ID   MRE11_METMA             Reviewed;         617 AA.
AC   Q8PUY5;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=DNA double-strand break repair protein Mre11 {ECO:0000255|HAMAP-Rule:MF_02044};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_02044};
GN   Name=mre11 {ECO:0000255|HAMAP-Rule:MF_02044}; OrderedLocusNames=MM_2193;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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:0000255|HAMAP-Rule:MF_02044}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02044};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_02044};
CC   -!- ACTIVITY REGULATION: Nuclease activity is regulated by Rad50.
CC       {ECO:0000255|HAMAP-Rule:MF_02044}.
CC   -!- SUBUNIT: Homodimer. Forms a heterotetramer composed of two Mre11
CC       subunits and two Rad50 subunits. {ECO:0000255|HAMAP-Rule:MF_02044}.
CC   -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000255|HAMAP-
CC       Rule:MF_02044}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE008384; AAM31889.1; -; Genomic_DNA.
DR   RefSeq; WP_011034124.1; NC_003901.1.
DR   AlphaFoldDB; Q8PUY5; -.
DR   SMR; Q8PUY5; -.
DR   STRING; 192952.MM_2193; -.
DR   EnsemblBacteria; AAM31889; AAM31889; MM_2193.
DR   GeneID; 1480535; -.
DR   KEGG; mma:MM_2193; -.
DR   PATRIC; fig|192952.21.peg.2511; -.
DR   eggNOG; arCOG00397; Archaea.
DR   HOGENOM; CLU_026621_3_1_2; -.
DR   OMA; DWDCAEV; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045027; F:DNA end binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000403; F:Y-form DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006302; P:double-strand break repair; IEA:UniProtKB-UniRule.
DR   CDD; cd00840; MPP_Mre11_N; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   HAMAP; MF_02044; Mre11; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR032885; Mre11_archaea-type.
DR   InterPro; IPR041796; Mre11_N.
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..617
FT                   /note="DNA double-strand break repair protein Mre11"
FT                   /id="PRO_0000138691"
FT   REGION          395..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..606
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        89
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         12
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         14
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         53
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         53
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         88
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         158
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         189
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         191
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
SQ   SEQUENCE   617 AA;  67781 MW;  68EC2721FD5E266F CRC64;
     MDREIRILHT ADTHLGYRQY HSEVRRQDFF KAFETVIKDA VDMQVDAVVH AGDLFDSRNP
     TLEDLLETMN VLSRLKVANI PFFGIVGNHE SKQSTQWLDL FEEMGLAGRL GKAPKMVGDV
     AIYGIDSVPK SKIPLFDYSG FEIPESLPEN CRKLLVMHQI MQPSPFPDWD CAEVIENLPF
     KADAVLLGDY HEYEKIKVGE SWVTYSGSTE RNSASEKEPR SYSIITLSGE GLEISRRTIP
     TRNFLFITAK VDGEEKPFEQ IFSTVNEHLE EIPESVVFLD VSGDSSSVLS FSEIEEYLLS
     KGALVVKVKD ARVKEGIPEE VIKVAFHDPD RAVAEELRRM SLNDGGLIVD EVIRSPDVPR
     SRVDEETENR LLGLIEAIDF KDPDFMIKIP VSHVSPVDPS SSVSSIESSG SVSPIDSVST
     VSPSSPSSSA IIKEPEELKP PGAAEEIENP KPAGVTEFTA AVAAKSETLM PPVRIQRSES
     LNESLNKIFE KHDVVPESPE TAGSIAGSVE TAVEDEISKV TPDSGVITAP QSSSPVSFSD
     NSQTGFSAIS PPESIPSPEI LKENSEADAD EKPVDGKLSE EKPVGVPDKA TKTVKQSHRK
     GKEKSAVPRQ YNLGDYL