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P06855 (KIPN_BPT4) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. 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:
Polynucleotide kinase

Short name=PNK
EC=2.7.1.78
Alternative name(s):
Polynucleotide 5'-hydroxyl-kinase
Gene names
Name:pseT
OrganismEnterobacteria phage T4 (Bacteriophage T4) [Reference proteome]
Taxonomic identifier10665 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length301 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a 5'-hydroxyl kinase, a 3'-phosphatase and a 2',3'-cyclic phosphodiesterase. Catalyzes the transfer of the terminal phosphate of ATP to the 5'-hydroxyl termini of ribo- and deoxyribonucleotides. In the presence of ADP the enzyme also catalyzes an exchange reaction. In the exchange reaction, an excess ADP causes the enzyme to transfer the 5' terminal phosphate from phosphorylated DNA to ADP. These activities modify the ends of nicked tRNA generated by a bacterial response to infection and facilitate repair by T4 RNA ligase.

Catalytic activity

ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA.

Subunit structure

Homotetramer.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 301301Polynucleotide kinase
PRO_0000164949

Secondary structure

...................................................... 301
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06855 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 0EAFB6BA83236D31

FASTA30134,620
        10         20         30         40         50         60 
MKKIILTIGC PGSGKSTWAR EFIAKNPGFY NINRDDYRQS IMAHEERDEY KYTKKKEGIV 

        70         80         90        100        110        120 
TGMQFDTAKS ILYGGDSVKG VIISDTNLNP ERRLAWETFA KEYGWKVEHK VFDVPWTELV 

       130        140        150        160        170        180 
KRNSKRGTKA VPIDVLRSMY KSMREYLGLP VYNGTPGKPK AVIFDVDGTL AKMNGRGPYD 

       190        200        210        220        230        240 
LEKCDTDVIN PMVVELSKMY ALMGYQIVVV SGRESGTKED PTKYYRMTRK WVEDIAGVPL 

       250        260        270        280        290        300 
VMQCQREQGD TRKDDVVKEE IFWKHIAPHF DVKLAIDDRT QVVEMWRRIG VECWQVASGD 


F 

« Hide

References

« Hide 'large scale' references
[1]"T4 polynucleotide kinase; cloning of the gene (pseT) and amplification of its product."
Midgley C.A., Murray N.E.
EMBO J. 4:2695-2703(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Bacteriophage T4 genome."
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.
Microbiol. Mol. Biol. Rev. 67:86-156(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Structure of a tRNA repair enzyme and molecular biology workhorse: T4 polynucleotide kinase."
Galburt E.A., Pelletier J., Wilson G., Stoddard B.L.
Structure 10:1249-1260(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03007 Genomic DNA. Translation: CAA26792.1.
AF158101 Genomic DNA. Translation: AAD42642.1.
PIRKIBPP4. A24642.
RefSeqNP_049834.1. NC_000866.4.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LTQX-ray2.33A1-301[»]
1LY1X-ray2.00A1-181[»]
1RC8X-ray2.75A1-301[»]
1RPZX-ray2.90A1-301[»]
1RRCX-ray2.46A1-301[»]
2IA5X-ray2.90A/B/C/D/E/F/G/H/I/J/K/L1-301[»]
ProteinModelPortalP06855.
SMRP06855. Positions 1-300.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP06855.
ChEMBLCHEMBL5292.
DrugBankDB01093. Dimethyl sulfoxide.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1258796.

Phylogenomic databases

ProtClustDBPHA2530.

Enzyme and pathway databases

SABIO-RKP06855.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
3.40.50.300. 1 hit.
InterProIPR023214. HAD-like_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF56784. SSF56784. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP06855.

Entry information

Entry nameKIPN_BPT4
AccessionPrimary (citable) accession number: P06855
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references