MRE11_PYRAB
ID MRE11_PYRAB Reviewed; 415 AA.
AC Q9UZC9; G8ZKL2;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 105.
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}; Synonyms=rad32;
GN OrderedLocusNames=PYRAB12190; ORFNames=PAB0811;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB50130.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ248286; CAB50130.1; ALT_INIT; Genomic_DNA.
DR EMBL; HE613800; CCE70655.1; -; Genomic_DNA.
DR PIR; E75103; E75103.
DR AlphaFoldDB; Q9UZC9; -.
DR SMR; Q9UZC9; -.
DR STRING; 272844.PAB0811; -.
DR EnsemblBacteria; CAB50130; CAB50130; PAB0811.
DR KEGG; pab:PAB0811; -.
DR PATRIC; fig|272844.11.peg.1299; -.
DR eggNOG; arCOG00397; Archaea.
DR HOGENOM; CLU_038682_0_0_2; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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..415
FT /note="DNA double-strand break repair protein Mre11"
FT /id="PRO_0000138695"
FT ACT_SITE 87
FT /note="Proton donor"
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 12
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 86
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 208
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 210
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
SQ SEQUENCE 415 AA; 48079 MW; B96DE08628464C32 CRC64;
MGIKFAHLAD VHLGYEQFNR SQRAEEFAKA FEDAIKICVD EKVDFIVIAG DLFNSSRPSP
GTIKTAVKIL QIPRDNNIPV FAIEGNHDRT QRGPSILHLL EDLGLLYVLG VRDEKVENEY
LTSEKTKAGW LVKGMYKDVE IHGMKYMSAA WFEGNIELFK SMFRPEGDAI LVLHQGVREI
TENNYPNYSS ELSLSDLPKG YLYYALGHIH KRFELTYDDA PVVYPGSLER WDFGDYSLKL
TWNGFQFKEE VGVDKGFYIV EDFKPRFIRI NARDFIDVHI KGHSENEIKK AVKLAVPKIP
RNSYVRFNIR WKRPVDVDWI KSIVNAEYVR VNPIIIKEER GPDGKDLDVK KFFTELEWKI
IELASEKEYE YYLNQIIDLL ASEEGKVEAK IDAKREEKKF VRPKNPGDIM AWVKG
