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MRE11_THEAC
ID   MRE11_THEAC             Reviewed;         376 AA.
AC   Q9HLR7;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=Ta0158;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(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; AL445063; CAC11305.1; -; Genomic_DNA.
DR   RefSeq; WP_010900585.1; NC_002578.1.
DR   AlphaFoldDB; Q9HLR7; -.
DR   SMR; Q9HLR7; -.
DR   STRING; 273075.Ta0158; -.
DR   EnsemblBacteria; CAC11305; CAC11305; CAC11305.
DR   GeneID; 1455805; -.
DR   KEGG; tac:Ta0158; -.
DR   eggNOG; arCOG00397; Archaea.
DR   HOGENOM; CLU_026621_5_2_2; -.
DR   OMA; YRQYNLD; -.
DR   OrthoDB; 25870at2157; -.
DR   Proteomes; UP000001024; 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; Reference proteome.
FT   CHAIN           1..376
FT                   /note="DNA double-strand break repair protein Mre11"
FT                   /id="PRO_0000138701"
FT   ACT_SITE        82
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         5
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         7
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         46
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         46
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         81
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         159
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="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT   BINDING         191
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
SQ   SEQUENCE   376 AA;  43330 MW;  9C9575D790D2475E CRC64;
     MHFSDTHIGY RSLTLDEREQ DFYDAFHEAI DIALENSVDF VIHTGDLFDT WVPGNRAIRE
     FRNAVMKLNA RNIPIFVIFG DHDRPRRNGE PAAGIFDFMG VHVLGWDAYE YAVRKFDGED
     VLIGGISNMK GYMKTRLKDE YKRSENIEEG YRNRILMSHQ AIDPFFVPDQ CEAKMDDLPM
     NFSYIAMGHL HDFMERRIGP LISYAGSTEI KSENEINGYL KQGKGVNIVD ISNGEVDLQR
     IRLKSVRPQI RVESDADNYV HEISEKLSSL RVKDNEKKPL VGLEIHGDIS METVMQDISK
     FDNAIFSRPK IRKDPKIPNI HTETADLREY FRAYLGDERL ADLAMKIMAH SRSKDIDGIM
     KEIEVLYGDN RQDSPD
 
 
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