ID A0A0F8XS35_9EURO Unreviewed; 793 AA.
AC A0A0F8XS35;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Double-strand break repair protein {ECO:0000256|PIRNR:PIRNR000882};
GN ORFNames=ARAM_004260 {ECO:0000313|EMBL:KKK26332.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK26332.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK26332.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK26332.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KKK26332.1}.
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DR EMBL; JZBS01000459; KKK26332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8XS35; -.
DR STRING; 308745.A0A0F8XS35; -.
DR OrthoDB; 169704at2759; -.
DR Proteomes; UP000034291; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT DOMAIN 290..470
FT /note="Mre11 DNA-binding"
FT /evidence="ECO:0000259|SMART:SM01347"
FT REGION 498..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..660
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000882-1"
SQ SEQUENCE 793 AA; 88486 MW; 12E385BD871FAC4E CRC64;
MAELGDAETI RILVSTDNHV GYNERDPIRG DDSWKSFHEV MCLATKHDVD MVLLAGDLFH
ENKPSRKSMY QVMRSMRMNC LGDKPCELEF LSDASENFQG AFNHVNYEDM DINVAIPIFS
IHGNHDDPSG EGHLAALDIL QVSGLINYYG RTPESDNIQI KPVLLQKGRT KLALYGMSNV
RDERLFRTFR DGKVKFFRPS IQKDDWYNLI CVHQNHHAYT ETGYLPENFL PEFLDLVVWG
HEHECLINPR INPETKFRVM QPGSSVATSL VPGEAVPKHV AILSITGKEM KCEPIRLKSV
RPFVMKEIVL SEEKGAQKLA RKENNRTEVT RFLMTIVEEL IEEAKAEWLE MQDGAADDEE
LEIPLPLVRL RVEISTPEGG SYDCENPQRF SNRFVGKVAN VNDVVQFYRK KKAATTSTGR
KKGNEVEETS ISHLTALDTV KVEQLVQEFL ASQSLSILPQ NSFGDAVAQF IDKDDKHAME
MFVNDSLDGQ IKHLLSLDRD SETEEDATPQ SSLQQAMEKY RSQMEEMFSK GVKKRSRGKK
RFKPKPDGWD SEFDGSWEDQ PGALIHSDNE GGNSPDDKDG AEPATGRSTT STRGRGRGRG
GTAAATRKAG TTTKKSAPTK TTRARGRRAV SDEEEEEKEH EDHDVVMIDD DDDDNNQPQP
LSDIEEDSDS QALFVKQPAS KSRKGKGGST TTNTTTTTRT TSQRQSKRSV PSPASSNTVG
GTAARKPRGA AGKQTQLTLD FVGSQSSARG STAASSNTRS MRPNRTTRSV SVLSEDVDDS
DGFEPMPSSR RRR
//
