O13911 (PNK1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional polynucleotide phosphatase/kinase

Alternative name(s):
DNA 5'-kinase/3'-phosphatase
Polynucleotide kinase-3'-phosphatase

Including the following 2 domains:

1. Polynucleotide 3'-phosphatase
   EC=3.1.3.32
   Alternative name(s):
   2'(3')-polynucleotidase
2. Polynucleotide 5'-hydroxyl-kinase
   EC=2.7.1.78

Gene names

Name:	pnk1
ORF Names:	SPAC23C11.04c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the phosphorylation of DNA at 5'-hydroxyl termini and can dephosphorylate its 3'-phosphate termini. Has a role in the repair of breaks in single stranded DNA. Ref.1
Catalytic activity	A 3'-phosphopolynucleotide + H2O = a polynucleotide + phosphate. ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA.
Subcellular location	Nucleus Ref.1.
Sequence similarities	In the N-terminal section; belongs to the DNA 3' phosphatase family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	nucleotide-excision repair, DNA damage removal Inferred from direct assay. Source: GeneDB_Spombe
Cellular component	nucleolus Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity Inferred from direct assay. Source: GeneDB_Spombe polynucleotide 3'-phosphatase activity Inferred from direct assay. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 421	421	Bifunctional polynucleotide phosphatase/kinase		PRO_0000058477
Regions
	Nucleotide binding	263 – 270	8	ATP Potential
Amino acid modifications
	Modified residue	8	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O13911 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: FE9A732CD40E3146	FASTA	421	48,477
	10 20 30 40 50 60 MSSKKRKSPP QESLTSYFEK SSKSSKKYGS QNKDSDSSST CLQQKIEIQW SITDSLYIAK 70 80 90 100 110 120 YGKLKKTKKF IAFDLDGTLI KTKSGRVFSK DAADWTWWHP SVVPKLKALY QDNYSLVIFS 130 140 150 160 170 180 NQNGIPRKPS AGHTFQMKIR AIFESLDLPI VLYAAILKDK FRKPLTGMWN SFLKDVNRSI 190 200 210 220 230 240 DLSFIKYVGD AAGRPGDHNS TDLKFAENIG IKFETPEQFF LGHSFVPPNF ESFHPKNYLV 250 260 270 280 290 300 RNSSSHPYHF KKSEHQEIVV LVGFPSSGKS TLAESQIVTQ GYERVNQDIL KTKSKCIKAA 310 320 330 340 350 360 IEALKKEKSV VIGMYSIIST TYAISDNTNP TIESRKMWID IAQEFEIPIR CIHLQSSEEL 370 380 390 400 410 420 ARHNNVFRYI HHNQKQLPEI AFNSFKSRFQ MPTVEEGFTN VEEVPFKCLK DYEDTWNYWY E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Pnk1, a DNA kinase/phosphatase required for normal response to DNA damage by gamma-radiation or camptothecin in Schizosaccharomyces pombe." Meijer M., Karimi-Busheri F., Huang T.Y., Weinfeld M., Young D. J. Biol. Chem. 277:4050-4055(2002) [PubMed: 11729194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB11157.1.
PIR	T38242.
RefSeq	NP_593635.1. NM_001019066.1.
3D structure databases
ProteinModelPortal	O13911.
ModBase	Search...
Protein-protein interaction databases
STRING	O13911.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2542032.
GenomeReviews	Gene locus pnk1 in contig CU329670_GR.
KEGG	spo:SPAC23C11.04c.
NMPDR	fig|4896.1.peg.3605.
Organism-specific databases
GeneDB_Spombe	SPAC23C11.04c.
Phylogenomic databases
eggNOG	fuNOG08837.
GeneTree	EFGT00050000006787.
HOGENOM	HBG329365.
OMA	RVAIDNT.
OrthoDB	EOG47M57H.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001304-MONOMER.
Gene expression databases
ArrayExpress	O13911.
Family and domain databases
InterPro	IPR023214. HAD-like_dom. IPR006549. HAD-SF_hydro_IIIA. IPR013954. PNK3P. IPR015636. PNK_3Pase_euk. IPR006551. Polynucleotide_phosphatase. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
KO	K08073.
PANTHER	PTHR12083. PNK_3Pase. 1 hit.
Pfam	PF08645. PNK3P. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01664. DNA-3'-Pase. 1 hit. TIGR01662. HAD-SF-IIIA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PNK1_SCHPO

Accession

Primary (citable) accession number: O13911

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program