MRE11_HALSA
ID MRE11_HALSA Reviewed; 387 AA.
AC Q9HRW4;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=VNG_0512G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=18502851; DOI=10.1128/jb.00292-08;
RA Kish A., DiRuggiero J.;
RT "Rad50 is not essential for the Mre11-dependent repair of DNA double-strand
RT breaks in Halobacterium sp. strain NRC-1.";
RL J. Bacteriol. 190:5210-5216(2008).
CC -!- FUNCTION: Part of the Rad50/Mre11 complex, which is involved in the
CC early steps of DNA double-strand break (DSB) repair. Mre11 binds to DSB
CC ends and has both double-stranded 3'-5' exonuclease activity and
CC single-stranded endonuclease activity. {ECO:0000255|HAMAP-
CC 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 -!- DISRUPTION PHENOTYPE: Mutants show a slight growth defect, but do not
CC show increased sensitivity to ionizing radiation or alkylating agents.
CC Show decreased rates of survival after UV-C irradiation. Display
CC extensive delay in the repair of DNA double-strand breaks.
CC {ECO:0000269|PubMed:18502851}.
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000255|HAMAP-
CC Rule:MF_02044}.
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DR EMBL; AE004437; AAG19044.1; -; Genomic_DNA.
DR PIR; H84209; H84209.
DR RefSeq; WP_010902340.1; NC_002607.1.
DR AlphaFoldDB; Q9HRW4; -.
DR SMR; Q9HRW4; -.
DR STRING; 64091.VNG_0512G; -.
DR PaxDb; Q9HRW4; -.
DR EnsemblBacteria; AAG19044; AAG19044; VNG_0512G.
DR GeneID; 5952568; -.
DR KEGG; hal:VNG_0512G; -.
DR PATRIC; fig|64091.14.peg.391; -.
DR HOGENOM; CLU_026621_3_0_2; -.
DR InParanoid; Q9HRW4; -.
DR OMA; PFAHADW; -.
DR OrthoDB; 25870at2157; -.
DR PhylomeDB; Q9HRW4; -.
DR Proteomes; UP000000554; 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..387
FT /note="DNA double-strand break repair protein Mre11"
FT /id="PRO_0000138686"
FT REGION 365..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 86
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 9
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 150
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 181
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 183
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
SQ SEQUENCE 387 AA; 42685 MW; 05194AF87D45C7E2 CRC64;
MARVIHTGDT HLGYQQYHAP QRRQDFLDAF DAVITDAIDE GVDAVVHAGD LYHDRQPGLR
DILDTIALLR PLQDADIPFL AVVGNHEGTR DAQWLDLFET LGLAERLDDS PRVVADTAFY
GLDYVPQSKR DDHDYTVADH DADHAALVSH GLFTPFPYAN WDLDAVLADA TVEFDAVLLG
DNHTPDTAQL GDTWVTYCGS TERASASERD PRGYNIVSFS SDATTDVAIS RKSLNTREFV
FVDADLGPTD GTAFIQERLR ERALDDAVVV VTITGDGDTV TPAEIERFGD DRGALLTRVN
DRREFDTGDD APDVDVSFAD PDDAVEQRVR DLGLDEPARD VDRIVRDDTL ADAAVRERVI
QRAEAVLDDD ADAADDDGRP TTVEEFQ
