ID H3ZM37_THELN Unreviewed; 439 AA.
AC H3ZM37;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=OCC_06831 {ECO:0000313|EMBL:EHR78981.1};
OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523849 {ECO:0000313|EMBL:EHR78981.1, ECO:0000313|Proteomes:UP000015502};
RN [1] {ECO:0000313|EMBL:EHR78981.1, ECO:0000313|Proteomes:UP000015502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
RC {ECO:0000313|Proteomes:UP000015502};
RX PubMed=22493191; DOI=10.1128/JB.00123-12;
RA Gardner A.F., Kumar S., Perler F.B.;
RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT litoralis NS-C.";
RL J. Bacteriol. 194:2375-2376(2012).
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:0000256|HAMAP-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02044}.
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DR EMBL; CP006670; EHR78981.1; -; Genomic_DNA.
DR RefSeq; WP_004067688.1; NC_022084.1.
DR AlphaFoldDB; H3ZM37; -.
DR STRING; 523849.OCC_06831; -.
DR PaxDb; 523849-OCC_06831; -.
DR GeneID; 16549252; -.
DR KEGG; tlt:OCC_06831; -.
DR HOGENOM; CLU_026621_5_1_2; -.
DR OrthoDB; 11638at2157; -.
DR Proteomes; UP000015502; 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 Gene3D; 3.30.110.80; DNA double-strand break repair nuclease; 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; NF041029; Mre11_Pyroc; 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 3..216
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT REGION 389..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 12
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 86
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 176
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
FT BINDING 215
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02044"
SQ SEQUENCE 439 AA; 51279 MW; F32CB2D0486EB344 CRC64;
MTFKFAHIAD VHLGFEQYRL PYRAEEFRVT FETAIKKAVE EKVDFILIAG DLFHRSNPSP
QTIKEAIDIL SIPKEEGIPV FAIEGNHDRT QKRISAYNLL ESLGLMYVLG FSEEKKENTY
QTTEKVNGKL IVKGVFEKGN KSLEIYGMKF MSAAWFERNK LSEYFKPSGD AVLMLHQGIK
EMMDSLKLET QRDYFEITLE DLPEGFLYYA MGHIHKRWQT NKGLGVVAYP GSLERWDFGD
YEMRYRWNGN AFIPQTGEDK GFLIVEDFKP RFVKLDVRPF YDVKIKADES VVKTELKKLS
TKIPKEAFLR VDIEWERPFD VSFLHEIFKV EYLHIRTKFK RPSIGKGKET NLKGFFTPLE
LKILELVGEK DFEDFEEVIE LLLKGSAPEK EATPKKEERK EEVKEEIKEE KPNLEAEKKI
KKIKEPPKKK SDLLSWLKG
//
