(data stored in ACNUC7421 zone)

SWISSPROT: C4KJI0_SULIK

ID   C4KJI0_SULIK            Unreviewed;       382 AA.
AC   C4KJI0;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 43.
DE   RecName: Full=DNA double-strand break repair protein Mre11 {ECO:0000256|HAMAP-Rule:MF_02044};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_02044};
GN   Name=mre11 {ECO:0000256|HAMAP-Rule:MF_02044};
GN   OrderedLocusNames=M164_0064 {ECO:0000313|EMBL:ACR40700.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR40700.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR40700.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Part of the Rad50/Mre11 complex, which is involved in
CC       the early steps of DNA double-strand break (DSB) repair. The
CC       complex may facilitate opening of the processed DNA ends to aid in
CC       the recruitment of HerA and NurA. Mre11 binds to DSB ends and has
CC       both double-stranded 3'-5' exonuclease activity and single-
CC       stranded endonuclease activity. {ECO:0000256|HAMAP-Rule:MF_02044}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02044};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_02044};
CC   -!- ENZYME REGULATION: Nuclease activity is regulated by Rad50.
CC       {ECO:0000256|HAMAP-Rule:MF_02044}.
CC   -!- SUBUNIT: Homodimer. Forms a heterotetramer composed of two Mre11
CC       subunits and two Rad50 subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_02044}.
CC   -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000256|HAMAP-
CC       Rule:MF_02044}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02044}.
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DR   EMBL; CP001402; ACR40700.1; -; Genomic_DNA.
DR   ProteinModelPortal; C4KJI0; -.
DR   EnsemblBacteria; ACR40700; ACR40700; M164_0064.
DR   KEGG; sid:M164_0064; -.
DR   HOGENOM; HOG000270625; -.
DR   OMA; GYRQYNL; -.
DR   OrthoDB; POG093Z03IE; -.
DR   BioCyc; SISL426118:GI01-64-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0045027; F:DNA end binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000403; F:Y-form DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006302; P:double-strand break repair; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.60.21.10; -; 2.
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   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KJI0.
DR   SWISS-2DPAGE; C4KJI0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_02044};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_02044};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_02044};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_02044};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02044};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_02044};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02044};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_02044}.
FT   DOMAIN        4    190       Metallophos. {ECO:0000259|Pfam:PF00149}.
FT   ACT_SITE     87     87       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_02044}.
FT   METAL        10     10       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02044}.
FT   METAL        12     12       Manganese 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02044}.
FT   METAL        51     51       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02044}.
FT   METAL        51     51       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02044}.
FT   METAL        86     86       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02044}.
FT   METAL       157    157       Manganese 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02044}.
FT   METAL       188    188       Manganese 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02044}.
FT   METAL       190    190       Manganese 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02044}.
SQ   SEQUENCE   382 AA;  43661 MW;  F24622308F962506 CRC64;
     MMVQILHISD THLGKRQYSL AEREKDIYDV FSQLIDIAIK ERVDAVIHSG DLFDVSNPTT
     NALVIAVKIL KKLKDANIPF LSIPGDHDTP KRKGYIIPHN ILTELDLIKI LNYDKPYIIK
     DIEIYGIPHI PTVSKNVLVS TLSSLKPKSS RSILLLHQGV KQILPYDGSW QMELGSLPKG
     FGYYALGHLH TRWRLIQDDG SIIAIAGSPD IMREEEIEGY EKFGKGAYLI DFSKDLPTLT
     TINTTVRPQK VVTINTKNLK NDISKIKSDL LKNNKGENNK PILHIIVEGE RMRKDLLYRE
     LLPLNDIALY YRIYKDETIQ SVDNLTYTLP QDRGLDKIII EYLTKYEKFN EDEANLILQM
     IKNVDSEDIV NEILKRLTGV NL
//

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