Q9W252 · RAD50_DROME
- ProteinDNA repair protein RAD50
- Generad50
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1318 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:15135728, PubMed:15296753).
The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (By similarity).
The complex 1 mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is 2 required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (By similarity).
The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (By similarity).
Within the complex, RAD50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11 (By similarity).
RAD50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the MRE11 active site: ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form (By similarity).
The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (By similarity).
The complex 1 mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is 2 required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (By similarity).
The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (By similarity).
Within the complex, RAD50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11 (By similarity).
RAD50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the MRE11 active site: ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form (By similarity).
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Cofactor
Note: Binds 1 zinc ion per homodimer.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 13 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 38 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 39 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 41 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 42 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 43 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 43 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 44 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 68 | ATP (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 70 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 166 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 166 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 689 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 692 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome, telomeric region | |
Cellular Component | condensed chromosome | |
Cellular Component | condensed nuclear chromosome | |
Cellular Component | Mre11 complex | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | double-stranded DNA binding | |
Molecular Function | double-stranded telomeric DNA binding | |
Molecular Function | G-quadruplex DNA binding | |
Molecular Function | metal ion binding | |
Molecular Function | single-stranded telomeric DNA binding | |
Biological Process | chromosome organization | |
Biological Process | chromosome organization involved in meiotic cell cycle | |
Biological Process | DNA duplex unwinding | |
Biological Process | DNA repair | |
Biological Process | double-strand break repair | |
Biological Process | protein localization | |
Biological Process | telomere maintenance | |
Biological Process | telomere maintenance via recombination | |
Biological Process | telomere maintenance via telomerase |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA repair protein RAD50
- EC number
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9W252
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to DNA double-strand breaks (DSBs).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Death during pupal stage, possibly due to the accumulation of DNA DSBs and the induction of apoptosis in third instar larvae.
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 208 | in strain: NC335, NC362 and NC390 | ||||
Sequence: E → D | ||||||
Natural variant | 219 | in strain: NC335, NC362 and NC390 | ||||
Sequence: H → V | ||||||
Natural variant | 220 | in strain: NC335, NC362 and NC390 | ||||
Sequence: V → E | ||||||
Natural variant | 246 | in strain: MW25 | ||||
Sequence: A → E | ||||||
Natural variant | 249 | in strain: MW25 | ||||
Sequence: S → M | ||||||
Natural variant | 281 | in strain: NC306 | ||||
Sequence: E → Q | ||||||
Natural variant | 349 | in strain: MW9 | ||||
Sequence: K → T | ||||||
Natural variant | 422 | in strain: NC361 and NC375 | ||||
Sequence: V → E | ||||||
Natural variant | 450 | in strain: MW6 | ||||
Sequence: V → I | ||||||
Natural variant | 480 | in strain: MW6 | ||||
Sequence: D → N | ||||||
Natural variant | 490 | in strain: MW25, MW27, MW56, MW9, NC303, NC306, NC335, NC336, NC390 and NC399 | ||||
Sequence: E → Q | ||||||
Natural variant | 491 | in strain: NC303, NC306 and NC335 | ||||
Sequence: V → I | ||||||
Natural variant | 580 | in strain: MW25 | ||||
Sequence: C → S | ||||||
Natural variant | 586 | in strain: MW25 | ||||
Sequence: M → I | ||||||
Natural variant | 623 | in strain: NC336, NC358, NC361, NC362 and NC375 | ||||
Sequence: S → N | ||||||
Natural variant | 646 | in strain: NC357 and NC397 | ||||
Sequence: T → S | ||||||
Natural variant | 657 | in strain: MW6, NC357, NC358, NC361, NC362, NC375 and NC397 | ||||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 17 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000138645 | 1-1318 | DNA repair protein RAD50 | |||
Sequence: MSSIESLSIQGIRSFGTYADDLQSIKFSSPVTLILGENGCGKTTVVECLKYALTGECPPGSDRGKSFVHDPKIFGLNEVLAQIKMQVRDRRGAQVSICRTMKVSKKRNKMSFETMDSTINFLTGAGQSKREKQDSLSGRSVDIDVAISDFMGVSKAIINNVLFCHQEDSSWPLDESKKLKEKFDAIFGITEYNKALDKIIKLRKEAMEELKIKEANIKHVAYLKQEMEVKTLNLQKAQRKCDAIKAQCSECEEEMKPIEARLVEIRNVEFEIGKYQAQKVEMDTKHKNCKDQISTLTLKIKKPFRGTLDELDQEISNFDQRMLEMRQKRTEVEGDLSQIKRSSVAEQEKLGTQDRKHCLAKQRHQSELACRAQLLKRVKEFCRELHIPIDCDLVEQPEKMGEVLRDIEAMIITKHCEITEIVEQNEKADRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIETSMQDLKKLEKEINEVNELYESATKNIDQQAIKDAIARKKASIAENQIQFKKLDEQLTFLGSMAKLVAECSLKQKELDKKNQEVHRVRSRHSDHFGKLFKEPITCNYRRSMQVVYEKLRREIQELNEKANTQKLKEQSYEIKRKNLISDISRMEKELKDSEELIYQKCRSTPYDDLLERSKTTISKLQFDHGALKSSEALYKKYIQKMDEEPSCPLCHHNMTSDEACDLTSELTDEIQKLPDNITRAEKALKAEQIKYENLLQLKPTILKVKELKDSLPQKKEELKKVEELLGDSVSEYETLIALIGEPTHNMELANSMMGDMSLLDEALKDSARLTKDLDLQKGQLPASYDSSVSMDDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLKERLEKLNSFLTTVASEISELKAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAKLDLRNEIKKLDEIIMASKDKLRKLEAEISLKTDELETIKTECSNQQTVERDLKDNRELKQLEDKEAKLRESCQVLDKQLGNLDFHSVSKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDEPRFKESLKNFRKANYEIEVTRLCIEDLGQYRLALEWALIQFHSEKMEMINRLIREYWRKIYRGNDIDYIQVKTDEVSSDASADRRKTYNYRVVQSKNYSEIEMRGRCSAGQRVLASLIIRLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNCIVEERQSQSNFMLIIITHDENFVSSLGKITSYHRVFRNEECKSVIRRVEAGPSKKALIDQ |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for coiled coil, region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 189-256 | |||||
Sequence: ITEYNKALDKIIKLRKEAMEELKIKEANIKHVAYLKQEMEVKTLNLQKAQRKCDAIKAQCSECEEEMK | ||||||
Coiled coil | 305-333 | |||||
Sequence: RGTLDELDQEISNFDQRMLEMRQKRTEVE | ||||||
Coiled coil | 434-641 | |||||
Sequence: VKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIETSMQDLKKLEKEINEVNELYESATKNIDQQAIKDAIARKKASIAENQIQFKKLDEQLTFLGSMAKLVAECSLKQKELDKKNQEVHRVRSRHSDHFGKLFKEPITCNYRRSMQVVYEKLRREIQELNEKANTQKLKEQSYEIKRKNLISDISRMEKELKDSEELIYQ | ||||||
Region | 447-466 | Disordered | ||||
Sequence: EQSVTAQEKQRESSKRESET | ||||||
Compositional bias | 451-466 | Basic and acidic residues | ||||
Sequence: TAQEKQRESSKRESET | ||||||
Coiled coil | 645-685 | |||||
Sequence: STPYDDLLERSKTTISKLQFDHGALKSSEALYKKYIQKMDE | ||||||
Domain | 645-741 | Zinc-hook | ||||
Sequence: STPYDDLLERSKTTISKLQFDHGALKSSEALYKKYIQKMDEEPSCPLCHHNMTSDEACDLTSELTDEIQKLPDNITRAEKALKAEQIKYENLLQLKP | ||||||
Coiled coil | 713-741 | |||||
Sequence: QKLPDNITRAEKALKAEQIKYENLLQLKP | ||||||
Coiled coil | 830-1101 | |||||
Sequence: VSMDDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLKERLEKLNSFLTTVASEISELKAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAKLDLRNEIKKLDEIIMASKDKLRKLEAEISLKTDELETIKTECSNQQTVERDLKDNRELKQLEDKEAKLRESCQVLDKQLGNLDFHSVSKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDE |
Domain
The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that 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. The two heads of the homodimer, which constitute the ATP-binding domain, interact with the MRE11 homodimer.
Sequence similarities
Belongs to the SMC family. RAD50 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,318
- Mass (Da)152,160
- Last updated2012-04-18 v4
- Checksum1C84EB7B3F9E3BB9
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0B4K7L0 | A0A0B4K7L0_DROME | rad50 | 1318 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 451-466 | Basic and acidic residues | ||||
Sequence: TAQEKQRESSKRESET | ||||||
Sequence conflict | 880 | in Ref. 5; AAK93530 | ||||
Sequence: R → K | ||||||
Sequence conflict | 959 | in Ref. 5; AAK93530 | ||||
Sequence: H → Q |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE013599 EMBL· GenBank· DDBJ | AAF46847.3 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT003555 EMBL· GenBank· DDBJ | AAO39559.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
FJ219324 EMBL· GenBank· DDBJ | ACI97309.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219329 EMBL· GenBank· DDBJ | ACI97314.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219330 EMBL· GenBank· DDBJ | ACI97315.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219331 EMBL· GenBank· DDBJ | ACI97316.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219332 EMBL· GenBank· DDBJ | ACI97317.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219333 EMBL· GenBank· DDBJ | ACI97318.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219334 EMBL· GenBank· DDBJ | ACI97319.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219335 EMBL· GenBank· DDBJ | ACI97320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219336 EMBL· GenBank· DDBJ | ACI97321.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219337 EMBL· GenBank· DDBJ | ACI97322.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219338 EMBL· GenBank· DDBJ | ACI97323.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219339 EMBL· GenBank· DDBJ | ACI97324.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219340 EMBL· GenBank· DDBJ | ACI97325.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219341 EMBL· GenBank· DDBJ | ACI97326.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219342 EMBL· GenBank· DDBJ | ACI97327.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219343 EMBL· GenBank· DDBJ | ACI97328.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219344 EMBL· GenBank· DDBJ | ACI97329.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219345 EMBL· GenBank· DDBJ | ACI97330.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219346 EMBL· GenBank· DDBJ | ACI97331.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219347 EMBL· GenBank· DDBJ | ACI97332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219348 EMBL· GenBank· DDBJ | ACI97333.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219349 EMBL· GenBank· DDBJ | ACI97334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ219350 EMBL· GenBank· DDBJ | ACI97335.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY052106 EMBL· GenBank· DDBJ | AAK93530.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |