ID   MRE11_XENLA             Reviewed;         711 AA.
AC   Q9W6K1; Q2TAT5;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Double-strand break repair protein MRE11;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:P49959};
GN   Name=mre11;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bibikova M., Carroll D.;
RT   "The Mre11 homolog from Xenopus laevis.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; AF134569; AAD31866.1; -; mRNA.
DR   EMBL; BC110736; AAI10737.1; -; mRNA.
DR   RefSeq; NP_001080975.1; NM_001087506.1.
DR   AlphaFoldDB; Q9W6K1; -.
DR   SMR; Q9W6K1; -.
DR   BioGRID; 98910; 1.
DR   MaxQB; Q9W6K1; -.
DR   DNASU; 394308; -.
DR   GeneID; 394308; -.
DR   KEGG; xla:394308; -.
DR   CTD; 394308; -.
DR   Xenbase; XB-GENE-957959; mre11.L.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 394308; Expressed in testis and 19 other tissues.
DR   GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR   GO; GO:0005657; C:replication fork; ISS:UniProtKB.
DR   GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IEA:InterPro.
DR   GO; GO:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
DR   GO; GO:0004520; F:endodeoxyribonuclease activity; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0110025; P:DNA strand resection involved in replication fork processing; ISS:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase; Manganese;
KW   Meiosis; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..711
FT                   /note="Double-strand break repair protein MRE11"
FT                   /id="PRO_0000138677"
FT   REGION          510..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..567
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..610
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   711 AA;  81131 MW;  D0B2A5A4B271BE26 CRC64;
     MSSSSSSLDD EDTFKILVAT DIHLGFMEKD AVRGNDSFVA FDEILRLAQD NEVDFLLLGG
     DLFHDNKPSR RTLHICLEQL RKYCMGDRPI EFEVLSDQSV NFGYSKFPWV NYQDNNLNIS
     LPVFSVHGNH DDPTGADALC ALDILSSAGL VNHFGRATSV EKIDISPVLL QKGHSKIALY
     GLGSIPDERL YRMFVNKQVM MLRPREDESS WFNLFVIHQN RSKHGPTNYI PEQFLDEFLD
     LVIWGHEHEC KIAPTRNEQQ LFYVSQPGSS VATSLSPGEA EKKHVGLLRI KGKKMNMQKI
     PLQTVRQFFI EDLVLSDYPD IFNPDNPRVT QEIETFCIEK VEAMLDTAER ERLGNPRQPD
     KPLIRLRVDY TGGFEPFNTL RFSQKFVDRT ANPKDIIHFF RHKEQKDKKD SITINFGKID
     SKPLLEGTTL RVEDLVKEYF KTAEKNVQLS LLTERGMGEA VQEFVDKEEK DALEELVKFQ
     LEKTQRFLKE RHIDAEEEKI DEEVRKFRET RKTNTNEEDE EVREAIQRAR THRSQAPDVE
     MSDEDDDALL RKVSLSDDED VRASMPARGR GRGRARGGRG QSTTTRGTSR RGRGSASADQ
     PSSGRATKAT GKNMSILDAF KPSSRQPTAR NVAKKTYSED IEDDDSDLEE VSFTPSSVIE
     SRRTSSTSTS YSRKSTQPQS QATKAHFFDD DDDEEDFDPF KKSGPSRRGR R