MRE11_YEAST
ID MRE11_YEAST Reviewed; 692 AA.
AC P32829; D6W049; P87289; Q07173;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Double-strand break repair protein MRE11;
GN Name=MRE11; OrderedLocusNames=YMR224C; ORFNames=YM9959.06C;
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] OF 1-643.
RX PubMed=7789757; DOI=10.1093/genetics/139.4.1521;
RA Johzuka K., Ogawa H.;
RT "Interaction of Mre11 and Rad50: two proteins required for DNA repair and
RT meiosis-specific double-strand break formation in Saccharomyces
RT cerevisiae.";
RL Genetics 139:1521-1532(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK1;
RA Nairz K., Klein F.;
RT "Recombination-dependent lethals in Yeast.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=7625279; DOI=10.1016/0065-227x(95)99383-z;
RA Ogawa H., Johzuka K., Nakagawa T., Leem S.H., Hagihara A.H.;
RT "Functions of the yeast meiotic recombination genes, MRE11 and MRE2.";
RL Adv. Biophys. 31:67-76(1995).
RN [6]
RP FUNCTION.
RX PubMed=9651580; DOI=10.1016/s1097-2765(00)80097-0;
RA Paull T.T., Gellert M.;
RT "The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA
RT double-strand breaks.";
RL Mol. Cell 1:969-979(1998).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in DNA double-strand break repair (DSBR). Possesses
CC single-strand endonuclease activity and double-strand-specific 3'-5'
CC exonuclease activity. Also involved in meiotic DSB processing.
CC {ECO:0000269|PubMed:7625279, ECO:0000269|PubMed:9651580}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Forms a complex with RAD50 and XRS2.
CC -!- INTERACTION:
CC P32829; P12753: RAD50; NbExp=21; IntAct=EBI-11255, EBI-14700;
CC P32829; P46946: SAE2; NbExp=2; IntAct=EBI-11255, EBI-16440;
CC P32829; P33301: XRS2; NbExp=19; IntAct=EBI-11255, EBI-20599;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 432 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000305}.
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DR EMBL; D11463; BAA02017.1; -; Genomic_DNA.
DR EMBL; Z49939; CAA90195.1; -; Genomic_DNA.
DR EMBL; U60829; AAB61454.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10123.1; -; Genomic_DNA.
DR PIR; S57592; S57592.
DR RefSeq; NP_013951.1; NM_001182731.1.
DR AlphaFoldDB; P32829; -.
DR SMR; P32829; -.
DR BioGRID; 35402; 591.
DR ComplexPortal; CPX-1872; MRE11-RAD50-XRS2 meiotic recombination initiation complex.
DR DIP; DIP-1313N; -.
DR IntAct; P32829; 12.
DR MINT; P32829; -.
DR STRING; 4932.YMR224C; -.
DR iPTMnet; P32829; -.
DR MaxQB; P32829; -.
DR PaxDb; P32829; -.
DR PRIDE; P32829; -.
DR EnsemblFungi; YMR224C_mRNA; YMR224C; YMR224C.
DR GeneID; 855264; -.
DR KEGG; sce:YMR224C; -.
DR SGD; S000004837; MRE11.
DR VEuPathDB; FungiDB:YMR224C; -.
DR eggNOG; KOG2310; Eukaryota.
DR GeneTree; ENSGT00390000017288; -.
DR HOGENOM; CLU_009535_3_0_1; -.
DR InParanoid; P32829; -.
DR OMA; SACNFVN; -.
DR BioCyc; YEAST:G3O-32905-MON; -.
DR Reactome; R-SCE-1834949; Cytosolic sensors of pathogen-associated DNA.
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:P32829; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P32829; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0030870; C:Mre11 complex; IDA:CACAO.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:SGD.
DR GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IMP:CACAO.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:SGD.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:SGD.
DR GO; GO:0004519; F:endonuclease activity; IDA:SGD.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IDA:SGD.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:SGD.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IBA:GO_Central.
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:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0006284; P:base-excision repair; IMP:SGD.
DR GO; GO:0010791; P:DNA double-strand break processing involved in repair via synthesis-dependent strand annealing; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:CACAO.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
DR GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IMP:SGD.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IBA:GO_Central.
DR GO; GO:0010780; P:meiotic DNA double-strand break formation involved in reciprocal meiotic recombination; IMP:CACAO.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; TAS:SGD.
DR GO; GO:0097552; P:mitochondrial double-strand break repair via homologous recombination; IMP:SGD.
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; IBA:GO_Central.
DR GO; GO:0046940; P:nucleoside monophosphate phosphorylation; IEA:GOC.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0051037; P:regulation of transcription involved in meiotic cell cycle; IMP:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR CDD; cd00840; MPP_Mre11_N; 1.
DR Gene3D; 3.30.110.110; -; 1.
DR Gene3D; 3.60.21.10; -; 1.
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 DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase; Manganese;
KW Meiosis; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..692
FT /note="Double-strand break repair protein MRE11"
FT /id="PRO_0000138680"
FT REGION 522..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT VARIANT 380
FT /note="P -> S (in strain: SK1)"
FT VARIANT 659
FT /note="P -> S (in strain: SK1)"
SQ SEQUENCE 692 AA; 77650 MW; D58433E32E852B73 CRC64;
MDYPDPDTIR ILITTDNHVG YNENDPITGD DSWKTFHEVM MLAKNNNVDM VVQSGDLFHV
NKPSKKSLYQ VLKTLRLCCM GDKPCELELL SDPSQVFHYD EFTNVNYEDP NFNISIPVFG
ISGNHDDASG DSLLCPMDIL HATGLINHFG KVIESDKIKV VPLLFQKGST KLALYGLAAV
RDERLFRTFK DGGVTFEVPT MREGEWFNLM CVHQNHTGHT NTAFLPEQFL PDFLDMVIWG
HEHECIPNLV HNPIKNFDVL QPGSSVATSL CEAEAQPKYV FILDIKYGEA PKMTPIPLET
IRTFKMKSIS LQDVPHLRPH DKDATSKYLI EQVEEMIRDA NEETKQKLAD DGEGDMVAEL
PKPLIRLRVD YSAPSNTQSP IDYQVENPRR FSNRFVGRVA NGNNVVQFYK KRSPVTRSKK
SGINGTSISD RDVEKLFSES GGELEVQTLV NDLLNKMQLS LLPEVGLNEA VKKFVDKDEK
TALKEFISHE ISNEVGILST NEEFLRTDDA EEMKALIKQV KRANSVRPTP PKENDETNFA
FNGNGLDSFR SSNREVRTGS PDITQSHVDN ESRITHISQA ESSKPTSKPK RVRTATKKKI
PAFSDSTVIS DAENELGDNN DAQDDVDIDE NDIIMVSTDE EDASYGLLNG RKTKTKTRPA
ASTKTASRRG KGRASRTPKT DILGSLLAKK RK
