ID   MRE11_NANEQ             Reviewed;         361 AA.
AC   P62132;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=DNA double-strand break repair protein Mre11 {ECO:0000250|UniProtKB:Q8U1N9};
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q8U1N9};
GN   Name=mre11 {ECO:0000250|UniProtKB:Q8U1N9}; OrderedLocusNames=NEQ383;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
CC   -!- FUNCTION: Part of the Rad50/Mre11 complex, which is involved in the
CC       early steps of DNA double-strand break (DSB) repair. The complex may
CC       facilitate opening of the processed DNA ends to aid in the recruitment
CC       of HerA and NurA. Mre11 binds to DSB ends and has both double-stranded
CC       3'-5' exonuclease activity and single-stranded endonuclease activity.
CC       {ECO:0000250|UniProtKB:Q8U1N9}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q8U1N9};
CC       Note=Binds 2 manganese ions per subunit.
CC       {ECO:0000250|UniProtKB:Q8U1N9};
CC   -!- ACTIVITY REGULATION: Nuclease activity is regulated by Rad50.
CC       {ECO:0000250|UniProtKB:Q8U1N9}.
CC   -!- SUBUNIT: Homodimer. Forms a heterotetramer composed of two Mre11
CC       subunits and two Rad50 subunits. {ECO:0000250|UniProtKB:Q8U1N9}.
CC   -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000305}.
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DR   EMBL; AE017199; AAR39230.1; -; Genomic_DNA.
DR   AlphaFoldDB; P62132; -.
DR   SMR; P62132; -.
DR   STRING; 228908.NEQ383; -.
DR   PRIDE; P62132; -.
DR   EnsemblBacteria; AAR39230; AAR39230; NEQ383.
DR   KEGG; neq:NEQ383; -.
DR   HOGENOM; CLU_060534_0_0_2; -.
DR   Proteomes; UP000000578; Chromosome.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase; Manganese;
KW   Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..361
FT                   /note="DNA double-strand break repair protein Mre11"
FT                   /id="PRO_0000138694"
FT   ACT_SITE        84
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT   BINDING         7
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT   BINDING         9
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT   BINDING         48
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT   BINDING         48
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT   BINDING         83
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT   BINDING         176
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT   BINDING         204
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT   BINDING         206
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1N9"
SQ   SEQUENCE   361 AA;  42565 MW;  BFAB206A0FE3C6B1 CRC64;
     MIAFISDLHL GNIYANKKET EEHSYNALAK IEEKLLEYQP DLVLVGGDIF DKNKVSGKEI
     GVFIDFINKM NKNNIGVVSI SGNHDGKYWL KESFDHAIPY ILYKSGINPE NGYEYYSFAG
     IYLKNSRDWK TLSMIEDKYD ISIVGFSFYT KDRLPELYEY LSIIDREKSD YILLMHQSLK
     SLLPQDPAAI DLTIENYKYA LFGHMHMKYY KDKIIVTPPP YSISLKEANT EKGFWLIDKK
     PVFVPIEDSR PFIKMAIDLD NPIEIKPNKN AILILDVYYR ESQIDKLNLL KKTLSENFLY
     VKINPILKET SKIIVKKSEN KEEIFKKYLK EDYDFFMELY EKFRDIKDPE TIVQYLEFFY
     R