Tag |
Content |
dbPAF ID |
dbPAF-0040800 |
Uniprot Accession |
Q9URU2; DNA2_SCHPO; O74241; Q9UTT6; Q9UUK8; |
Genbank Protein ID |
NP_596499.2; |
Genbank Nucleotide ID |
NM_001022420.2; |
Protein Name |
DNA replication ATP-dependent helicase/nuclease dna2 |
Protein Synonyms/Alias |
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Gene Name |
dna2 |
Gene Synonyms/Alias |
SPBC16D10.04c; |
Organism |
Schizosaccharomyces pombe (strain 972 / ATCC 24843)(Fission yeast) |
NCBI Taxa ID |
284812 |
Functional Description (View all) |
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.Functional Description
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.
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Phosphorylation Sites
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dbPAF PTMs: 2 Position | Peptides | Source | References ( PMIDs ) |
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134 | KDLCRSSSTQHLLDH | UniProt | 22682245 | 200 | VSENQSRSFGSYDEV | curated | 22817900 |
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Sequence (Fasta) | MFNDQSKTTS SVKGICATTD NNHGNLKKTN STPFRKNYLL NGRTKLKLEN FAYNASTEIS 60 SPKISEKKHS SLPIKRKNTF NESSTSFSPF TKAHKEITDD LKPDKSFTRK SDLNSQDMPV 120 CFQETSKDLC RSSSTQHLLD HQTTDSTIID MKPVSTNSKS DVFTLYTDET VLLRRCASDN 180 KPLINNNLSS SNVSENQSRS FGSYDEVKNQ GNNLHKVPSL VSIIRNARSS EQSRIAANSS 240 CLLKGSDTEI DEDDFALEAE DLAALDSLER QYSQLPNSTV TASAKDIEKT AKVNHVGGDL 300 QSYCSATKAS DATINEEPVN LALDKACNSL PDINSDFIDD WDDSCDGCTP GELCEFSSEY 360 TVLEVHEDFI FHEGNHFRQL KLILEANDIL HQLFLRGDWT ETSIFVGDSI RVEATFDKDN 420 TAIVDNDKGL IIIHPKILMS ATAVASSFPC LRKAVISDRV GIYGPPTKAM VTGNILHDFF 480 QHALYRGIDA LENVDINLET SIKTYISDIY FADLSLDEIR EELDARLPLL KSIVERYLIS 540 KKNDNNNESI HISRLLDIEE SIWSPRFGLK GNIDATVEVV LTEKPESSST LTLPLELKTG 600 RYVDNISHFA QSLLYTLLIS DRYGINTNQA LLCYLENSTI KNLVASNSQL RGLIMTRNSL 660 AQHNFRRSLP EMISNRKICD HCSLVSECLF FQKMSDKGVA NSNGLTESWN EWMREVKDED 720 LEFYKKWEKL LNQEERLLLL KRGDVLTFDT EELEAYGKTL YPLYITKEDI VCLEIDDRVF 780 HYKFAFLNDN GYPRNFLHSG FSVGERVFIS DEHGHWSLAK GHIVHIQDSC IEVRTRHRLH 840 IPWLKMPNFD FKKNQVFFGN YEDSKLSFIG SNHTRYRIDK DEFSSGIASI RGTLMSSVLP 900 DAPLIIRDMI IRLKPPKFCN SALIDPEFLK CLNEDQITAL KKCHAAEHYS LILGMPGTGK 960 TTTISSLIRS LLAKKKKILL TSFTHLAVDN ILIKLKGCDS TIVRLGSPHK IHPLVKEFCL 1020 TEGTTFDDLA SLKHFYEDPQ IVACSSLGVY HSIFNKRKFD YCIIDEASQI PLPICLGPLQ 1080 LAEKFVLVGD HYQLPPLVKN SRTSKDGLSL SLFKLLSEKH PEAVTTLRLQ YRMNEDINSL 1140 SSELIYGGNL VCGSKTISQK KLILPKAHLS DGLPDSSSSL HWVNKLINPS HSVIFFNTDD 1200 ILGVESKTNN ILENHTEAFL IEQAVSSFLE RGVKQSSIGI ISIYKSQVEL LSKNLKSFTE 1260 IEINTVDRYQ GRDKDIILIS FVRSNSKNLV GELLRDWHRL NVALSRAKVK CIMFGSLSTL 1320 SSSNIVSHLL KLLEKNKWIF TLNENDIATK FDENSSPIKD CSQVATTNNA KVIIRKNQRF 1380 FNSDNLCEKA ILPQLEF
1398Fasta Sequence
>Q9URU2|dna2|Schizosaccharomyces pombe (strain 972 / ATCC 24843)(Fission yeast) MFNDQSKTTSSVKGICATTDNNHGNLKKTNSTPFRKNYLLNGRTKLKLENFAYNASTEISSPKISEKKHSSLPIKRKNTFNESSTSFSPFTKAHKEITDDLKPDKSFTRKSDLNSQDMPVCFQETSKDLCRSSSTQHLLDHQTTDSTIIDMKPVSTNSKSDVFTLYTDETVLLRRCASDNKPLINNNLSSSNVSENQSRSFGSYDEVKNQGNNLHKVPSLVSIIRNARSSEQSRIAANSSCLLKGSDTEIDEDDFALEAEDLAALDSLERQYSQLPNSTVTASAKDIEKTAKVNHVGGDLQSYCSATKASDATINEEPVNLALDKACNSLPDINSDFIDDWDDSCDGCTPGELCEFSSEYTVLEVHEDFIFHEGNHFRQLKLILEANDILHQLFLRGDWTETSIFVGDSIRVEATFDKDNTAIVDNDKGLIIIHPKILMSATAVASSFPCLRKAVISDRVGIYGPPTKAMVTGNILHDFFQHALYRGIDALENVDINLETSIKTYISDIYFADLSLDEIREELDARLPLLKSIVERYLISKKNDNNNESIHISRLLDIEESIWSPRFGLKGNIDATVEVVLTEKPESSSTLTLPLELKTGRYVDNISHFAQSLLYTLLISDRYGINTNQALLCYLENSTIKNLVASNSQLRGLIMTRNSLAQHNFRRSLPEMISNRKICDHCSLVSECLFFQKMSDKGVANSNGLTESWNEWMREVKDEDLEFYKKWEKLLNQEERLLLLKRGDVLTFDTEELEAYGKTLYPLYITKEDIVCLEIDDRVFHYKFAFLNDNGYPRNFLHSGFSVGERVFISDEHGHWSLAKGHIVHIQDSCIEVRTRHRLHIPWLKMPNFDFKKNQVFFGNYEDSKLSFIGSNHTRYRIDKDEFSSGIASIRGTLMSSVLPDAPLIIRDMIIRLKPPKFCNSALIDPEFLKCLNEDQITALKKCHAAEHYSLILGMPGTGKTTTISSLIRSLLAKKKKILLTSFTHLAVDNILIKLKGCDSTIVRLGSPHKIHPLVKEFCLTEGTTFDDLASLKHFYEDPQIVACSSLGVYHSIFNKRKFDYCIIDEASQIPLPICLGPLQLAEKFVLVGDHYQLPPLVKNSRTSKDGLSLSLFKLLSEKHPEAVTTLRLQYRMNEDINSLSSELIYGGNLVCGSKTISQKKLILPKAHLSDGLPDSSSSLHWVNKLINPSHSVIFFNTDDILGVESKTNNILENHTEAFLIEQAVSSFLERGVKQSSIGIISIYKSQVELLSKNLKSFTEIEINTVDRYQGRDKDIILISFVRSNSKNLVGELLRDWHRLNVALSRAKVKCIMFGSLSTLSSSNIVSHLLKLLEKNKWIFTLNENDIATKFDENSSPIKDCSQVATTNNAKVIIRKNQRFFNSDNLCEKAILPQLEF
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Keyword |
KW-0004--4Fe-4S KW-0067--ATP-binding KW-0158--Chromosome KW-0181--Complete proteome KW-0963--Cytoplasm KW-0227--DNA damage KW-0234--DNA repair KW-0235--DNA replication KW-0238--DNA-binding KW-0255--Endonuclease KW-0347--Helicase KW-0378--Hydrolase KW-0408--Iron KW-0411--Iron-sulfur KW-0479--Metal-binding KW-0511--Multifunctional enzyme KW-0540--Nuclease KW-0547--Nucleotide-binding KW-0539--Nucleus KW-0597--Phosphoprotein KW-1185--Reference proteome KW-0779--Telomere
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Interpro |
IPR026851--Dna2 IPR022765--Dna2/Cas4_DUF83 IPR014808--DNA_replication_fac_Dna2_N IPR027417--P-loop_NTPase
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PROSITE |
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Pfam |
PF01930--Cas_Cas4 PF08696--Dna2
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Gene Ontology |
GO:0000781--C:chromosome, telomeric region GO:0005829--C:cytosol GO:0043596--C:nuclear replication fork GO:0005634--C:nucleus GO:0005657--C:replication fork GO:0035861--C:site of double-strand break GO:0051539--F:4 iron, 4 sulfur cluster binding GO:1990601--F:5' overhang single-stranded DNA endodeoxyribonuclease activity GO:0017108--F:5'-flap endonuclease activity GO:0005524--F:ATP binding GO:0004003--F:ATP-dependent DNA helicase activity GO:0003682--F:chromatin binding GO:0046872--F:metal ion binding GO:0004518--F:nuclease activity GO:0019901--F:protein kinase binding GO:0045145--F:single-stranded DNA 5'-3' exodeoxyribonuclease activity GO:0043142--F:single-stranded DNA-dependent ATPase activity GO:0042162--F:telomeric DNA binding GO:0032508--P:DNA duplex unwinding GO:0006281--P:DNA repair GO:0090305--P:nucleic acid phosphodiester bond hydrolysis GO:1903461--P:Okazaki fragment processing involved in mitotic DNA replication GO:1903469--P:removal of RNA primer involved in mitotic DNA replication GO:0031297--P:replication fork processing GO:0071932--P:replication fork reversal GO:0072429--P:response to intra-S DNA damage checkpoint signaling GO:0000723--P:telomere maintenance GO:0031860--P:telomeric 3' overhang formation
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