RAD32_SCHPO
ID RAD32_SCHPO Reviewed; 649 AA.
AC Q09683;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 167.
DE RecName: Full=DNA repair protein rad32;
GN Name=rad32; ORFNames=SPAC13C5.07;
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].
RC STRAIN=972 / ATCC 24843;
RX PubMed=7885834; DOI=10.1093/nar/23.3.383;
RA Tavassoli M., Shayeghi M., Nasim A., Watts F.Z.;
RT "Cloning and characterisation of the Schizosaccharomyces pombe rad32 gene:
RT a gene required for repair of double strand breaks and recombination.";
RL Nucleic Acids Res. 23:383-388(1995).
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: Required for the repair of double strand breaks (DSB) caused
CC by gamma and UV radiation. May work in conjunction with rhp51.
CC -!- SUBUNIT: Associates with nbn. Forms a multisubunit endonuclease
CC complex, MRN, together with nbn and rad50.
CC {ECO:0000269|PubMed:12944482}.
CC -!- INTERACTION:
CC Q09683; O43070: nbs1; NbExp=6; IntAct=EBI-2124866, EBI-2125045;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12944482}.
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000305}.
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DR EMBL; X82322; CAA57765.1; ALT_TERM; Genomic_DNA.
DR EMBL; CU329670; CAA90458.1; -; Genomic_DNA.
DR PIR; S58097; S58097.
DR RefSeq; NP_592935.1; NM_001018336.2.
DR PDB; 4FBK; X-ray; 2.38 A; A/B=15-413.
DR PDB; 4FBQ; X-ray; 2.50 A; A/B=15-413.
DR PDB; 4FBW; X-ray; 2.20 A; A/B=7-413.
DR PDB; 4FCX; X-ray; 3.00 A; A/B=15-413.
DR PDBsum; 4FBK; -.
DR PDBsum; 4FBQ; -.
DR PDBsum; 4FBW; -.
DR PDBsum; 4FCX; -.
DR AlphaFoldDB; Q09683; -.
DR SMR; Q09683; -.
DR BioGRID; 279207; 137.
DR DIP; DIP-52388N; -.
DR IntAct; Q09683; 2.
DR STRING; 4896.SPAC13C5.07.1; -.
DR MaxQB; Q09683; -.
DR PaxDb; Q09683; -.
DR PRIDE; Q09683; -.
DR EnsemblFungi; SPAC13C5.07.1; SPAC13C5.07.1:pep; SPAC13C5.07.
DR GeneID; 2542757; -.
DR KEGG; spo:SPAC13C5.07; -.
DR PomBase; SPAC13C5.07; -.
DR VEuPathDB; FungiDB:SPAC13C5.07; -.
DR eggNOG; KOG2310; Eukaryota.
DR HOGENOM; CLU_009535_3_0_1; -.
DR InParanoid; Q09683; -.
DR OMA; QWMRPET; -.
DR PhylomeDB; Q09683; -.
DR Reactome; R-SPO-1834949; Cytosolic sensors of pathogen-associated DNA.
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:Q09683; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0030870; C:Mre11 complex; IDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0045027; F:DNA end binding; ISO:PomBase.
DR GO; GO:0008311; F:double-stranded DNA 3'-5' exodeoxyribonuclease activity; ISO:PomBase.
DR GO; GO:0030145; F:manganese ion binding; IDA:PomBase.
DR GO; GO:0004518; F:nuclease activity; IDA:PomBase.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; ISO:PomBase.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; ISO:PomBase.
DR GO; GO:0000403; F:Y-form DNA binding; ISO:PomBase.
DR GO; GO:0000729; P:DNA double-strand break processing; IMP:PomBase.
DR GO; GO:0006302; P:double-strand break repair; IMP:PomBase.
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; IMP:PomBase.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; 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:0097552; P:mitochondrial double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IGI:PomBase.
DR CDD; cd00840; MPP_Mre11_N; 1.
DR DisProt; DP02842; -.
DR Gene3D; 3.30.110.110; -; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR IDEAL; IID50245; -.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR003701; Mre11.
DR InterPro; IPR038487; Mre11_capping_dom.
DR InterPro; IPR007281; Mre11_DNA-bd.
DR InterPro; IPR041796; Mre11_N.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF04152; Mre11_DNA_bind; 1.
DR PIRSF; PIRSF000882; DSB_repair_MRE11; 1.
DR SMART; SM01347; Mre11_DNA_bind; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR TIGRFAMs; TIGR00583; mre11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase;
KW Manganese; Meiosis; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..649
FT /note="DNA repair protein rad32"
FT /id="PRO_0000138683"
FT REGION 553..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:4FBW"
FT TURN 29..33
FT /evidence="ECO:0007829|PDB:4FBW"
FT TURN 35..39
FT /evidence="ECO:0007829|PDB:4FBW"
FT HELIX 40..54
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:4FBW"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:4FBW"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4FBW"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:4FBW"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:4FCX"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:4FBW"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:4FBW"
FT TURN 210..214
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:4FBW"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:4FBW"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:4FBW"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:4FBW"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:4FBW"
FT HELIX 332..358
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:4FBW"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:4FBW"
FT HELIX 389..394
FT /evidence="ECO:0007829|PDB:4FBW"
FT TURN 395..399
FT /evidence="ECO:0007829|PDB:4FBW"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:4FBW"
SQ SEQUENCE 649 AA; 73689 MW; 400B349EF4FA3428 CRC64;
MPNDPSDMNN ELHNENTIRI LISSDPHVGY GEKDPVRGND SFVSFNEILE IARERDVDMI
LLGGDIFHDN KPSRKALYQA LRSLRLNCLG DKPCELELLS DTSLTTGDTA VCNINYLDPN
INVAIPVFSI HGNHDDPSGD GRYSALDILQ VTGLVNYFGR VPENDNIVVS PILLQKGFTK
LALYGISNVR DERLYHSFRE NKVKFLRPDL YRDEWFNLLT VHQNHSAHTP TSYLPESFIQ
DFYDFVLWGH EHECLIDGSY NPTQKFTVVQ PGSTIATSLS PGETAPKHCG ILNITGKDFH
LEKIRLRTVR PFIMKDIILS EVSSIPPMVE NKKEVLTYLI SKVEEAITEA NAQWYEAQGT
VPVVENEKPP LPLIRLRVDY TGGYQTENPQ RFSNRFVGRV ANATDVVQFY LKKKYTRSKR
NDGLYTSAVE DIKINSLRVE SLVNEYLKTN RLECLPEDSL GEAVVNFVEK DDRDAIKECV
ETQLNKQINL LVKKRVTEEN LEQEISSIIN DLPKISTTKR KDYEELPEEV SETSINIAEH
TPVLKHTSSL LDHHSPLATS SSEHEMEATP SPALLKKTNK RRELPSSLTK KNTRTPQRSK
EVKKVPARKL SQSTKKSDKN TQSTLLFYDP SSTTEAQYLD NEDDEILDD
