ID PNK1_SCHPO Reviewed; 421 AA. AC O13911; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JUN-2009, entry version 58. DE RecName: Full=Bifunctional polynucleotide phosphatase/kinase; DE AltName: Full=Polynucleotide kinase-3'-phosphatase; DE AltName: Full=DNA 5'-kinase/3'-phosphatase; DE Includes: DE RecName: Full=Polynucleotide 3'-phosphatase; DE EC=3.1.3.32; DE AltName: Full=2'(3')-polynucleotidase; DE Includes: DE RecName: Full=Polynucleotide 5'-hydroxyl-kinase; DE EC=2.7.1.78; GN Name=pnk1; ORFNames=SPAC23C11.04c; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=21683566; PubMed=11729194; DOI=10.1074/jbc.M109383200; RA Meijer M., Karimi-Busheri F., Huang T.Y., Weinfeld M., Young D.; RT "Pnk1, a DNA kinase/phosphatase required for normal response to DNA RT damage by gamma-radiation or camptothecin in Schizosaccharomyces RT pombe."; RL J. Biol. Chem. 277:4050-4055(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND MASS RP SPECTROMETRY. RX PubMed=18257517; DOI=10.1021/pr7006335; RA Wilson-Grady J.T., Villen J., Gygi S.P.; RT "Phosphoproteome analysis of fission yeast."; RL J. Proteome Res. 7:1088-1097(2008). CC -!- FUNCTION: Catalyzes the phosphorylation of DNA at 5'-hydroxyl CC termini and can dephosphorylate its 3'-phosphate termini. Has a CC role in the repair of breaks in single stranded DNA. CC -!- CATALYTIC ACTIVITY: A 3'-phosphopolynucleotide + H(2)O = a CC polynucleotide + phosphate. CC -!- CATALYTIC ACTIVITY: ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: In the N-terminal section; belongs to the DNA 3' CC phosphatase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU329670; CAB11157.1; -; Genomic_DNA. DR PIR; T38242; T38242. DR RefSeq; NP_593635.1; -. DR GeneID; 2542032; -. DR KEGG; spo:SPAC23C11.04c; -. DR NMPDR; fig|4896.1.peg.3605; -. DR GeneDB_Spombe; SPAC23C11.04c; -. DR OMA; O13911; SWQRCVT. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-001304-MON; -. DR BRENDA; 2.7.1.78; 653. DR BRENDA; 3.1.3.32; 653. DR ArrayExpress; O13911; -. DR GO; GO:0005730; C:nucleolus; IDA:GeneDB_SPombe. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046404; F:ATP-dependent polydeoxyribonucleotide 5'-hy...; IDA:GeneDB_SPombe. DR GO; GO:0046403; F:polynucleotide 3'-phosphatase activity; IDA:GeneDB_SPombe. DR GO; GO:0000718; P:nucleotide-excision repair, DNA damage removal; IDA:GeneDB_SPombe. DR InterPro; IPR006551; DNA-3-Pase. DR InterPro; IPR006549; HAD-SF_hydro_IIIA. DR InterPro; IPR013954; PNK3P_central-region. DR InterPro; IPR015636; PNK_3Pase. DR PANTHER; PTHR12083; PNK_3Pase; 1. DR Pfam; PF08645; PNK3P; 1. DR TIGRFAMs; TIGR01664; DNA-3_-Pase; 1. DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; DNA damage; DNA repair; Hydrolase; KW Kinase; Multifunctional enzyme; Nucleotide-binding; Nucleus; KW Phosphoprotein; Transferase. FT CHAIN 1 421 Bifunctional polynucleotide FT phosphatase/kinase. FT /FTId=PRO_0000058477. FT NP_BIND 263 270 ATP (Potential). FT MOD_RES 8 8 Phosphoserine. SQ SEQUENCE 421 AA; 48477 MW; FE9A732CD40E3146 CRC64; MSSKKRKSPP QESLTSYFEK SSKSSKKYGS QNKDSDSSST CLQQKIEIQW SITDSLYIAK YGKLKKTKKF IAFDLDGTLI KTKSGRVFSK DAADWTWWHP SVVPKLKALY QDNYSLVIFS NQNGIPRKPS AGHTFQMKIR AIFESLDLPI VLYAAILKDK FRKPLTGMWN SFLKDVNRSI DLSFIKYVGD AAGRPGDHNS TDLKFAENIG IKFETPEQFF LGHSFVPPNF ESFHPKNYLV RNSSSHPYHF KKSEHQEIVV LVGFPSSGKS TLAESQIVTQ GYERVNQDIL KTKSKCIKAA IEALKKEKSV VIGMYSIIST TYAISDNTNP TIESRKMWID IAQEFEIPIR CIHLQSSEEL ARHNNVFRYI HHNQKQLPEI AFNSFKSRFQ MPTVEEGFTN VEEVPFKCLK DYEDTWNYWY E //