MRE11_SULAC
ID MRE11_SULAC Reviewed; 382 AA.
AC Q8NKQ0; Q4JCJ7;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, 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=Saci_0052;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=12052775; DOI=10.1093/embo-reports/kvf112;
RA Constantinesco F., Forterre P., Elie C.;
RT "NurA, a novel 5'-3' nuclease gene linked to rad50 and mre11 homologs of
RT thermophilic Archaea.";
RL EMBO Rep. 3:537-542(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [3]
RP FUNCTION IN DNA REPAIR, AND INTERACTION WITH RAD50 AND HERA.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=18294364; DOI=10.1186/1471-2199-9-25;
RA Quaiser A., Constantinesco F., White M.F., Forterre P., Elie C.;
RT "The Mre11 protein interacts with both Rad50 and the HerA bipolar helicase
RT and is recruited to DNA following gamma irradiation in the archaeon
RT Sulfolobus acidocaldarius.";
RL BMC Mol. Biol. 9:25-25(2008).
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 (By similarity). Recruited immediately to chromosomal DNA after gamma
CC irradiation, and remains DNA bound in the course of DNA repair
CC (PubMed:18294364). {ECO:0000255|HAMAP-Rule:MF_02044,
CC ECO:0000269|PubMed:18294364}.
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 (By similarity). Interacts with Rad50
CC and HerA (PubMed:18294364). {ECO:0000255|HAMAP-Rule:MF_02044,
CC ECO:0000269|PubMed:18294364}.
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000255|HAMAP-
CC Rule:MF_02044}.
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DR EMBL; AJ437617; CAD26844.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY79482.1; -; Genomic_DNA.
DR RefSeq; WP_011276983.1; NC_007181.1.
DR AlphaFoldDB; Q8NKQ0; -.
DR SMR; Q8NKQ0; -.
DR STRING; 330779.Saci_0052; -.
DR EnsemblBacteria; AAY79482; AAY79482; Saci_0052.
DR GeneID; 3472967; -.
DR KEGG; sai:Saci_0052; -.
DR PATRIC; fig|330779.12.peg.49; -.
DR eggNOG; arCOG00397; Archaea.
DR HOGENOM; CLU_026621_5_2_2; -.
DR OMA; YRQYNLD; -.
DR Proteomes; UP000001018; 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 1: Evidence at protein level;
KW DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase; Manganese;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..382
FT /note="DNA double-strand break repair protein Mre11"
FT /id="PRO_0000138698"
FT ACT_SITE 85
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 49
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 49
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 84
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 156
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 187
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="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
SQ SEQUENCE 382 AA; 44157 MW; 561035790C1AEF60 CRC64;
MQLLHISDTH LGKRQYNLES REKDVYDTFT QLIDIAINEH VKAVIHTGDL FDVNNPPNRA
KLHAIKELKR LKDHNIPFIC IAGDHDSPKR KEEIYPQRIL EEFNLIKILQ KIDNRVKLEN
VEVYGISHIS NVSVNDLKEQ LSKVKPETRK SILMLHQGIR TYLPYQGAWQ IELSDLPKGF
SLYAVGHLHS RRKDYLDGGA LIEIAGSPDI MREEEIEDYQ KSKKGATLID MSGDLPSINY
INVNIRDQLV LDINVDKIEQ SIESVIQKLK ENVKNDKKPI LHIELEGTVP IRKDVLMTKL
QALRDYVEHY RIYKNNIVSI KEENLKTKLK TTYSSLNDII ADYLKGIGYT DEETKIIIDI
INEEDEKKVE ELLKKFAGVE DK
