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DNA replication ATP-dependent helicase/nuclease dna2 [Includes: DNA replication nuclease dna2 (EC 3.1.-.-); DNA replication ATP-dependent helicase dna2 (EC 3.6.4.12)]

 DNA2_SCHPO              Reviewed;        1397 AA.
Q9URU2; O74241; Q9UTT6; Q9UUK8;
14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
25-OCT-2017, entry version 128.
RecName: Full=DNA replication ATP-dependent helicase/nuclease dna2;
Includes:
RecName: Full=DNA replication nuclease dna2;
EC=3.1.-.-;
Includes:
RecName: Full=DNA replication ATP-dependent helicase dna2;
EC=3.6.4.12;
Name=dna2; ORFNames=SPBC16D10.04c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
PubMed=10880469;
Kang H.-Y., Choi E., Bae S.-H., Lee K.-H., Gim B.-S., Kim H.-D.,
Park C., MacNeill S.A., Seo Y.-S.;
"Genetic analyses of Schizosaccharomyces pombe dna2+ reveal that dna2
plays an essential role in Okazaki fragment metabolism.";
Genetics 155:1055-1067(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
REVISION OF GENE MODEL.
PubMed=21511999; DOI=10.1126/science.1203357;
Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K.,
Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.,
Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L.,
FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D.,
Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M.,
Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M.,
Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D.,
Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H.,
Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
"Comparative functional genomics of the fission yeasts.";
Science 332:930-936(2011).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 120-140, AND
SUBCELLULAR LOCATION.
STRAIN=ATCC 38364 / 968;
PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
Hiraoka Y.;
"Large-scale screening of intracellular protein localization in living
fission yeast cells by the use of a GFP-fusion genomic DNA library.";
Genes Cells 5:169-190(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1053-1243.
STRAIN=972 / ATCC 24843;
PubMed=9649516;
Gould K.L., Burns C.G., Feoktistova A., Hu C.-P., Pasion S.G.,
Forsburg S.L.;
"Fission yeast cdc24(+) encodes a novel replication factor required
for chromosome integrity.";
Genetics 149:1221-1233(1998).
[6]
FUNCTION.
PubMed=15302919; DOI=10.1093/nar/gkh720;
Ryu G.H., Tanaka H., Kim D.H., Kim J.H., Bae S.H., Kwon Y.N.,
Rhee J.S., MacNeill S.A., Seo Y.S.;
"Genetic and biochemical analyses of Pfh1 DNA helicase function in
fission yeast.";
Nucleic Acids Res. 32:4205-4216(2004).
[7]
FUNCTION, AND TELOMERE-BINDING.
PubMed=15485922; DOI=10.1128/MCB.24.21.9557-9567.2004;
Tomita K., Kibe T., Kang H.Y., Seo Y.S., Uritani M., Ushimaru T.,
Ueno M.;
"Fission yeast Dna2 is required for generation of the telomeric
single-strand overhang.";
Mol. Cell. Biol. 24:9557-9567(2004).
[8]
FUNCTION, AND INTERACTION WITH CDC24.
PubMed=15576681; DOI=10.1093/nar/gkh963;
Tanaka H., Ryu G.H., Seo Y.S., MacNeill S.A.;
"Genetics of lagging strand DNA synthesis and maturation in fission
yeast: suppression analysis links the Dna2-Cdc24 complex to DNA
polymerase delta.";
Nucleic Acids Res. 32:6367-6377(2004).
[9]
FUNCTION.
PubMed=15915339; DOI=10.1007/s00294-005-0584-2;
Tsutsui Y., Morishita T., Natsume T., Yamashita K., Iwasaki H.,
Yamao F., Shinagawa H.;
"Genetic and physical interactions between Schizosaccharomyces pombe
Mcl1 and Rad2, Dna2 and DNA polymerase alpha: evidence for a
multifunctional role of Mcl1 in DNA replication and repair.";
Curr. Genet. 48:34-43(2005).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823372; DOI=10.1038/nbt1222;
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the
fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
[11]
FUNCTION, PHOSPHORYLATION AT SER-134 AND SER-219, AND MUTAGENESIS OF
SER-219; GLU-559 AND LYS-960.
PubMed=22682245; DOI=10.1016/j.cell.2012.04.030;
Hu J., Sun L., Shen F., Chen Y., Hua Y., Liu Y., Zhang M., Hu Y.,
Wang Q., Xu W., Sun F., Ji J., Murray J.M., Carr A.M., Kong D.;
"The intra-s phase checkpoint targets dna2 to prevent stalled
replication forks from reversing.";
Cell 149:1221-1232(2012).
-!- FUNCTION: Key enzyme involved in DNA replication and DNA repair.
Involved in Okazaki fragments processing by cleaving long flaps
that escape fen1: flaps that are longer than 27 nucleotides are
coated by replication protein A complex (RPA), leading to recruit
dna2 which cleaves the flap until it is too short to bind RPA and
becomes a substrate for fen1. Is a target of the intra-S phase
checkpoint, associating with stalled replication forks when
phosphorylated at Ser-219 and preventing the stalled replication
forks from reversing. Also involved in 5'-end resection of DNA
during double-strand break (DSB) repair by mediating the cleavage
of 5'-ssDNA. Also required for the production of G-rich single-
strand overhangs at telomere ends and thus in telomere length
maintenance. Possesses different enzymatic activities, such as
single-stranded DNA (ssDNA)-dependent ATPase, 5'-3' helicase and
endonuclease activities. While the ATPase and endonuclease
activities are well-defined and play a key role in Okazaki
fragments processing and DSB repair, the 5'-3' DNA helicase
activity is atypical: it cannot load onto its tracking strand
internally and has an absolute free 5'-end requirement. Helicase
activity may promote the motion of dna2 on the flap, helping the
nuclease function. {ECO:0000269|PubMed:15302919,
ECO:0000269|PubMed:15485922, ECO:0000269|PubMed:15576681,
ECO:0000269|PubMed:15915339, ECO:0000269|PubMed:22682245}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000250};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
-!- SUBUNIT: Interacts with cdc1, cdc24 and rad2.
{ECO:0000269|PubMed:15576681}.
-!- INTERACTION:
O75004:cdc24; NbExp=3; IntAct=EBI-16120355, EBI-1559355;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, telomere.
Note=Recruited to double-strand. break (DSB) sites.
-!- PTM: Phosphorylated at Ser-219 by cds1/check2, leading to
association with stalled replication forks.
{ECO:0000269|PubMed:22682245}.
-!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF144384; AAD38528.1; -; Genomic_DNA.
EMBL; CU329671; CAB38508.2; -; Genomic_DNA.
EMBL; AB028014; BAA87318.1; -; Genomic_DNA.
EMBL; AF075169; AAC39502.1; -; Genomic_DNA.
PIR; T39568; T39568.
PIR; T47242; T47242.
PIR; T51292; T51292.
RefSeq; NP_596499.2; NM_001022420.2.
BioGrid; 276685; 17.
DIP; DIP-61017N; -.
IntAct; Q9URU2; 3.
MINT; MINT-4707004; -.
STRING; 4896.SPBC16D10.04c.1; -.
iPTMnet; Q9URU2; -.
MaxQB; Q9URU2; -.
PRIDE; Q9URU2; -.
EnsemblFungi; SPBC16D10.04c.1; SPBC16D10.04c.1:pep; SPBC16D10.04c.
GeneID; 2540148; -.
KEGG; spo:SPBC16D10.04c; -.
EuPathDB; FungiDB:SPBC16D10.04c; -.
PomBase; SPBC16D10.04c; dna2.
InParanoid; Q9URU2; -.
KO; K10742; -.
OMA; DIEENLW; -.
OrthoDB; EOG092C07AQ; -.
Reactome; R-SPO-174437; Removal of the Flap Intermediate from the C-strand.
Reactome; R-SPO-69166; Removal of the Flap Intermediate.
PRO; PR:Q9URU2; -.
Proteomes; UP000002485; Chromosome II.
GO; GO:0005737; C:cytoplasm; IDA:PomBase.
GO; GO:0005829; C:cytosol; IDA:PomBase.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:PomBase.
GO; GO:0043596; C:nuclear replication fork; IDA:PomBase.
GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
GO; GO:0005634; C:nucleus; IDA:PomBase.
GO; GO:0005657; C:replication fork; IDA:UniProtKB.
GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:1990601; F:5' overhang single-stranded DNA endodeoxyribonuclease activity; IDA:PomBase.
GO; GO:0017108; F:5'-flap endonuclease activity; ISO:PomBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; ISO:PomBase.
GO; GO:0003682; F:chromatin binding; IDA:PomBase.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004518; F:nuclease activity; IMP:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; IDA:PomBase.
GO; GO:0043142; F:single-stranded DNA-dependent ATPase activity; IEA:InterPro.
GO; GO:0006281; P:DNA repair; ISS:PomBase.
GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IMP:PomBase.
GO; GO:1903469; P:removal of RNA primer involved in mitotic DNA replication; IC:PomBase.
GO; GO:0031297; P:replication fork processing; IMP:PomBase.
GO; GO:0071932; P:replication fork reversal; IMP:UniProtKB.
GO; GO:0072429; P:response to intra-S DNA damage checkpoint signaling; IMP:UniProtKB.
GO; GO:0031860; P:telomeric 3' overhang formation; IGI:PomBase.
InterPro; IPR026851; Dna2.
InterPro; IPR022765; Dna2/Cas4_DUF83.
InterPro; IPR014808; DNA_replication_fac_Dna2_N.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR10887:SF14; PTHR10887:SF14; 1.
Pfam; PF01930; Cas_Cas4; 1.
Pfam; PF08696; Dna2; 1.
SUPFAM; SSF52540; SSF52540; 2.
1: Evidence at protein level;
4Fe-4S; ATP-binding; Chromosome; Complete proteome; Cytoplasm;
DNA damage; DNA repair; DNA replication; DNA-binding; Endonuclease;
Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding;
Multifunctional enzyme; Nuclease; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Telomere.
CHAIN 1 1397 DNA replication ATP-dependent
helicase/nuclease dna2.
/FTId=PRO_0000080710.
NP_BIND 954 961 ATP. {ECO:0000250}.
REGION 390 808 Nuclease activity. {ECO:0000250}.
REGION 809 1397 Helicase activity. {ECO:0000250}.
METAL 450 450 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 679 679 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 682 682 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 688 688 Iron-sulfur (4Fe-4S). {ECO:0000250}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000269|PubMed:22682245}.
MOD_RES 219 219 Phosphoserine; by CHEK2.
{ECO:0000269|PubMed:22682245}.
MUTAGEN 219 219 S->A: Impaired phosphorylation by
cds1/check2, leading to stalled fork
reversing. {ECO:0000269|PubMed:22682245}.
MUTAGEN 219 219 S->D: Mimics phosphorylation; not able to
rescue hydroxyurea-sensitivity in cds1
mutant cells.
{ECO:0000269|PubMed:22682245}.
MUTAGEN 559 559 E->A: Not able to complement a dna2(ts)
mutant at restrictive temperature of 36
degrees Celsius.
{ECO:0000269|PubMed:22682245}.
MUTAGEN 960 960 K->T: Able to complement a dna2(ts)
mutant at restrictive temperature of 36
degrees Celsius.
{ECO:0000269|PubMed:22682245}.
SEQUENCE 1397 AA; 157659 MW; 5BE34210382E4B8C CRC64;
MFNDQSKTTS SVKGICATTD NNHGNLKKTN STPFRKNYLL NGRTKLKLEN FAYNASTEIS
SPKISEKKHS SLPIKRKNTF NESSTSFSPF TKAHKEITDD LKPDKSFTRK SDLNSQDMPV
CFQETSKDLC RSSSTQHLLD HQTTDSTIID MKPVSTNSKS DVFTLYTDET VLLRRCASDN
KPLINNNLSS SNVSENQSRS FGSYDEVKNQ GNNLHKVPSL VSIIRNARSS EQSRIAANSS
CLLKGSDTEI DEDDFALEAE DLAALDSLER QYSQLPNSTV TASAKDIEKT AKVNHVGGDL
QSYCSATKAS DATINEEPVN LALDKACNSL PDINSDFIDD WDDSCDGCTP GELCEFSSEY
TVLEVHEDFI FHEGNHFRQL KLILEANDIL HQLFLRGDWT ETSIFVGDSI RVEATFDKDN
TAIVDNDKGL IIIHPKILMS ATAVASSFPC LRKAVISDRV GIYGPPTKAM VTGNILHDFF
QHALYRGIDA LENVDINLET SIKTYISDIY FADLSLDEIR EELDARLPLL KSIVERYLIS
KKNDNNNESI HISRLLDIEE SIWSPRFGLK GNIDATVEVV LTEKPESSST LTLPLELKTG
RYVDNISHFA QSLLYTLLIS DRYGINTNQA LLCYLENSTI KNLVASNSQL RGLIMTRNSL
AQHNFRRSLP EMISNRKICD HCSLVSECLF FQKMSDKGVA NSNGLTESWN EWMREVKDED
LEFYKKWEKL LNQEERLLLL KRGDVLTFDT EELEAYGKTL YPLYITKEDI VCLEIDDRVF
HYKFAFLNDN GYPRNFLHSG FSVGERVFIS DEHGHWSLAK GHIVHIQDSC IEVRTRHRLH
IPWLKMPNFD FKKNQVFFGN YEDSKLSFIG SNHTRYRIDK DEFSSGIASI RGTLMSSVLP
DAPLIIRDMI IRLKPPKFCN SALIDPEFLK CLNEDQITAL KKCHAAEHYS LILGMPGTGK
TTTISSLIRS LLAKKKKILL TSFTHLAVDN ILIKLKGCDS TIVRLGSPHK IHPLVKEFCL
TEGTTFDDLA SLKHFYEDPQ IVACSSLGVY HSIFNKRKFD YCIIDEASQI PLPICLGPLQ
LAEKFVLVGD HYQLPPLVKN SRTSKDGLSL SLFKLLSEKH PEAVTTLRLQ YRMNEDINSL
SSELIYGGNL VCGSKTISQK KLILPKAHLS DGLPDSSSSL HWVNKLINPS HSVIFFNTDD
ILGVESKTNN ILENHTEAFL IEQAVSSFLE RGVKQSSIGI ISIYKSQVEL LSKNLKSFTE
IEINTVDRYQ GRDKDIILIS FVRSNSKNLV GELLRDWHRL NVALSRAKVK CIMFGSLSTL
SSSNIVSHLL KLLEKNKWIF TLNENDIATK FDENSSPIKD CSQVATTNNA KVIIRKNQRF
FNSDNLCEKA ILPQLEF


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