MRE11_SULTO
ID MRE11_SULTO Reviewed; 387 AA.
AC Q96YR6;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=STK_21070;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP INTERACTION WITH HERA.
RX PubMed=18243819; DOI=10.1016/j.dnarep.2007.10.010;
RA Zhang S., Wei T., Hou G., Zhang C., Liang P., Ni J., Sheng D., Shen Y.;
RT "Archaeal DNA helicase HerA interacts with Mre11 homologue and unwinds
RT blunt-ended double-stranded DNA and recombination intermediates.";
RL DNA Repair 7:380-391(2008).
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 (By similarity). Interacts with HerA
CC (PubMed:18243819). {ECO:0000255|HAMAP-Rule:MF_02044,
CC ECO:0000269|PubMed:18243819}.
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000255|HAMAP-
CC Rule:MF_02044}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000023; BAB67211.1; -; Genomic_DNA.
DR RefSeq; WP_010980186.1; NC_003106.2.
DR AlphaFoldDB; Q96YR6; -.
DR SMR; Q96YR6; -.
DR STRING; 273063.STK_21070; -.
DR PRIDE; Q96YR6; -.
DR EnsemblBacteria; BAB67211; BAB67211; STK_21070.
DR GeneID; 1460179; -.
DR KEGG; sto:STK_21070; -.
DR PATRIC; fig|273063.9.peg.2399; -.
DR eggNOG; arCOG00397; Archaea.
DR OMA; YRQYNLD; -.
DR OrthoDB; 25870at2157; -.
DR Proteomes; UP000001015; 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 1: Evidence at protein level;
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_0000138700"
FT ACT_SITE 88
FT /note="Proton donor"
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 13
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 52
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 52
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 87
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 190
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02044"
FT BINDING 192
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; 44979 MW; 3B1AB914C7154EFA CRC64;
MSKTQILHIS DTHLGKRQYN LDFREQDVYD TFSQLIDIAI KEHVDGIIHT GDLFDINDPP
NKAEIVAIRE LKRLKEAGIP FIVIAGDHDS PKKFTAIYPQ KILEEFDLIK FLSKPDTPYK
LGEITIYGIS HVPNVAKERL KELLSRLKPE NKKSILLLHQ GLKEVLPYEG AWQIQIDDLP
KAFSYYALGH FHTRRVFQLD GGRIIEIAGS PDILREEEIE GYEKEGKGAT LIDFSGDIPT
IQKINIDVRK QYVVTLNTNN LREEIRKLRE KYDTNNEKKP IFHIILEGKS IPKNVLMKEL
QEINNFAPYW RIYKDNTKEK DEKDVKIDLP TDTTIENLIY NYLVKIANFS ETEARMIVDI
INRADEREYV KEELMKMIGV ENDNKKN
