MRE11_METJA
ID MRE11_METJA Reviewed; 366 AA.
AC Q58719;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=MJ1323;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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 -!- INTERACTION:
CC Q58719; Q58719: mre11; NbExp=3; IntAct=EBI-10107692, EBI-10107692;
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000255|HAMAP-
CC Rule:MF_02044}.
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DR EMBL; L77117; AAB99332.1; -; Genomic_DNA.
DR PIR; B64465; B64465.
DR RefSeq; WP_010870840.1; NC_000909.1.
DR PDB; 3AUZ; X-ray; 3.21 A; A=1-313.
DR PDB; 3AV0; X-ray; 3.10 A; A=1-366.
DR PDB; 4TUG; X-ray; 3.55 A; A/B/C/D/E/F=1-333.
DR PDB; 4TUI; X-ray; 3.59 A; A/B/C/D/E/F=1-333.
DR PDB; 5DNY; X-ray; 3.11 A; A/C=1-366.
DR PDB; 5F3W; X-ray; 3.11 A; A/C=1-366.
DR PDBsum; 3AUZ; -.
DR PDBsum; 3AV0; -.
DR PDBsum; 4TUG; -.
DR PDBsum; 4TUI; -.
DR PDBsum; 5DNY; -.
DR PDBsum; 5F3W; -.
DR AlphaFoldDB; Q58719; -.
DR SMR; Q58719; -.
DR MINT; Q58719; -.
DR STRING; 243232.MJ_1323; -.
DR EnsemblBacteria; AAB99332; AAB99332; MJ_1323.
DR GeneID; 1452225; -.
DR KEGG; mja:MJ_1323; -.
DR eggNOG; arCOG00397; Archaea.
DR HOGENOM; CLU_026621_5_2_2; -.
DR InParanoid; Q58719; -.
DR OMA; YRQYNLD; -.
DR OrthoDB; 25870at2157; -.
DR PhylomeDB; Q58719; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0045027; F:DNA end binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004529; F:exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0006281; P:DNA repair; IBA:GO_Central.
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 3D-structure; DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase;
KW Manganese; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..366
FT /note="DNA double-strand break repair protein Mre11"
FT /id="PRO_0000138689"
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 158
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 186
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 188
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 19..37
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 58..73
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:5DNY"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:3AV0"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:5DNY"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:5DNY"
FT HELIX 133..148
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:3AV0"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:3AV0"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:3AV0"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:3AV0"
FT STRAND 296..303
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 336..347
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 352..362
FT /evidence="ECO:0007829|PDB:3AV0"
SQ SEQUENCE 366 AA; 43132 MW; EFF6ADAD43EB5AFC CRC64;
MMFVHIADNH LGYRQYNLDD REKDIYDSFK LCIKKILEIK PDVVLHSGDL FNDLRPPVKA
LRIAMQAFKK LHENNIKVYI VAGNHEMPRR LGEESPLALL KDYVKILDGK DVINVNGEEI
FICGTYYHKK SKREEMLDKL KNFESEAKNY KKKILMLHQG INPYIPLDYE LEHFDLPKFS
YYALGHIHKR ILERFNDGIL AYSGSTEIIY RNEYEDYKKE GKGFYLVDFS GNDLDISDIE
KIDIECREFV EVNIKDKKSF NEAVNKIERC KNKPVVFGKI KREFKPWFDT LKDKILINKA
IIVDDEFIDM PDNVDIESLN IKELLVDYAN RQGIDGDLVL SLYKALLNNE NWKELLDEYY
NTKFRG
