PNK1_SCHPO
ID PNK1_SCHPO Reviewed; 408 AA.
AC O13911;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Bifunctional polynucleotide phosphatase/kinase;
DE AltName: Full=DNA 5'-kinase/3'-phosphatase;
DE AltName: Full=Polynucleotide kinase-3'-phosphatase;
DE Includes:
DE RecName: Full=Polynucleotide 3'-phosphatase;
DE EC=3.1.3.32 {ECO:0000269|PubMed:11729194};
DE AltName: Full=2'(3')-polynucleotidase;
DE Includes:
DE RecName: Full=Polynucleotide 5'-hydroxyl-kinase;
DE EC=2.7.1.78 {ECO:0000269|PubMed:11729194};
GN Name=pnk1; ORFNames=SPAC23C11.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RX 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 damage
RT by gamma-radiation or camptothecin in Schizosaccharomyces pombe.";
RL J. Biol. Chem. 277:4050-4055(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY 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 termini
CC and can dephosphorylate its 3'-phosphate termini. Has a role in the
CC repair of breaks in single-stranded DNA. {ECO:0000269|PubMed:11729194}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'end (2'-deoxyribonucleotide 3'-phosphate)-DNA + H2O = a
CC 3'-end 2'-deoxyribonucleotide-DNA + phosphate; Xref=Rhea:RHEA:14113,
CC Rhea:RHEA-COMP:13863, Rhea:RHEA-COMP:13864, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:138147, ChEBI:CHEBI:138148;
CC EC=3.1.3.32; Evidence={ECO:0000269|PubMed:11729194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14114;
CC Evidence={ECO:0000305|PubMed:11729194};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end dephospho-2'-deoxyribonucleoside-DNA + ATP = a 5'-end
CC 5'-monophospho-2'-deoxyribonucleoside-DNA + ADP + H(+);
CC Xref=Rhea:RHEA:15669, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:13184,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:136412,
CC ChEBI:CHEBI:136416, ChEBI:CHEBI:456216; EC=2.7.1.78;
CC Evidence={ECO:0000269|PubMed:11729194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15670;
CC Evidence={ECO:0000305|PubMed:11729194};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11729194,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DNA 3'
CC phosphatase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB11157.2; -; Genomic_DNA.
DR PIR; T38242; T38242.
DR RefSeq; NP_593635.2; NM_001019066.2.
DR AlphaFoldDB; O13911; -.
DR SMR; O13911; -.
DR BioGRID; 278514; 186.
DR STRING; 4896.SPAC23C11.04c.1; -.
DR iPTMnet; O13911; -.
DR MaxQB; O13911; -.
DR PaxDb; O13911; -.
DR PRIDE; O13911; -.
DR EnsemblFungi; SPAC23C11.04c.1; SPAC23C11.04c.1:pep; SPAC23C11.04c.
DR GeneID; 2542032; -.
DR KEGG; spo:SPAC23C11.04c; -.
DR PomBase; SPAC23C11.04c; pnk1.
DR VEuPathDB; FungiDB:SPAC23C11.04c; -.
DR eggNOG; KOG2134; Eukaryota.
DR HOGENOM; CLU_014938_3_1_1; -.
DR InParanoid; O13911; -.
DR OMA; KTREKCV; -.
DR BRENDA; 3.1.3.32; 5613.
DR PRO; PR:O13911; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0046404; F:polydeoxyribonucleotide 5'-hydroxyl-kinase activity; IDA:PomBase.
DR GO; GO:0046403; F:polynucleotide 3'-phosphatase activity; IDA:PomBase.
DR GO; GO:0006284; P:base-excision repair; IMP:PomBase.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0046939; P:nucleotide phosphorylation; IBA:GO_Central.
DR GO; GO:0000012; P:single strand break repair; IDA:PomBase.
DR Gene3D; 3.40.50.1000; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013954; PNK3P.
DR InterPro; IPR006551; Polynucleotide_phosphatase.
DR Pfam; PF08645; PNK3P; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01664; DNA-3'-Pase; 1.
DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; Hydrolase; Kinase;
KW Multifunctional enzyme; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..408
FT /note="Bifunctional polynucleotide phosphatase/kinase"
FT /id="PRO_0000058477"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 408 AA; 47089 MW; F4305563D5872634 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 VIDNTNPTIE SRKMWIDIAQ EFEIPIRCIH LQSSEELARH NNVFRYIHHN
QKQLPEIAFN SFKSRFQMPT VEEGFTNVEE VPFKCLKDYE DTWNYWYE
