ID RAD50_DICDI Reviewed; 1351 AA.
AC Q54CS9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=DNA repair protein RAD50;
DE EC=3.6.-.-;
DE AltName: Full=DNA recombination/repair protein;
GN Name=rad50; ORFNames=DDB_G0292786;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Essential component of the MRN complex, a complex that
CC possesses single-stranded DNA endonuclease and 3' to 5' exonuclease
CC activities, and plays a central role in double-strand break (DSB)
CC repair, chromosome morphogenesis, DNA repair and meiosis. In the
CC complex, it mediates the ATP-binding and is probably required to bind
CC DNA ends and hold them in close proximity (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per homodimer. {ECO:0000250};
CC -!- SUBUNIT: Probable component of the MRN complex with mre11.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC {ECO:0000250}.
CC -!- DOMAIN: The zinc-hook, which separates the large intramolecular coiled
CC coil regions, contains 2 Cys residues that coordinate one molecule of
CC zinc with the help of the 2 Cys residues of the zinc-hook of another
CC RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of
CC the homodimer, which constitute the ATP-binding domain, interact with
CC the mre11 homodimer (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000196; EAL61067.1; -; Genomic_DNA.
DR RefSeq; XP_629462.1; XM_629460.1.
DR AlphaFoldDB; Q54CS9; -.
DR SMR; Q54CS9; -.
DR STRING; 44689.Q54CS9; -.
DR PaxDb; 44689-DDB0232401; -.
DR EnsemblProtists; EAL61067; EAL61067; DDB_G0292786.
DR GeneID; 8628852; -.
DR KEGG; ddi:DDB_G0292786; -.
DR dictyBase; DDB_G0292786; rad50.
DR eggNOG; KOG0962; Eukaryota.
DR HOGENOM; CLU_006184_0_0_1; -.
DR InParanoid; Q54CS9; -.
DR OMA; FSDYYYR; -.
DR PhylomeDB; Q54CS9; -.
DR Reactome; R-DDI-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-DDI-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-DDI-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR PRO; PR:Q54CS9; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR GO; GO:0030870; C:Mre11 complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:dictyBase.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0090304; P:nucleic acid metabolic process; IBA:GO_Central.
DR GO; GO:0000019; P:regulation of mitotic recombination; ISS:UniProtKB.
DR GO; GO:0000722; P:telomere maintenance via recombination; IBA:GO_Central.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR PANTHER; PTHR18867:SF12; DNA REPAIR PROTEIN RAD50; 1.
DR PANTHER; PTHR18867; RAD50; 1.
DR Pfam; PF13476; AAA_23; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Chromosome; Coiled coil; DNA damage; DNA repair;
KW Hydrolase; Meiosis; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Telomere; Zinc.
FT CHAIN 1..1351
FT /note="DNA repair protein RAD50"
FT /id="PRO_0000327594"
FT DOMAIN 688..784
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT COILED 182..224
FT /evidence="ECO:0000255"
FT COILED 250..290
FT /evidence="ECO:0000255"
FT COILED 338..358
FT /evidence="ECO:0000255"
FT COILED 458..562
FT /evidence="ECO:0000255"
FT COILED 606..715
FT /evidence="ECO:0000255"
FT COILED 760..1045
FT /evidence="ECO:0000255"
FT COILED 1074..1128
FT /evidence="ECO:0000255"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 732
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT BINDING 735
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 1351 AA; 156207 MW; B4AAFA88FAD0433D CRC64;
MTSIEKLLVQ GIRSFDPREA SVIDFYSPLT LIVGQNGAGK TTIIECLKYT CTGEMPPNCS
SGQAFIHDTK IAGESEVKAQ IKLRFKNPIG KPIVASRSLS LIQKSNKKQE YKQIDASLQS
YTSDGQKVSK SFRCSDMDKE IPDLMGVAKP ILKHVIFCHQ EDSNWPLSES AKLKLKFDEI
FSAVKYTKAL KSLKDKRKEL TTLIKELKLR LETISANIEH CNRIRKELIK AEEIYSNGNK
SLEDIKIAII EKQKTLSTIK IAESKLQELK NEVTVLNARK LEMERVKNQL FNSLTEVYQN
ETDEELVFMQ SEFNRECETM ATAEKELLEN SEVLLSQKEV INNLIKENSS QKGRLQSLIS
QQDSILSDRD KQMKELVTRY KMSDFIQIQL PYQKEIVIKF INEITQKFDT LTSGISNYSK
TNKQKLNAIQ MKINQKRVDS NQFTSSSNEK MSTITLNSKK IQSLDQEIQQ HTNSIGEIDT
LEKQIQFSQS ELSILKSDAN LQEIQQSLDN LTTEKLEIEK EIQSLQSSLK LLNLQASSRT
RLNIKRKEIQ QNQQNINSQL NSQIINSINL ILPNEFNNDN NNDDDDDQFR FNIIQRIEPI
VPLINKKRLI FTNQLNELKQ QFQILQNKKN QIDAQLTSSI EPQLKKKQIE LESYEKLIND
SKLKQSNLFE NVNSNNNNNN NNNNGITVLL FENKINEMKL SLEKLEKSFI VLESEDILYK
EYIEKANQDK ECSLCKNEMN GNELTSFVHT LETHCNDIPN QLKQLKIEIS NSKIQLEKFN
KLLPIIVKRE ELIEKSIPEL KESQKNLLEQ QLKSNEMVLE KQNQIESLES QSVLYQQVTL
VFQYIDQTKQ SIQSIESEIQ KEEKEIMKQS SDLRTIEEVD KDLEIQQEQL KTIEKEISNF
TNKQKNDQIG IFEKERQLIS IKNQLTTIKS ASGIIDHLRD TKKELQSNNQ QLQLEIENLQ
QSIDQSNNDA KQLENEFQQL EIEFEKKIDA YSKEKNTFSV RLDSINSLQS KILDPSELCK
QLNEIQEKNQ ELESNLSTLS QDYLIGQQHI STIQQNLSSK DITKRAISDN ISFRQHKNNV
EQIIRQISRK NELIKEMMQS QLEIDSNKLE QEINSLKSKF DQITGQTAVL QSQINSNRQE
LSKPTYKNID DVNKDLLIKL QTTETVGKDL DKYYKALDKS LMKYHTLKMD EINRSIKEIW
QTTYKGSDID TIEIRSEESG TANKTINYRV VMIKGDVELD MRGRCSAGQK VLACLVIRLA
LAENFCSNCG ILALDEPTSH LDRANIESFA NSLLNIIESR KSQKGFQLII ITHDEEFVQY
LSRGNYCDYY WRVTKNANQH SHLERKEIAE L
//
