MRE11_HALVD
ID MRE11_HALVD Reviewed; 441 AA.
AC D4GUK0; P62130;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=HVO_0853;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN POLYPLOID ORGANISMS, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=DS2 / DS70;
RX PubMed=19593371; DOI=10.1371/journal.pgen.1000552;
RA Delmas S., Shunburne L., Ngo H.P., Allers T.;
RT "Mre11-Rad50 promotes rapid repair of DNA damage in the polyploid archaeon
RT Haloferax volcanii by restraining homologous recombination.";
RL PLoS Genet. 5:E1000552-E1000552(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
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 (By similarity). In polyploid
CC organisms, the Rad50/Mre11 complex appears to restrain the repair of
CC double-strand breaks by homologous recombination, allowing another
CC pathway to act as the primary mode of repair (PubMed:19593371).
CC {ECO:0000255|HAMAP-Rule:MF_02044, ECO:0000269|PubMed:19593371}.
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 -!- DISRUPTION PHENOTYPE: Mutants are more resistant to DNA damage, but
CC recover more slowly than the wild-type. {ECO:0000269|PubMed:19593371}.
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000255|HAMAP-
CC Rule:MF_02044}.
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DR EMBL; AJ635369; CAG25774.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE04038.1; -; Genomic_DNA.
DR RefSeq; WP_013035492.1; NC_013967.1.
DR AlphaFoldDB; D4GUK0; -.
DR SMR; D4GUK0; -.
DR IntAct; D4GUK0; 6.
DR STRING; 309800.C498_14473; -.
DR EnsemblBacteria; ADE04038; ADE04038; HVO_0853.
DR GeneID; 8926365; -.
DR KEGG; hvo:HVO_0853; -.
DR eggNOG; arCOG00397; Archaea.
DR HOGENOM; CLU_026621_3_0_2; -.
DR OMA; PFAHADW; -.
DR Proteomes; UP000008243; 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; IPR024654; Calcineurin-like_PHP_lpxH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR032885; Mre11_archaea-type.
DR InterPro; IPR041796; Mre11_N.
DR Pfam; PF12850; Metallophos_2; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase; Manganese;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..441
FT /note="DNA double-strand break repair protein Mre11"
FT /id="PRO_0000410348"
FT REGION 360..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..401
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 86
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 9
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 150
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 181
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 183
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
SQ SEQUENCE 441 AA; 48175 MW; 4417A07DDC5A0419 CRC64;
MTRVIHTGDT HLGYQQYHSP ERRQDFLDAF ERVVADALDG DVDAVVHAGD LYHDRRPELP
DLLGTLAALR RLDDAGIPFL AIVGNHESTR GGQWLDLFER LGLATRLGRD PHVVGGVAFY
GLDHVPRSRR DELDYQFDPV DADRAVLVAH GLFTPFAHAD WETETVLAES NVDFDAVLLG
DNHVPDTAEL DGTWVTYCGS TERASASERD PRGYNLVEFT PDAVDIRRRT LETRPFAFVE
VDLAGDEGIE RVRQRVREFD LEDAVVIVEL RGEGETVTPA AVESFAVEEG ALVARVNDKR
DIDDDGDLAT DVTFADPDDA VRERVREMGL SSAALDVDET VRASKVADSN VRDEVRERVE
SLLSDDPDAF VAAERESDAE AEESESVEDA ADGEDAAAVE DTAETAAEAA TDTDTETTAD
TDSETAADPA ASRDSSLGDF A
