Q0U5F2 · KU70_PHANO

Function

function

Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching (By similarity).

Catalytic activity

GO annotations

AspectTerm
Cellular Componentchromosome, telomeric region
Cellular ComponentKu70:Ku80 complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functiondamaged DNA binding
Molecular FunctionDNA helicase activity
Molecular Functiontelomeric DNA binding
Biological ProcessDNA recombination
Biological Processdouble-strand break repair via nonhomologous end joining
Biological Processtelomere maintenance

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent DNA helicase II subunit 1
  • EC number
  • Alternative names
    • ATP-dependent DNA helicase II subunit Ku70

Gene names

    • Name
      KU70
    • ORF names
      SNOG_13012

Organism names

Accessions

  • Primary accession
    Q0U5F2

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002783461-652ATP-dependent DNA helicase II subunit 1

Interaction

Subunit

Heterodimer of Ku70 and Ku80.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-22Disordered
Region38-59Disordered
Compositional bias43-58Basic and acidic residues
Domain274-486Ku
Region565-612Disordered
Compositional bias568-594Basic and acidic residues
Domain613-647SAP

Sequence similarities

Belongs to the ku70 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    652
  • Mass (Da)
    72,705
  • Last updated
    2006-09-05 v1
  • Checksum
    B4062F9323EB5179
MADTQDNRPGEEEDDDEEIDESAYKTMKDAVLFAIDVSPSMLERPPKTEDKKADRDSPTSAALKCAYQLMQQRIISNPNDMMGILLFGTEKTDLKDGDSTFQHCYLLADLDVPSAQDVKRLRDLVEDEEEAEQILKPAKDGASIATVLFCANQIFTTKAPNFSSRRLFLVTDNDYPVNVKADKDTAVTRARDLYDLGCTIDLFPISQPDQTFDRSRFYDDLVYPTSPSDPDAPIAVATTTKVAKSGEGITLLKQLISSINSKATPRRALFSLPLELGPDLRIGVKGYILIKRQEHAKSCYVWVGGDKPQIVSSSTSHMADDTARVVEKTELRKAYKFGGDAITFTPDEIIKIRQAFGDPIIRIIGFKPISCLPIWTNTNKATFIYPSEADFIGSTRVFSALQQKLLKSKKMGLVWFIARRNAAPILSALIPAEEQTNEDGEQAMPPGLWLVPLPWADDIRQFPSPAADVLKTTDALTDKMRIIIEQLQLPKGVYDPAKYPNPDLQWFYRILQAMALEEELPEKPDDKTMPKFRQIDKRCGEYITEYGAEFEAAFAQLAVSTFPHRGKRASADPGDDKPAPKRVKKEPKVKEEGEDDEGLTDEQMATVNNKGQISKQTVAVLKAWLSQRGESTSGKKADLVERVQGYLEGKGL

Sequence caution

The sequence EAT79812.2 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias43-58Basic and acidic residues
Compositional bias568-594Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CH445348
EMBL· GenBank· DDBJ
EAT79812.2
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.

Genome annotation databases

Similar Proteins

Disclaimer

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