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Protein

DNA replication ATP-dependent helicase/nuclease dna2

Gene

dna2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi450 – 4501Iron-sulfur (4Fe-4S)By similarity
Metal bindingi679 – 6791Iron-sulfur (4Fe-4S)By similarity
Metal bindingi682 – 6821Iron-sulfur (4Fe-4S)By similarity
Metal bindingi688 – 6881Iron-sulfur (4Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi954 – 9618ATPBy similarity

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • 5'-flap endonuclease activity Source: PomBase
  • 5' overhang single-stranded DNA endodeoxyribonuclease activity Source: PomBase
  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: PomBase
  • chromatin binding Source: PomBase
  • metal ion binding Source: UniProtKB-KW
  • nuclease activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • single-stranded DNA 5'-3' exodeoxyribonuclease activity Source: PomBase
  • single-stranded DNA-dependent ATPase activity Source: InterPro
  • telomeric DNA binding Source: PomBase

GO - Biological processi

  • DNA repair Source: PomBase
  • Okazaki fragment processing involved in mitotic DNA replication Source: PomBase
  • removal of RNA primer involved in mitotic DNA replication Source: PomBase
  • replication fork processing Source: PomBase
  • replication fork reversal Source: UniProtKB
  • response to intra-S DNA damage checkpoint signaling Source: UniProtKB
  • telomere maintenance Source: PomBase
  • telomeric 3' overhang formation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Helicase, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair, DNA replication

Keywords - Ligandi

4Fe-4S, ATP-binding, DNA-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-174437. Removal of the Flap Intermediate from the C-strand.
R-SPO-69166. Removal of the Flap Intermediate.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication ATP-dependent helicase/nuclease dna2
Including the following 2 domains:
DNA replication nuclease dna2 (EC:3.1.-.-)
DNA replication ATP-dependent helicase dna2 (EC:3.6.4.12)
Gene namesi
Name:dna2
ORF Names:SPBC16D10.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC16D10.04c.
PomBaseiSPBC16D10.04c. dna2.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: UniProtKB-SubCell
  • cytosol Source: PomBase
  • nuclear replication fork Source: PomBase
  • nucleus Source: PomBase
  • replication fork Source: UniProtKB
  • site of double-strand break Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi219 – 2191S → A: Impaired phosphorylation by cds1/check2, leading to stalled fork reversing. 1 Publication
Mutagenesisi219 – 2191S → D: Mimics phosphorylation; not able to rescue hydroxyurea-sensitivity in cds1 mutant cells. 1 Publication
Mutagenesisi559 – 5591E → A: Not able to complement a dna2(ts) mutant at restrictive temperature of 36 degrees Celsius. 1 Publication
Mutagenesisi960 – 9601K → T: Able to complement a dna2(ts) mutant at restrictive temperature of 36 degrees Celsius. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13971397DNA replication ATP-dependent helicase/nuclease dna2PRO_0000080710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei134 – 1341Phosphoserine1 Publication
Modified residuei219 – 2191Phosphoserine; by CHEK21 Publication

Post-translational modificationi

Phosphorylated at Ser-219 by cds1/check2, leading to association with stalled replication forks.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9URU2.

PTM databases

iPTMnetiQ9URU2.

Interactioni

Subunit structurei

Interacts with cdc1, cdc24 and rad2.1 Publication

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi276685. 17 interactions.
DIPiDIP-61017N.
MINTiMINT-4707004.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni390 – 808419Nuclease activityBy similarityAdd
BLAST
Regioni809 – 1397589Helicase activityBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the DNA2/NAM7 helicase family.Curated

Phylogenomic databases

InParanoidiQ9URU2.
KOiK10742.
OMAiHWCGLLA.
OrthoDBiEOG092C07AQ.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR026851. Dna2.
IPR022765. Dna2/Cas4_DUF83.
IPR014808. DNA_replication_fac_Dna2_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10887:SF14. PTHR10887:SF14. 4 hits.
PfamiPF01930. Cas_Cas4. 1 hit.
PF08696. Dna2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9URU2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNDQSKTTS SVKGICATTD NNHGNLKKTN STPFRKNYLL NGRTKLKLEN
60 70 80 90 100
FAYNASTEIS SPKISEKKHS SLPIKRKNTF NESSTSFSPF TKAHKEITDD
110 120 130 140 150
LKPDKSFTRK SDLNSQDMPV CFQETSKDLC RSSSTQHLLD HQTTDSTIID
160 170 180 190 200
MKPVSTNSKS DVFTLYTDET VLLRRCASDN KPLINNNLSS SNVSENQSRS
210 220 230 240 250
FGSYDEVKNQ GNNLHKVPSL VSIIRNARSS EQSRIAANSS CLLKGSDTEI
260 270 280 290 300
DEDDFALEAE DLAALDSLER QYSQLPNSTV TASAKDIEKT AKVNHVGGDL
310 320 330 340 350
QSYCSATKAS DATINEEPVN LALDKACNSL PDINSDFIDD WDDSCDGCTP
360 370 380 390 400
GELCEFSSEY TVLEVHEDFI FHEGNHFRQL KLILEANDIL HQLFLRGDWT
410 420 430 440 450
ETSIFVGDSI RVEATFDKDN TAIVDNDKGL IIIHPKILMS ATAVASSFPC
460 470 480 490 500
LRKAVISDRV GIYGPPTKAM VTGNILHDFF QHALYRGIDA LENVDINLET
510 520 530 540 550
SIKTYISDIY FADLSLDEIR EELDARLPLL KSIVERYLIS KKNDNNNESI
560 570 580 590 600
HISRLLDIEE SIWSPRFGLK GNIDATVEVV LTEKPESSST LTLPLELKTG
610 620 630 640 650
RYVDNISHFA QSLLYTLLIS DRYGINTNQA LLCYLENSTI KNLVASNSQL
660 670 680 690 700
RGLIMTRNSL AQHNFRRSLP EMISNRKICD HCSLVSECLF FQKMSDKGVA
710 720 730 740 750
NSNGLTESWN EWMREVKDED LEFYKKWEKL LNQEERLLLL KRGDVLTFDT
760 770 780 790 800
EELEAYGKTL YPLYITKEDI VCLEIDDRVF HYKFAFLNDN GYPRNFLHSG
810 820 830 840 850
FSVGERVFIS DEHGHWSLAK GHIVHIQDSC IEVRTRHRLH IPWLKMPNFD
860 870 880 890 900
FKKNQVFFGN YEDSKLSFIG SNHTRYRIDK DEFSSGIASI RGTLMSSVLP
910 920 930 940 950
DAPLIIRDMI IRLKPPKFCN SALIDPEFLK CLNEDQITAL KKCHAAEHYS
960 970 980 990 1000
LILGMPGTGK TTTISSLIRS LLAKKKKILL TSFTHLAVDN ILIKLKGCDS
1010 1020 1030 1040 1050
TIVRLGSPHK IHPLVKEFCL TEGTTFDDLA SLKHFYEDPQ IVACSSLGVY
1060 1070 1080 1090 1100
HSIFNKRKFD YCIIDEASQI PLPICLGPLQ LAEKFVLVGD HYQLPPLVKN
1110 1120 1130 1140 1150
SRTSKDGLSL SLFKLLSEKH PEAVTTLRLQ YRMNEDINSL SSELIYGGNL
1160 1170 1180 1190 1200
VCGSKTISQK KLILPKAHLS DGLPDSSSSL HWVNKLINPS HSVIFFNTDD
1210 1220 1230 1240 1250
ILGVESKTNN ILENHTEAFL IEQAVSSFLE RGVKQSSIGI ISIYKSQVEL
1260 1270 1280 1290 1300
LSKNLKSFTE IEINTVDRYQ GRDKDIILIS FVRSNSKNLV GELLRDWHRL
1310 1320 1330 1340 1350
NVALSRAKVK CIMFGSLSTL SSSNIVSHLL KLLEKNKWIF TLNENDIATK
1360 1370 1380 1390
FDENSSPIKD CSQVATTNNA KVIIRKNQRF FNSDNLCEKA ILPQLEF
Length:1,397
Mass (Da):157,659
Last modified:October 3, 2012 - v2
Checksum:i5BE34210382E4B8C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144384 Genomic DNA. Translation: AAD38528.1.
CU329671 Genomic DNA. Translation: CAB38508.2.
AB028014 Genomic DNA. Translation: BAA87318.1.
AF075169 Genomic DNA. Translation: AAC39502.1.
PIRiT39568.
T47242.
T51292.
RefSeqiNP_596499.2. NM_001022420.2.

Genome annotation databases

EnsemblFungiiSPBC16D10.04c.1; SPBC16D10.04c.1:pep; SPBC16D10.04c.
GeneIDi2540148.
KEGGispo:SPBC16D10.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144384 Genomic DNA. Translation: AAD38528.1.
CU329671 Genomic DNA. Translation: CAB38508.2.
AB028014 Genomic DNA. Translation: BAA87318.1.
AF075169 Genomic DNA. Translation: AAC39502.1.
PIRiT39568.
T47242.
T51292.
RefSeqiNP_596499.2. NM_001022420.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276685. 17 interactions.
DIPiDIP-61017N.
MINTiMINT-4707004.

PTM databases

iPTMnetiQ9URU2.

Proteomic databases

MaxQBiQ9URU2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC16D10.04c.1; SPBC16D10.04c.1:pep; SPBC16D10.04c.
GeneIDi2540148.
KEGGispo:SPBC16D10.04c.

Organism-specific databases

EuPathDBiFungiDB:SPBC16D10.04c.
PomBaseiSPBC16D10.04c. dna2.

Phylogenomic databases

InParanoidiQ9URU2.
KOiK10742.
OMAiHWCGLLA.
OrthoDBiEOG092C07AQ.

Enzyme and pathway databases

ReactomeiR-SPO-174437. Removal of the Flap Intermediate from the C-strand.
R-SPO-69166. Removal of the Flap Intermediate.

Miscellaneous databases

PROiQ9URU2.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR026851. Dna2.
IPR022765. Dna2/Cas4_DUF83.
IPR014808. DNA_replication_fac_Dna2_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10887:SF14. PTHR10887:SF14. 4 hits.
PfamiPF01930. Cas_Cas4. 1 hit.
PF08696. Dna2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiDNA2_SCHPO
AccessioniPrimary (citable) accession number: Q9URU2
Secondary accession number(s): O74241, Q9UTT6, Q9UUK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: October 3, 2012
Last modified: September 7, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.