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Protein

DNA replication ATP-dependent helicase/nuclease DNA2

Gene

Dna2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Key enzyme involved in DNA replication and DNA repair in nucleus and mitochondrion. 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. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair: recruited by BLM and mediates the cleavage of 5'-ssDNA, while the 3'-ssDNA cleavage is prevented by the presence of RPA. Also involved in DNA replication checkpoint independently of Okazaki fragments processing. 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 subject to debate. According to various reports, the helicase activity is weak and its function remains largely unclear. Helicase activity may promote the motion of DNA2 on the flap, helping the nuclease function (By similarity).By similarity

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 bindingi137 – 1371Iron-sulfur (4Fe-4S)By similarity
Metal bindingi394 – 3941Iron-sulfur (4Fe-4S)By similarity
Metal bindingi397 – 3971Iron-sulfur (4Fe-4S)By similarity
Metal bindingi403 – 4031Iron-sulfur (4Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi648 – 6558ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication ATP-dependent helicase/nuclease DNA2
Alternative name(s):
DNA replication ATP-dependent helicase-like homolog
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1306791. Dna2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10591059DNA replication ATP-dependent helicase/nuclease DNA2PRO_0000419466Add
BLAST

Post-translational modificationi

Acetylated by EP300, leading to stimulate the 5'-3' endonuclease, the 5'-3' helicase and DNA-dependent ATPase activities, possibly by increasing DNA substrate affinity.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiD3ZG52.
PeptideAtlasiD3ZG52.

Interactioni

Subunit structurei

Interacts with BLM and WDHD1.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000438.

Structurei

3D structure databases

ProteinModelPortaliD3ZG52.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni82 – 519438Nuclease activityBy similarityAdd
BLAST
Regioni520 – 1059540Helicase activityBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the DNA2/NAM7 helicase family.Curated

Phylogenomic databases

eggNOGiKOG1805. Eukaryota.
COG1112. LUCA.
InParanoidiD3ZG52.
OMAiEHESLCH.
OrthoDBiEOG7K6PT8.
PhylomeDBiD3ZG52.
TreeFamiTF314903.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR026851. Dna2.
IPR014808. DNA_replication_fac_Dna2_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10887:SF14. PTHR10887:SF14. 2 hits.
PfamiPF08696. Dna2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

D3ZG52-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPLDDLDLL LLEEDSGAEA VPRMEILQKK ADAFFAETVL SRGVDNRYLV
60 70 80 90 100
LAVETKLNER GAEEKHLLIT VSQEGEQEVL CILRNGWSSV PVEPGDIIHI
110 120 130 140 150
EGDCTSEPWI VDDDFGYFIL SPDMLISGTS VASSIRCLRR AVLSETFRVS
160 170 180 190 200
DTATRQMLIG TILHEVFQKA ISESFAPEKL QELALQTLRE VRHLKEMYRL
210 220 230 240 250
NLSQDEVRCE VEEYLPSFSK WADEFMHKGT KAEFPQMHLS LPSDSSDRSS
260 270 280 290 300
PCNIEVVKSL DIEESIWSPR FGLKGKIDVT VGVKIHRDCK TKYKIMPLEL
310 320 330 340 350
KTGKESNSIE HRGQVILYTL LSQERREDPE AGWLLYLKTG QMYPVPANHL
360 370 380 390 400
DKRELLKLRN QLAFSLLHRV SRAAAGEEAR LLALPQIIEE EKTCKYCSQM
410 420 430 440 450
GNCALYSRAV EQVHDTSIPE GMRSKIQEGT QHLTRAHLKY FSLWCLMLTL
460 470 480 490 500
ESQSKDTKKS HQSIWLTPAS KLEESGNCIG SLVRTEPVKR VCDGHYLHNF
510 520 530 540 550
QRKNGPMPAT NLMAGDRIIL SGEERKLFAL SKGYVKRIDT AAVTCLLDRN
560 570 580 590 600
LSTLPETTLF RLDREEKHGD INTPLGNLSK LMENTDSSKR LRELIIDFKE
610 620 630 640 650
PQFIAYLSSV LPHDAKDTVA NILKGLNKPQ RQAMKKVLLS KDYTLIVGMP
660 670 680 690 700
GTGKTTTICA LVRILSACGF SVLLTSYTHS AVDNILLKLA KFKIGFLRLG
710 720 730 740 750
QSHKVHPDIQ KFTEEEMCRL RSIASLAHLE ELYNSHPVVA TTCMGISHPM
760 770 780 790 800
FSRKTFDFCI VDEASQISQP ICLGPLFFSR RFVLVGDHKQ LPPLVLNREA
810 820 830 840 850
RALGMSESLF KRLERNESAV VQLTIQYRMN RKIMSLSNKL TYEGKLECGS
860 870 880 890 900
DRVANAVITL PNLKDVRLEF YADYSDNPWL AGVFEPDNPV CFLNTDKVPA
910 920 930 940 950
PEQIENGGVS NVTEARLIVF LTSTFIKAGC SPSDIGIIAP YRQQLRTITD
960 970 980 990 1000
LLARSSVGMV EVNTVDKYQG RDKSLILVSF VRSNEDGTLG ELLKDWRRLN
1010 1020 1030 1040 1050
VAITRAKHKL ILLGSVSSLK RFPPLEKLFD HLNAEQLISN LPSREHESLY

HILGDCQRD
Length:1,059
Mass (Da):119,588
Last modified:April 20, 2010 - v1
Checksum:iAAFC221E6785C5AF
GO

Genome annotation databases

UCSCiRGD:1306791. rat.

Cross-referencesi

3D structure databases

ProteinModelPortaliD3ZG52.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000438.

Proteomic databases

PaxDbiD3ZG52.
PeptideAtlasiD3ZG52.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:1306791. rat.

Organism-specific databases

RGDi1306791. Dna2.

Phylogenomic databases

eggNOGiKOG1805. Eukaryota.
COG1112. LUCA.
InParanoidiD3ZG52.
OMAiEHESLCH.
OrthoDBiEOG7K6PT8.
PhylomeDBiD3ZG52.
TreeFamiTF314903.

Miscellaneous databases

PROiD3ZG52.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR026851. Dna2.
IPR014808. DNA_replication_fac_Dna2_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10887:SF14. PTHR10887:SF14. 2 hits.
PfamiPF08696. Dna2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.

Entry informationi

Entry nameiDNA2_RAT
AccessioniPrimary (citable) accession number: D3ZG52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: April 20, 2010
Last modified: July 6, 2016
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. 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.