citable) accession number: F5WV83
Entry historyi
Integrated into UniProtKB/TrEMBL: July 27, 2011
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.