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C3CS73 (C3CS73_BACTU) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + thymidine = ADP + thymidine 5'-phosphate. SAAS SAAS020634 RuleBase RU000544 HAMAP-Rule MF_00124

Subunit structure

Homotetramer By similarity. SAAS SAAS020634 HAMAP-Rule MF_00124

Subcellular location

Cytoplasm By similarity SAAS SAAS020634 HAMAP-Rule MF_00124.

Sequence similarities

Belongs to the thymidine kinase family. RuleBase RU004165 HAMAP-Rule MF_00124

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding15 – 228ATP By similarity HAMAP-Rule MF_00124
Nucleotide binding88 – 914ATP By similarity HAMAP-Rule MF_00124

Sites

Active site891Proton acceptor By similarity HAMAP-Rule MF_00124
Metal binding1451Zinc By similarity HAMAP-Rule MF_00124
Metal binding1481Zinc By similarity HAMAP-Rule MF_00124
Metal binding1831Zinc By similarity HAMAP-Rule MF_00124
Metal binding1861Zinc By similarity HAMAP-Rule MF_00124

Sequences

Sequence LengthMass (Da)Tools
C3CS73 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 6B421C91EF8D86F4

FASTA19521,702
        10         20         30         40         50         60 
MYLINQNGWI EVICGSMFSG KSEELIRRVR RTQFAKQHAI VFKPCIDNRY SEEDVVSHNG 

        70         80         90        100        110        120 
LKVKAVPVSA SKDIFEHITE DMDVIAIDEV QFFDGDIVEV VQVLANRGYR VIVAGLDQDF 

       130        140        150        160        170        180 
RGLPFGQVPQ LMAIAEHVTK LQAVCSACGS PASRTQRLID GEPAAFDDPI ILVGASESYE 

       190 
PRCRHCHAVP TNKDK 

« Hide

References

[1]"Genomic characterization of the Bacillus cereus sensu lato species: Backdrop to the evolution of Bacillus anthracis."
Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., Sozhamannan S., Mateczun A.J., Du L., Read T.D.
Genome Res. 22:1512-1524(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Bt407 EMBL EEM25984.1.
[2]"Complete Genome Sequence of Bacillus thuringiensis Strain 407 Cry-."
Sheppard A.E., Poehlein A., Rosenstiel P., Liesegang H., Schulenburg H.
Genome Announc. 1:E00158-12(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003889 Genomic DNA. Translation: AFV21182.1.
ACMZ01000111 Genomic DNA. Translation: EEM25984.1.
RefSeqYP_006930119.1. NC_018877.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFV21182; AFV21182; BTB_c55320.
EEM25984; EEM25984; bthur0002_52040.
GeneID13848215.
KEGGbtg:BTB_c55320.
PATRIC26099879. VBIBacThu117809_1209.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00857.

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 nameC3CS73_BACTU
AccessionPrimary (citable) accession number: C3CS73
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: July 9, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)