Q97WH0 · RAD50_SACS2

Function

function

Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per homodimer.

Features

Showing features for binding site.

1864100200300400500600700800
TypeIDPosition(s)Description
Binding site32-38ATP (UniProtKB | ChEBI)
Binding site131ATP (UniProtKB | ChEBI)
Binding site426Zn2+ (UniProtKB | ChEBI)
Binding site429Zn2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionzinc ion binding
Biological Processdouble-strand break repair

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    DNA double-strand break repair Rad50 ATPase

Gene names

    • Name
      rad50
    • Ordered locus names
      SSO2249

Organism names

Accessions

  • Primary accession
    Q97WH0

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001386651-864DNA double-strand break repair Rad50 ATPase

Proteomic databases

Interaction

Subunit

Homodimer. Forms a heterotetramer composed of two Mre11 subunits and two Rad50 subunits.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for coiled coil, domain.

TypeIDPosition(s)Description
Coiled coil176-319
Coiled coil376-413
Domain380-478Zinc-hook
Coiled coil440-697

Domain

The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.

Sequence similarities

Belongs to the SMC family. RAD50 subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    864
  • Mass (Da)
    101,602
  • Last updated
    2001-09-26 v1
  • Checksum
    657076AEA9B709FC
MRIDKITLTNFLSHEHSEIQFMGEINVIVGQNGAGKSSIIDGIVFSLFRTHSRGNNDNLIRKGSNRGSVTLYLSNEKDKIEIIRDIRSTTEDRLIRNQFPIARSATVVSNEIEKILGIDKDIALSTIIVRQGELDKILENFQEIMGKILKLELIEKLIDSRGPIVEFRKNLENKLRELDRIEQDYNNFKKTVEEKRARVLELKKDKEKLEDEIKNLEKRIKDIKDQFDEYEKKRNQYLKLTTTLKIKEGELNELNRSIEELRKQTENMDQLEKEINELENLRNIKLKFEKYEVLAKSHTEMSANVINLEKEIEEYEKAIRRKEELEPKYLKYKELERKLEELQPKYQQYLKLKSDLDSKLNLKERLEKDASELSNDIDKVNSLEQKVEETRKKQLNLRAQLAKVESLISEKNEIINNISQVEGETCPVCGRPLDEEHKQKIIKEAKSYILQLELNKNELEEELKKITNELNKIEREYRRLSNNKASYDNVMRQLKKLNEEIENLHSEIESLKNIDEEIKKINEEVKELKLYYEEFMRLSKYTKEELDKKRVKLDEMKKKKEEIEKEMRGLESELKGLDRKALESKILDLENKRVKLDEMKKKKGILEDYIRQVKLLQEEVKNLREEVNIIQFDENRYNELKTSLDAYNLSLKEKENRKSRIEGELESLEKDIEEISNRIANYELQLKDREKIINAINKLEKIRSALGERKLQSYIIMTTKQLIENNLNDIISKFDLSIKNVEMEIMPKTGRGRSSSGDILVYTNSGDTLPIVSLSGGERIALSIALRLAIAKALMSNTNFFILDEPTIHLDDQRKAYLIEIIRAAKESVPQIIVVTHDEEVVQAADYVIRVEKRGNKSFVREET

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE006641
EMBL· GenBank· DDBJ
AAK42417.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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