ID G3YES0_ASPNA Unreviewed; 792 AA.
AC G3YES0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Double-strand break repair protein {ECO:0000256|PIRNR:PIRNR000882};
GN ORFNames=ASPNIDRAFT_225671 {ECO:0000313|EMBL:EHA18257.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA18257.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA18257.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
CC -!- FUNCTION: Involved in DNA double-strand break repair (DSBR). Possesses
CC single-strand endonuclease activity and double-strand-specific 3'-5'
CC exonuclease activity. Also involved in meiotic DSB processing.
CC {ECO:0000256|PIRNR:PIRNR000882}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRNR:PIRNR000882};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR000882}.
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family.
CC {ECO:0000256|ARBA:ARBA00009028, ECO:0000256|PIRNR:PIRNR000882,
CC ECO:0000256|RuleBase:RU003447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHA18257.1}.
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DR EMBL; ACJE01000021; EHA18257.1; -; Genomic_DNA.
DR AlphaFoldDB; G3YES0; -.
DR STRING; 380704.G3YES0; -.
DR HOGENOM; CLU_009535_1_0_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0030870; C:Mre11 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0008296; F:3'-5'-DNA exonuclease activity; IEA:InterPro.
DR GO; GO:0004520; F:DNA endonuclease activity; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IEA:UniProtKB-UniRule.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR CDD; cd00840; MPP_Mre11_N; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.30.110.110; Mre11, capping domain; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR003701; Mre11.
DR InterPro; IPR038487; Mre11_capping_dom.
DR InterPro; IPR007281; Mre11_DNA-bd.
DR InterPro; IPR041796; Mre11_N.
DR NCBIfam; TIGR00583; mre11; 1.
DR PANTHER; PTHR10139; DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11; 1.
DR PANTHER; PTHR10139:SF1; DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF04152; Mre11_DNA_bind; 1.
DR PIRSF; PIRSF000882; DSB_repair_MRE11; 1.
DR SMART; SM01347; Mre11_DNA_bind; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR000882};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PIRNR:PIRNR000882};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759,
KW ECO:0000256|PIRNR:PIRNR000882};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR000882};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000882};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR000882};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254, ECO:0000256|PIRNR:PIRNR000882};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR000882};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR000882}.
FT DOMAIN 288..467
FT /note="Mre11 DNA-binding"
FT /evidence="ECO:0000259|SMART:SM01347"
FT REGION 525..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..683
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000882-1"
SQ SEQUENCE 792 AA; 88892 MW; 1E33A7D1C279A06E CRC64;
MHPDSETIRI LVSTDNHVGY NERDPIRGDD SWKSFHEVMC LAKEQDVDMV LLAGDLFHEN
KPSRKSMYQV MRSIRMNCLG DKPCELEMLS DASENFQGAF NHVNYEDLDI NVAIPIFSIH
GNHDDPSGEG HLAALDLLQV SGLINYYGRT PESDNIQIKP VLLQKGRTKL ALYGMSNVRD
ERLFRTFRDG KVKFYQPSIQ KEDWFNLMSV HQNHYAHTET GYLPENFLPE FLDLVVWGHE
HECLINPRLN PETKFHVMQP GSSVATSLVP GESVAKHVAI LSITGREFKC EPIRLKSVRP
FAMREIILSE EKGAQKLARK DNNRTEVTRL LMEIVEELIE EAKTEWLEMQ DETAEDEELE
VPLPLVRLRV ETSTPEGGSY DCENPQRFSN RFVGKVANVN DVVQFYRKKK NTNSTRKPGE
TDLDETAVSH LSTLDTVKVE QLVRDFLSAQ SLTILPQNSF GDAVAQFIDK DDKHALEMFV
NESLESQMKH LLALDRDHDL EEEEEIAESS LQKAMERYRT QMEDMFSRGI KKRTRGKKRF
KPKPDGWDTE FDGVWEDQPG ALIHSDNEDG DPNEDVAGED GAEPPTTSRA TSSTRGRGRG
RGGRATTTAA TTRKTATTKA APATTTSKKT TTSTKSRKRR TVSDEEDEQE DVIMLDDDDD
DDDDNAATSL PNIDEEDDDD DDSLFVKQPA KSTTSTRSRR TTTAATAKAT TQRRKAPSPA
PSSNTVGGTG QATRRTRGKQ ATQTTLNFVG SQSSVRGTAG SGRSMRATRA ASEDIEDDSD
AFEPMASSAR RR
//
