ID M0I7F1_9EURY Unreviewed; 433 AA.
AC M0I7F1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA double-strand break repair protein Mre11 {ECO:0000256|HAMAP-Rule:MF_02044};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_02044};
GN Name=mre11 {ECO:0000256|HAMAP-Rule:MF_02044};
GN ORFNames=C441_10868 {ECO:0000313|EMBL:ELZ92716.1};
OS Haloferax sulfurifontis ATCC BAA-897.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=662480 {ECO:0000313|EMBL:ELZ92716.1, ECO:0000313|Proteomes:UP000011508};
RN [1] {ECO:0000313|EMBL:ELZ92716.1, ECO:0000313|Proteomes:UP000011508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-897 {ECO:0000313|EMBL:ELZ92716.1,
RC ECO:0000313|Proteomes:UP000011508};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Part of the Rad50/Mre11 complex, which is involved in the
CC early steps of DNA double-strand break (DSB) repair. Mre11 binds to DSB
CC ends and has both double-stranded 3'-5' exonuclease activity and
CC single-stranded endonuclease activity. {ECO:0000256|HAMAP-
CC Rule:MF_02044}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02044};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_02044};
CC -!- ACTIVITY REGULATION: Nuclease activity is regulated by Rad50.
CC {ECO:0000256|HAMAP-Rule:MF_02044}.
CC -!- SUBUNIT: Homodimer. Forms a heterotetramer composed of two Mre11
CC subunits and two Rad50 subunits. {ECO:0000256|HAMAP-Rule:MF_02044}.
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000256|HAMAP-
CC Rule:MF_02044}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELZ92716.1}.
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DR EMBL; AOLM01000019; ELZ92716.1; -; Genomic_DNA.
DR AlphaFoldDB; M0I7F1; -.
DR PATRIC; fig|662480.6.peg.2153; -.
DR Proteomes; UP000011508; Unassembled WGS sequence.
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 NCBIfam; NF041030; Mre11_Halo; 1.
DR PANTHER; PTHR30337; COMPONENT OF ATP-DEPENDENT DSDNA EXONUCLEASE; 1.
DR PANTHER; PTHR30337:SF0; NUCLEASE SBCCD SUBUNIT D; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_02044};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_02044}; Endonuclease {ECO:0000256|HAMAP-Rule:MF_02044};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_02044}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_02044};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_02044};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02044};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_02044}.
FT DOMAIN 2..182
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT REGION 356..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..413
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 6
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 47
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 47
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 147
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 178
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 180
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
SQ SEQUENCE 433 AA; 47647 MW; 659AFFB598F5D32D CRC64;
MIHTGDTHIG YQQYHSPERR QDFLDAFERV VADALDGDVD AVVHAGDLYH DRRPELPDLL
GTLAALRRLD DAGIPFLAIV GNHESTRGGQ WLDLFERLGL ATRLGRDPHV VGDVAFYGLD
HVPRSRRDEL DYQFEPHDAE RAVLVAHGLF TPFAHADWET ETVLAESNVD FDAVLLGDNH
VPDTADLDGT WVTYCGSTER ASATERDPRG YNLVEFAPDA VDIRRRTLET RPFAFVEVDL
AGDEGIERVR QRVREFDVED AVVIVELRGE GDAVTPAAVE SFAVEEGALV ARVNDKRDID
DDADLATDVT FADPDDAVRE RVREMGLSSA ALDVDETVRA SKVADSNVRD EVRERVESLL
SDDPDAFVAA ERETEGEDEG ENSETVEDVE AAEDATETDP ETTETDPETT ADTDSEAPAD
PAASRDSSLG DFA
//
