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F6QXW0 · DNA2_XENTR

Function

function

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 by mediating 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).

Catalytic activity

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site142[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site395[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site398[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site404[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site649-656ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentnucleus
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Function5'-3' DNA helicase activity
Molecular Function5'-flap endonuclease activity
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionDNA binding
Molecular Functionmetal ion binding
Molecular Functionnuclease activity
Molecular Functionsingle-stranded DNA helicase activity
Biological Processbase-excision repair
Biological ProcessDNA double-strand break processing
Biological ProcessDNA replication
Biological ProcessDNA replication checkpoint signaling
Biological ProcessDNA replication, Okazaki fragment processing

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    DNA replication ATP-dependent helicase/nuclease DNA2
  • Alternative names
    • DNA replication ATP-dependent helicase-like homolog

Including 2 domains:

  • Recommended name
    DNA replication ATP-dependent helicase DNA2
  • EC number

Gene names

    • Name
      dna2

Organism names

Accessions

  • Primary accession
    F6QXW0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004194671-1048DNA replication ATP-dependent helicase/nuclease DNA2

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region86-521Nuclease activity
Region522-1048Helicase activity
Region683-724Disordered
Compositional bias686-700Basic residues
Compositional bias701-721Polar residues

Sequence similarities

Belongs to the DNA2/NAM7 helicase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,048
  • Mass (Da)
    118,558
  • Last updated
    2011-07-27 v1
  • MD5 Checksum
    5B410277ACDA2B287741B34671B44E76
MEPVSAECQLPPEDDLLEMMMEQSFTEPEEKSKDKSTRKIIPKTKLCRGLNNRYCVLNVKEVYAQGEEKHLTITASQEGDDLELCILKDDWVALHIKPGDIIHLEGNCAFDNTWTISRDTGYLILYPDLLISGTSIANGIRCLRRSVLSEKFKVCDKGSRQMLIGTMLHDIFQRATTRGFTDSVLQELAHHTVHGPKYLKEMYQLKLNQTDVMGEVQEYLPSFAKWAIDFMTHPLNQHQINVTRPTAGDPTEATKVSEFLDIEENIWSPRFGLKGKIDVTARVKIHQKSKSHLKIMPLELKTGKESNSIEHRSQVVLYTLLSQERREDPEAGLLLYLKTGNMYSVPGNRLDRRELLKIRNELSYYLTNVVHKSDNGSKEITLASLPALIADRQACKFCSQMRNCALYSRSVEQQIENCYIPAEMIPVVQKETEHLNKDHLQYFRLWYLMCTLEGNSKDSKMGRKNIWMMSSSEREEDGQCIGNLIRTGPVQTISDGQHLHSFQRKSGTVPATNLMSGDRVVVSGEDKFLALSSGYIKEVKHNNITCILDRSLGKLPEDLLFRLDHEEGGGGLESHLGNLSRLMENSPVSDKLRKLIIDFSKPNFVQHLSSVLPSDAKDIVANILKGLNKPQKQAMKRVLLSKDYTLIVGMPGTGKTTTICTLVSTLHLKTCTSCLVDDHREAAGTHRSHRHSKGTVNLGKQKRQHRVTSTTSSTSAKCRSKTEPAVSAENKKLQKLISGSHVCIMVNGHKTFSQNNYIIFFDNILLLKKLPLHYMCAFALIHHQCFKGCVKSVSLVRELGMSESLFKRLERNQEAVVQLTVQYRMNSQIMALSNKLVYEGRLECASDRVSNAVVKLPHIKTLLLELEFRESQESMWIKDVLEPSNPVCFLNTEKIPALETEEKGGISNWIEAKLVFCLTKLFLKAGCRPSDIGIIAPYRQQLKVISNYFNSLSASAVEVNTVDKYQGRDKSVIIVSFVRSNIDGKLGDLLKDWRRLNVALTRAKHKLIMLGCVPTLSRFLCLEQLICHLKSKNHIYDLPAGAHEHMPV

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8J0QRW9A0A8J0QRW9_XENTRdna21053

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias686-700Basic residues
Compositional bias701-721Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAMC01051984
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AAMC01051985
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AAMC01051986
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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