MRE11_METAC
ID MRE11_METAC Reviewed; 614 AA.
AC Q8TRL2;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=MA_1163;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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; AE010299; AAM04584.1; -; Genomic_DNA.
DR RefSeq; WP_011021187.1; NC_003552.1.
DR AlphaFoldDB; Q8TRL2; -.
DR SMR; Q8TRL2; -.
DR STRING; 188937.MA_1163; -.
DR EnsemblBacteria; AAM04584; AAM04584; MA_1163.
DR GeneID; 1473051; -.
DR KEGG; mac:MA_1163; -.
DR HOGENOM; CLU_026621_3_1_2; -.
DR InParanoid; Q8TRL2; -.
DR OMA; DWDCAEV; -.
DR OrthoDB; 9329at2157; -.
DR PhylomeDB; Q8TRL2; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
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:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IBA:GO_Central.
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..614
FT /note="DNA double-strand break repair protein Mre11"
FT /id="PRO_0000138688"
FT REGION 393..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 89
FT /note="Proton donor"
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 14
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 53
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 53
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 88
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 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 614 AA; 68374 MW; 786CBB85FD68CD56 CRC64;
MDREIRILHT ADTHLGYRQY HSEVRRQDFF KAFETVIQDA VDMQVDAVVH AGDLFDSRNP
TLEDLLETMN ILSRLKAVDI PFFGIVGNHE SKQNTQWLDL FEEMGLAERL GKTPKLVGNT
TIYGIDSVPK SKIPLYDYSG FELPDSLPEN CKKLLVMHQI VQPFPYADWD CAEVLENLPF
KVDAILLGDY HKYEKIKVGE EETWATYSGS TERNSASENE PRSYNIITLS GEGLEISRRT
IPTRNFLFIT AKIDGEEKPY EQIFSAINEH LEEIPESVVF LDISGNSDSV LSFSEIEEYL
LSKGALVSKV KDARIKETLP EEVAKVAFSD PDHAVAEEIR RMSLNDGGLI VDEIIRSPDV
VRSRVDEETE NRLLRLIETI DFEDPDFRIE IPASPISSTD SIDPVSPINH PVSSADSVSA
VSPESSADHV SPDIIENNEK PIPAVEAEKI ETLDPAGETE FVAGIAGKTE TFRAPVRIKN
SESLNEALKK SYEAPDKVRE APDVNPEPPE PLPAFKNIGS PETFGSCETT VSSEVPEKGG
ERTELEDDAV NKTEKETGKL SGFGVEAGSE KEDADRIEKP AHVPDKAEKP VKQSQRKGKG
KSAVPRQYNL GDYL
