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Reviewed, UniProtKB/Swiss-Prot O13911 (PNK1_SCHPO)

Last modified February 9, 2010. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional polynucleotide phosphatase/kinase
Alternative name(s):
    Polynucleotide kinase-3'-phosphatase
    DNA 5'-kinase/3'-phosphatase
Including the following 2 domains:
    1- Recommended name:
            Polynucleotide 3'-phosphatase
              EC=3.1.3.32
        Alternative name(s):
            2'(3')-polynucleotidase
    2- Recommended name:
            Polynucleotide 5'-hydroxyl-kinase
              EC=2.7.1.78
Gene names
Name: pnk1
ORF Names: SPAC23C11.04c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processDNA damage
DNA repair
   Cellular componentNucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological processnucleotide-excision repair, DNA damage removal

Inferred from direct assay. Source: GeneDB_SPombe

   Cellular componentnucleolus

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity Ref.1

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Bifunctional polynucleotide phosphatase/kinase
PRO_0000058477

Regions

Nucleotide binding263 – 2708ATP Potential

Amino acid modifications

Modified residue81Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
O13911-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: FE9A732CD40E3146

FASTA42148,477
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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: ATCC 38366 / 972.
[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.
PIRT38242.
RefSeqNP_593635.1.

3D structure databases

SMRO13911. Positions 48-416.
ModBaseSearch...

Genome annotation databases

GeneID2542032.
GenomeReviewsGene locus pnk1 in contig CU329670_GR.
KEGGspo:SPAC23C11.04c.
NMPDRfig|4896.1.peg.3605.

Organism-specific databases

GeneDB_SpombeSPAC23C11.04c.

Phylogenomic databases

eggNOGfuNOG08837.
HOGENOMHBG329365.
OMASWQRCVT.
OrthoDBEOG9615MT.
PhylomeDBO13911.

Enzyme and pathway databases

BRENDA2.7.1.78. 653.
3.1.3.32. 653.

Gene expression databases

ArrayExpressO13911.

Family and domain databases

InterProIPR006551. DNA-3-Pase.
IPR006549. HAD-SF_hydro_IIIA.
IPR015636. PNK_3Pase.
[Graphical view]
PANTHERPTHR12083. PNK_3Pase. 1 hit.
TIGRFAMsTIGR01664. DNA-3_-Pase. 1 hit.
TIGR01662. HAD-SF-IIIA. 1 hit.
ProtoNetSearch...

Entry information

Entry namePNK1_SCHPO
AccessionPrimary (citable) accession number: O13911
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: February 9, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents