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RAD50_DICDI
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   03-AUG-2022, entry version 110.
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 (Slime mold).
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}.
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DR   EMBL; AAFI02000196; EAL61067.1; -; Genomic_DNA.
DR   RefSeq; XP_629462.1; XM_629460.1.
DR   AlphaFoldDB; Q54CS9; -.
DR   SMR; Q54CS9; -.
DR   STRING; 44689.DDB0232401; -.
DR   PaxDb; Q54CS9; -.
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; CFGVNCG; -.
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   Reactome; R-DDI-5693607; Processing of DNA double-strand break ends.
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:0140664; F:ATP-dependent DNA damage sensor 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:0090305; P:nucleic acid phosphodiester bond hydrolysis; 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   CDD; cd03240; ABC_Rad50; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR045171; ABC_Rad50.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
DR   InterPro; IPR013134; Zn_hook_RAD50.
DR   Pfam; PF13476; AAA_23; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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
 
 
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