ID   MRE11_ENCCU             Reviewed;         567 AA.
AC   Q8SRV0;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Double-strand break repair protein MRE11;
GN   Name=MRE11; OrderedLocusNames=ECU05_1280;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Forms a complex with RAD50. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000305}.
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DR   EMBL; AL590445; CAD26648.1; -; Genomic_DNA.
DR   RefSeq; NP_597471.1; NM_001041337.1.
DR   AlphaFoldDB; Q8SRV0; -.
DR   SMR; Q8SRV0; -.
DR   STRING; 284813.Q8SRV0; -.
DR   GeneID; 859137; -.
DR   KEGG; ecu:ECU05_1280; -.
DR   VEuPathDB; MicrosporidiaDB:ECU05_1280; -.
DR   HOGENOM; CLU_009535_3_4_1; -.
DR   InParanoid; Q8SRV0; -.
DR   OMA; SACNFVN; -.
DR   OrthoDB; 834694at2759; -.
DR   Proteomes; UP000000819; Chromosome V.
DR   GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR   GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IEA:InterPro.
DR   GO; GO:0004520; F:endodeoxyribonuclease activity; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   CDD; cd00840; MPP_Mre11_N; 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; 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.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase; Manganese;
KW   Meiosis; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..567
FT                   /note="Double-strand break repair protein MRE11"
FT                   /id="PRO_0000381757"
FT   REGION          513..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        105
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   567 AA;  65003 MW;  091FC7D9E64611E4 CRC64;
     MKILITSDNH LGYRESDPVL LDDSYDTFEE ILGIAQRERV DLVLQGGDLF HENRPSRSCL
     NRTIGLFRRY CIGNERSGLR SNLALNFHDQ NIGISIPVVS IHGNHDDPSG ISMVSPIDIL
     QSAGLVNYIG KYNLIDRIDV YPLLLEKEYR VAIYGLGHIK DRRLYRMFCE GRIVFHRPED
     YDSWYNVLIL HQNRIPREKE HFSSDLVEGF FDLIVYGHEH ESMVVKGDCL ILQPGSTVRT
     SLCEGERHDK YAYILRIGEE CTLEHVKLRS VRPLLLDTLR IEERDNVEEK VENKIRGMID
     LGRKKESLFN KEITAIDVDT KRFKCRGDSN EACGAGPVCK GYQLEEKTRI PLVKLKIELC
     GDEVLDKHRF SAQFKGLVAN PSDMLTISRK TRRREEVETQ PMAERVEISQ ILRKILGNVE
     FGVLSRLGFS ESLDEFVKGD SNAFMGMVRK NIEKVVNAVD HSSIVDEDVI KAMKRASREE
     DRGYEEDHFE PRAALGVLDE MDPGLANKNL RNEYSSRLGG NSEENESKAK KNFNVEDLLG
     KEYLSKKLRK DKEDSSTDVS FTFSKYL