MRE11_THEVO
ID MRE11_THEVO Reviewed; 374 AA.
AC Q97C75;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=TV0229;
GN ORFNames=TVG0238008;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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}.
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DR EMBL; BA000011; BAB59371.1; -; Genomic_DNA.
DR AlphaFoldDB; Q97C75; -.
DR SMR; Q97C75; -.
DR STRING; 273116.14324443; -.
DR DNASU; 1440744; -.
DR EnsemblBacteria; BAB59371; BAB59371; BAB59371.
DR KEGG; tvo:TVG0238008; -.
DR eggNOG; arCOG00397; Archaea.
DR HOGENOM; CLU_026621_5_2_2; -.
DR OMA; HDFSYVR; -.
DR PhylomeDB; Q97C75; -.
DR Proteomes; UP000001017; 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.
FT CHAIN 1..374
FT /note="DNA double-strand break repair protein Mre11"
FT /id="PRO_0000138702"
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 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
SQ SEQUENCE 374 AA; 42598 MW; 5AFE7C2084D9143E CRC64;
MVRFLHMSDT HIGAKSLTIE EREQDYYDTF QEAVEIAIDE KVDFIIHSGD LFDTWIPGNR
SMKVFRDAMM KLNDRQIPVF YVFGDHDRPR RNSESAAGIF DFLGLHILGR DEFAGIEREF
SGMKVFIGGI SNMKGYLRNQ LKEEYKKAES ASTGYKNSIL ISHQALDPIF IPEQCEAKVN
DLPMNYSYIA MGHLHDFVER EIGPLLSYPG STELKSDREI NGLLKMGKGI NVIDLDNGVA
SLHRVKLKKV RYQFKVESDP ENYLEEIKSI LDKYANAIGE KKPIVNLIIN GQISMEEVYE
DLKKINGAIF NRPQILKIVD MPNVPSGSSE LREYFQAFLK DQKLTDLAMK VFQHTADGDK
EAIIREAAGE AIDN
