RAD50_YEAST
ID RAD50_YEAST Reviewed; 1312 AA.
AC P12753; D6W0U3;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=DNA repair protein RAD50;
DE EC=3.6.-.-;
DE AltName: Full=153 kDa protein;
GN Name=RAD50; OrderedLocusNames=YNL250W; ORFNames=N0872;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RE821;
RX PubMed=2659437; DOI=10.1093/genetics/122.1.47;
RA Alani E., Subbiah S., Kleckner N.;
RT "The yeast RAD50 gene encodes a predicted 153-kD protein containing a
RT purine nucleotide-binding domain and two large heptad-repeat regions.";
RL Genetics 122:47-57(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9234673;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<849::aid-yea106>3.0.co;2-n;
RA Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.;
RT "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the
RT left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL Yeast 13:849-860(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469 AND THR-568, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Involved in DNA double-strand break repair (DSBR). The
CC rad50/mre11 complex possesses single-strand endonuclease activity and
CC ATP-dependent double-strand-specific exonuclease activity. Rad50
CC provides ATP-dependent control of mre11 by unwinding and/or
CC repositioning DNA ends into the mre11 active site.
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: Homodimer (By similarity). Forms a complex with MRE11.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P12753; P39009: DUN1; NbExp=2; IntAct=EBI-14700, EBI-6194;
CC P12753; P32829: MRE11; NbExp=21; IntAct=EBI-14700, EBI-11255;
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. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 830 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; X14814; CAA32919.1; -; Genomic_DNA.
DR EMBL; X96722; CAA65494.1; -; Genomic_DNA.
DR EMBL; Z71526; CAA96157.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10309.1; -; Genomic_DNA.
DR PIR; S05808; BWBYDL.
DR RefSeq; NP_014149.1; NM_001183088.1.
DR AlphaFoldDB; P12753; -.
DR SMR; P12753; -.
DR BioGRID; 35589; 340.
DR ComplexPortal; CPX-1872; MRE11-RAD50-XRS2 meiotic recombination initiation complex.
DR DIP; DIP-2419N; -.
DR IntAct; P12753; 40.
DR MINT; P12753; -.
DR STRING; 4932.YNL250W; -.
DR iPTMnet; P12753; -.
DR MaxQB; P12753; -.
DR PaxDb; P12753; -.
DR PRIDE; P12753; -.
DR EnsemblFungi; YNL250W_mRNA; YNL250W; YNL250W.
DR GeneID; 855471; -.
DR KEGG; sce:YNL250W; -.
DR SGD; S000005194; RAD50.
DR VEuPathDB; FungiDB:YNL250W; -.
DR eggNOG; KOG0962; Eukaryota.
DR GeneTree; ENSGT00390000018781; -.
DR HOGENOM; CLU_006184_0_0_1; -.
DR InParanoid; P12753; -.
DR OMA; CFGVNCG; -.
DR BioCyc; YEAST:G3O-33247-MON; -.
DR Reactome; R-SCE-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-SCE-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR PRO; PR:P12753; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P12753; protein.
DR GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0030870; C:Mre11 complex; IPI:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:SGD.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:SGD.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
DR GO; GO:0006284; P:base-excision repair; IMP:SGD.
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:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:SGD.
DR GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IC:ComplexPortal.
DR GO; GO:0097552; P:mitochondrial double-strand break repair via homologous recombination; IMP:SGD.
DR GO; GO:0032078; P:negative regulation of endodeoxyribonuclease activity; IDA:SGD.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; IMP:SGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
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; IPR004584; Rad50_eukaryotes.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00606; rad50; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; DNA damage; DNA repair; Hydrolase; Meiosis;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Zinc.
FT CHAIN 1..1312
FT /note="DNA repair protein RAD50"
FT /id="PRO_0000138648"
FT DOMAIN 640..741
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT COILED 185..347
FT /evidence="ECO:0000255"
FT COILED 403..558
FT /evidence="ECO:0000255"
FT COILED 640..678
FT /evidence="ECO:0000255"
FT COILED 712..741
FT /evidence="ECO:0000255"
FT COILED 787..1108
FT /evidence="ECO:0000255"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT BINDING 690
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 568
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1312 AA; 152569 MW; 58A0AA173AC5677E CRC64;
MSAIYKLSIQ GIRSFDSNDR ETIEFGKPLT LIVGMNGSGK TTIIECLKYA TTGDLPPNSK
GGVFIHDPKI TGEKDIRAQV KLAFTSANGL NMIVTRNIQL LMKKTTTTFK TLEGQLVAIN
NSGDRSTLST RSLELDAQVP LYLGVPKAIL EYVIFCHQED SLWPLSEPSN LKKKFDEIFQ
AMKFTKALDN LKSIKKDMSV DIKLLKQSVE HLKLDKDRSK AMKLNIHQLQ TKIDQYNEEV
SEIESQLNEI TEKSDKLFKS NQDFQKILSK VENLKNTKLS ISDQVKRLSN SIDILDLSKP
DLQNLLANFS KVLMDKNNQL RDLETDISSL KDRQSSLQSL SNSLIRRQGE LEAGKETYEK
NRNHLSSLKE AFQHKFQGLS NIENSDMAQV NHEMSQFKAF ISQDLTDTID QFAKDIQLKE
TNLSDLIKSI TVDSQNLEYN KKDRSKLIHD SEELAEKLKS FKSLSTQDSL NHELENLKTY
KEKLQSWESE NIIPKLNQKI EEKNNEMIIL ENQIEKFQDR IMKTNQQADL YAKLGLIKKS
INTKLDELQK ITEKLQNDSR IRQVFPLTQE FQRADLEMDF QKLFINMQKN IAINNKKMHE
LDRRYTNALY NLNTIEKDLQ DNQKSKEKVI QLLSENLPED CTIDEYNDVL EETELSYKTA
LENLKMHQTT LEFNRKALEI AERDSCCYLC SRKFENESFK SKLLQELKTK TDANFEKTLK
DTVQNEKEYL HSLRLLEKHI ITLNSINEKI DNSQKCLEKA KEETKTSKSK LDELEVDSTK
LKDEKELAES EIRPLIEKFT YLEKELKDLE NSSKTISEEL SIYNTSEDGI QTVDELRDQQ
RKMNDSLREL RKTISDLQME KDEKVRENSR MINLIKEKEL TVSEIESSLT QKQNIDDSIR
SKRENINDID SRVKELEARI ISLKNKKDEA QSVLDKVKNE RDIQVRNKQK TVADINRLID
RFQTIYNEVV DFEAKGFDEL QTTIKELELN KAQMLELKEQ LDLKSNEVNE EKRKLADSNN
EEKNLKQNLE LIELKSQLQH IESEISRLDV QNAEAERDKY QEESLRLRTR FEKLSSENAG
KLGEMKQLQN QIDSLTHQLR TDYKDIEKNY HKEWVELQTR SFVTDDIDVY SKALDSAIMK
YHGLKMQDIN RIIDELWKRT YSGTDIDTIK IRSDEVSSTV KGKSYNYRVV MYKQDVELDM
RGRCSAGQKV LASIIIRLAL SETFGANCGV IALDEPTTNL DEENIESLAK SLHNIINMRR
HQKNFQLIVI THDEKFLGHM NAAAFTDHFF KVKRDDRQKS QIEWVDINRV TY
