RAD50_SCHPO
ID RAD50_SCHPO Reviewed; 1285 AA.
AC Q9UTJ8; Q9P3T5;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=DNA repair protein rad50;
DE EC=3.6.-.-;
GN Name=rad50; ORFNames=SPAC1556.01c, SPAP4C9.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH RAD21
RP COHESIN COMPLEX.
RX PubMed=11726502; DOI=10.1093/emboj/20.23.6660;
RA Hartsuiker E., Vaessen E., Carr A.M., Kohli J.;
RT "Fission yeast Rad50 stimulates sister chromatid recombination and links
RT cohesion with repair.";
RL EMBO J. 20:6660-6671(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12944482; DOI=10.1128/mcb.23.18.6564-6573.2003;
RA Chahwan C., Nakamura T.M., Sivakumar S., Russell P., Rhind N.;
RT "The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-
RT phase DNA damage checkpoint.";
RL Mol. Cell. Biol. 23:6564-6573(2003).
CC -!- FUNCTION: Involved in DNA double-strand break (DSB) repair. Involved in
CC mating type switching and has a role in choosing the sister chromatid
CC for recombinational repair. Also has a role in telomere length
CC maintenance. {ECO:0000269|PubMed:11726502}.
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: Heterodimer (By similarity). Interacts with the rad21 cohesin
CC complex. Forms a multisubunit endonuclease complex, MRN, together with
CC nbn and rad32. {ECO:0000250, ECO:0000269|PubMed:11726502,
CC ECO:0000269|PubMed:12944482}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12944482}. Chromosome
CC {ECO:0000269|PubMed:12944482}.
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 -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB96041.3; -; Genomic_DNA.
DR PIR; T50080; T50080.
DR RefSeq; XP_001713090.2; XM_001713038.3.
DR AlphaFoldDB; Q9UTJ8; -.
DR SMR; Q9UTJ8; -.
DR BioGRID; 278131; 33.
DR DIP; DIP-52389N; -.
DR IntAct; Q9UTJ8; 1.
DR STRING; 4896.SPAC1556.01c.1; -.
DR iPTMnet; Q9UTJ8; -.
DR MaxQB; Q9UTJ8; -.
DR PaxDb; Q9UTJ8; -.
DR PRIDE; Q9UTJ8; -.
DR EnsemblFungi; SPAC1556.01c.1; SPAC1556.01c.1:pep; SPAC1556.01c.
DR PomBase; SPAC1556.01c; rad50.
DR VEuPathDB; FungiDB:SPAC1556.01c; -.
DR eggNOG; KOG0962; Eukaryota.
DR HOGENOM; CLU_006184_0_0_1; -.
DR InParanoid; Q9UTJ8; -.
DR OMA; CFGVNCG; -.
DR PhylomeDB; Q9UTJ8; -.
DR Reactome; R-SPO-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-SPO-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-SPO-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SPO-5693607; Processing of DNA double-strand break ends.
DR PRO; PR:Q9UTJ8; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR GO; GO:0030870; C:Mre11 complex; IPI:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0045027; F:DNA end binding; EXP:PomBase.
DR GO; GO:0003678; F:DNA helicase activity; ISO:PomBase.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; ISO:PomBase.
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:0043047; F:single-stranded telomeric DNA binding; ISO:PomBase.
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:1990918; P:double-strand break repair involved in meiotic recombination; IMP:PomBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IC:PomBase.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:PomBase.
DR GO; GO:0007534; P:gene conversion at mating-type locus; IMP:PomBase.
DR GO; GO:1990898; P:meiotic DNA double-strand break clipping; IMP:PomBase.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:PomBase.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IMP:PomBase.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central.
DR GO; GO:0010520; P:regulation of reciprocal meiotic recombination; IMP:PomBase.
DR GO; GO:0031297; P:replication fork processing; IMP:PomBase.
DR GO; GO:0120290; P:stalled replication fork localization to nuclear periphery; IMP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IGI:PomBase.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:PomBase.
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 SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00606; rad50; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromosome; Coiled coil; DNA damage; DNA repair; Hydrolase;
KW Meiosis; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Zinc.
FT CHAIN 1..1285
FT /note="DNA repair protein rad50"
FT /id="PRO_0000138647"
FT DOMAIN 630..726
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT COILED 295..365
FT /evidence="ECO:0000255"
FT COILED 630..668
FT /evidence="ECO:0000255"
FT COILED 698..726
FT /evidence="ECO:0000255"
FT COILED 727..809
FT /evidence="ECO:0000255"
FT COILED 814..902
FT /evidence="ECO:0000255"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 674
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT BINDING 677
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 1285 AA; 149029 MW; DF45B2EAE7097295 CRC64;
MSCIDRMSIM GIRSFDNRSR ESIQFFSPLT LIVGQNGSGK TTIIECLKYA TTGILPPNTK
GGAFIHDPKI CGEKEVLAQV KLAFRNTNQV KMICTRSLQL SVKKTTRQQK TLDGQLLILK
DNERTTISNR CAELDSQVPL SLGVSKALLD YVIFCHQEES FWPLSEPANL KKRFDEIFES
LRYAKALDQI KGLKRDQETQ VKVDQATLTH YRSDKERAEK IELRVHESLK RISCIRSKVE
ELDQEITETA RLQDELFKST EEYEQQMITI RHLESQSDII NTTINDLKSQ MTITDESSED
LEKLHSNFAE KVKEEQELYK SLEKKRSDLE SLLKSRRELL EKLTGDLGKI QGEIESLEKL
KVKKSTMINE IVHRYNINEI NEEGIMTEVS KYASLVNKNY EISSGKLKER QVAVRARIEG
IKAHEMFLNN RVSEINSSLE KQLTTQKELR SRFEILFPVK LQREDFTKDV EKSDLWIKSL
RQEYESKNLL ELLDKHQTAL SSVENRLDEI SEIVDSYHKY SGVRTKLQVF EENKTNKSAI
LANQLMTLKS SFSEVMSYEL KDDDNYNEEL DKLVEDVRKK LQEKEEAESS LRSVRERLEI
RISLSVQSIN DLTENKKIKT KTLKSYSGTF ASMISEIKAL ESEIEENRKT LHSLQFGSTF
YEKAIEICVD QHACQLCQRS LDKEEEKLFV EHCHSMIDVI PSKSAEVYSH LETLTKTFKN
LSEAKPIFDE IELLDKRLSE TKTELSDLQG DLQGLDIRKD EIQSELDTLY LRRANLEKLQ
LLVKDISNLE EEIRTIDRET EVLRIELPSS IAHHNLDEIY AEREKLLEKR GYLRKQIERT
KLEETSFKKK IDDAVLANNE QKLKLTKLNF QVNELEQLEK DINKSSEDCD LQKKKLLEVS
SKQGSQAPFL NELESEYEKL EADIQEMAQK SRTEILEANE YLHQLNEWNS ELRIDVSTKF
KCIKEKKSNI GEEVRIIASK IESTDDNLRK LQERLADLRT RERNASDNLR LRALMRQLEE
AVTQKNYLLS QQSHDDRESF RERMQILKSK YGALNAERAG LLGECKQLEN SITKDKEELN
MEFKDADERF RRQLIKTKTT GKANEDLGKY AKALDVAIMQ LHSMKMNEIN RIVDELWKQT
YCGTDIDTIL IRSDSEGKGN RTYNYRVCMV KGDAELDMRG RCSAGQKVLA CIIIRLALAE
CLGVNCGILA LDEPTTNLDE ENICSLAKNL SRIVEFRRKQ ANFQLIVITH DEQFIRLVNS
DAYCSYYYRV KRDTNQKSMI VKEPL
