A0A4D7H9D1 · A0A4D7H9D1_9EURY

  • Protein
    DNA double-strand break repair Rad50 ATPase
  • Gene
    rad50
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per homodimer.

Features

Showing features for binding site.

1897100200300400500600700800
TypeIDPosition(s)Description
Binding site12ATP (UniProtKB | ChEBI)
Binding site32-38ATP (UniProtKB | ChEBI)
Binding site140ATP (UniProtKB | ChEBI)
Binding site457Zn2+ (UniProtKB | ChEBI)
Binding site460Zn2+ (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
    • ORF names
      FCF25_11250

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MHR1
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloprofundus

Accessions

  • Primary accession
    A0A4D7H9D1

Proteomes

Interaction

Subunit

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

Family & Domains

Features

Showing features for compositional bias, region, domain, coiled coil.

TypeIDPosition(s)Description
Compositional bias339-354Polar residues
Region339-386Disordered
Compositional bias355-386Basic and acidic residues
Domain410-509Zinc-hook
Region456-490Disordered
Compositional bias512-655Basic and acidic residues
Region512-662Disordered
Coiled coil679-733
Region873-897Disordered

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
    897
  • Mass (Da)
    101,880
  • Last updated
    2019-07-03 v1
  • Checksum
    5C9D636E87F33E92
MRFDRIRLKNFKPYADTDLELGEGVTVIHGLNGSGKSSLLEACFFALYGAKALDGTLEDVVTNGEEESEIELWFTHAGEKYRIERRIRLSGERATTAKCVLEGSAVPDGSVDGARDVRKFVVDLLRMDADAFVNCAYVRQGEVNKLINATPGERQDMIDDLLQLGKLEEYRERARNARLGVEDVLENKRGRLDELDSQVEAKEAANPYERLSALRTELSEVKAAIERYETQRERAEKSRDEAIETLDDYEEKRTELGDLDDDIESLKSAIAETEEKRETLRENAREVRERIDELESAVADAVAGSELDADDGDAVSARLTELSTRHEELTESIQELREKAQGFENQSSNLGEKATDLESRAEQKRTRADELEAERETAEAELDDRREALDDLDARIDDLDATFEDAPVDRGDASEHLADLREQKSSLRDELETVRTKLRSTRQRVEEARRLLDEGKCPECGQPVDESPHVDTLDEDRARVDDLDDEREELEAEVASLDDDIDTAAELVDAENELERLRERRDSVTTLVDQRERTLAEKAEQAEAARTAAEEHEGKAEELREAAEQTASRAEETRDRIAELEEEREGVKSSEERLERIQSLRDEISDAESKLDRLSERRSDLDELNDERRERLAEKQRRRRELREDVDESQIRQAKEQRSNAEQYLKQVEPELESLAEKRTKLDNDIGGAKTDIERLEELQEKRDHVEERVDALESLHEETEELEAMYGDLRAELRQRNVETLERMLNETFDLVYANDAYARIRLDGEYALTVYQKDGQALDPEQLSGGERALFNLSLRCAIYRLLAEGIEGAAPTPPLILDEPTVFLDSGHVGRLVDLVQEMRGFGVRQIIIVSHDDELVGAADDLVTVEKNPTSNRSTVRHEEAAGLSAVESVADD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias339-354Polar residues
Compositional bias355-386Basic and acidic residues
Compositional bias512-655Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP039833
EMBL· GenBank· DDBJ
QCJ47660.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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