P06855 (KIPN_BPT4) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polynucleotide kinase
Short name=PNK
EC=2.7.1.78

Alternative name(s):
Polynucleotide 5'-hydroxyl-kinase

Gene names

Name:

pseT

Organism

Enterobacteria phage T4 (Bacteriophage T4) [Reference proteome]

Taxonomic identifier

10665 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › Tevenvirinae › T4likevirus › Enterobacteria phage T4 sensu lato

Virus host

Escherichia coli [TaxID: 562]

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	DNA damage DNA repair
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 301

301

Polynucleotide kinase

PRO_0000164949

Secondary structure

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301

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

15 – 25

11

Beta strand

29 – 32

4

Helix

34 – 41

8

Helix

47 – 49

3

Helix

54 – 72

19

Helix

75 – 77

3

Beta strand

80 – 83

4

Helix

90 – 103

14

Beta strand

106 – 111

6

Helix

116 – 123

8

Helix

127 – 129

3

Helix

133 – 147

15

Beta strand

156 – 158

3

Beta strand

160 – 165

6

Turn

168 – 170

3

Helix

181 – 186

6

Helix

191 – 202

12

Beta strand

206 – 211

6

Beta strand

218 – 220

3

Helix

223 – 234

12

Beta strand

241 – 245

5

Helix

254 – 265

12

Turn

266 – 269

4

Beta strand

271 – 277

7

Helix

280 – 288

9

Beta strand

293 – 295

3

Sequences

	Sequence		Length	Mass (Da)
	P06855 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 0EAFB6BA83236D31	FASTA	301	34,620
	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

References

	« Hide 'large scale' referencesShow '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.

PIR

KIBPP4. A24642.

RefSeq

NP_049834.1. NC_000866.4.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LTQ	X-ray	2.33	A	1-301	[»]
1LY1	X-ray	2.00	A	1-181	[»]
1RC8	X-ray	2.75	A	1-301	[»]
1RPZ	X-ray	2.90	A	1-301	[»]
1RRC	X-ray	2.46	A	1-301	[»]
2IA5	X-ray	2.90	A/B/C/D/E/F/G/H/I/J/K/L	1-301	[»]

ProteinModelPortal

P06855.

SMR

P06855. Positions 1-300.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1258796.

Phylogenomic databases

ProtClustDB

PHA2530.

Enzyme and pathway databases

SABIO-RK

P06855.

Family and domain databases

Gene3D

3.40.50.1000. 1 hit.

InterPro

IPR023214. HAD-like_dom.
[Graphical view]

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

ProtoNet

Search...

Other

BindingDB

P06855.

ChEMBL

CHEMBL5292.

DrugBank

DB01093. Dimethyl sulfoxide.

EvolutionaryTrace

P06855.

Entry information

Entry name

KIPN_BPT4

Accession

Primary (citable) accession number: P06855

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program