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InterPro: IPR015636 Polynucleotide kinase 3, phosphatase

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164 proteins

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Accession

IPR015636 PNK_3Pase

Type

Family

Signatures Help

Database	ID	Name	Proteins
PANTHER	PTHR12083	PNK_3Pase	164
Signatures in BioMart

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Children

IPR006550 Polynucleotide kinase 3-phosphatase

Contains

IPR006549 HAD-superfamily hydrolase, subfamily IIIA
IPR006551 DNA 3-phosphatase

InterPro annotation

Entry Details in BioMart

Abstract

Many eukaryotes possess polynucleotide kinase phosphatase (PNKP), a bifunctional enzyme with 5'-kinase and 3'-phosphatase activities provided by two non-overlapping catalytic domains [1]. These proteins catalyse the dephosphorylation of DNA 3'-phosphates. It is believed that this activity is important for the repair of single-strand breaks in DNA caused by radiation or oxidative damage. Mammalian polynucleotide kinase phosphatase (PNKP) is a key component of both the base excision repair (BER) and nonhomologous end-joining (NHEJ) DNA repair pathways. PNKP creates 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. PNKP is recruited to repair complexes through interactions between its N-terminal FHA domain and phosphorylated components of either pathway [2].

Synonym(s): PNKP,PNK

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PDB - click here

SCOP: b.26.1.2 , c.108.1.9

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Overlapping InterPro entries Help

IPR015636

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P21286 Uncharacterized 20.8 kDa protein in FGF-VUBI intergenic region

Q03796 Polynucleotide 3'-phosphatase

Q19683 Uncharacterized protein F21D5.5

Q96T60 Bifunctional polynucleotide phosphatase/kinase

Q9JLV6 Bifunctional polynucleotide phosphatase/kinase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006551	DNA 3-phosphatase
IPR006550	Polynucleotide kinase 3-phosphatase
IPR013954	Polynucleotide kinase 3 phosphatase, central region
IPR015636	Polynucleotide kinase 3, phosphatase
IPR006549	HAD-superfamily hydrolase, subfamily IIIA
IPR008984	SMAD/FHA domain
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain

Publications Open in usermanual
1.	Deshpande RA, Wilson TE. Identification of DNA 3'-phosphatase active site residues and their differential role in DNA binding, Mg2+ coordination, and catalysis. Biochemistry 43 8579-89 2004 [PubMed: 15222769] http://dx.doi.org/10.1021/bi049434n
2.	Bernstein NK, Williams RS, Rakovszky ML, Cui D, Green R, Karimi-Busheri F, Mani RS, Galicia S, Koch CA, Cass CE, Durocher D, Weinfeld M, Glover JN. The molecular architecture of the mammalian DNA repair enzyme, polynucleotide kinase. Mol. Cell 17 657-70 2005 [PubMed: 15749016] http://dx.doi.org/10.1016/j.molcel.2005.02.012

Additional Reading Open in usermanual
	Ali AA, Jukes RM, Pearl LH, Oliver AW. Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK. Nucleic Acids Res. 37 2009 1701-12 [PubMed: 19155274] http://dx.doi.org/10.1093/nar/gkn1086

InterPro 23.1