ID A0A175VPJ0_9PEZI Unreviewed; 727 AA.
AC A0A175VPJ0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Double-strand break repair protein {ECO:0000256|PIRNR:PIRNR000882};
GN ORFNames=MMYC01_209930 {ECO:0000313|EMBL:KXX73303.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX73303.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA van de Sande W.W.J.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXX73303.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA Van De Sande W.;
RT "Madurella mycetomatis genome sequencing.";
RL Submitted (JAN-2016) 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:KXX73303.1}.
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DR EMBL; LCTW02000498; KXX73303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175VPJ0; -.
DR STRING; 100816.A0A175VPJ0; -.
DR VEuPathDB; FungiDB:MMYC01_209930; -.
DR OrthoDB; 169704at2759; -.
DR Proteomes; UP000078237; 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:UP000078237}.
FT DOMAIN 288..468
FT /note="Mre11 DNA-binding"
FT /evidence="ECO:0000259|SMART:SM01347"
FT REGION 519..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..699
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 727 AA; 81982 MW; 971964D9AC6AC1F2 CRC64;
MLLDADTIRI LVSTDNHVGF EERDPIRKDD SWRTFDEIMQ LARTRDVDMV LLGGDLFHEN
KPSRKAMYQV MRSLRRNCLG MKPCELEFLS DAAEVFEGSV AHVNYQDPDI NISIPVFSIH
GNHDDPSGDG HYCSLDLLQV AGLVNYFGRV PEADNIQVKP ILLQKGKTKL ALYGLSNVRD
ERMYRTFRDN KVRFYRPNRQ KADFFNLLTV HQNHHAHTPT SYLPENMLPD FMDLVIWGHE
HECLIDPKRN PETGFHVMQP GSSIATSLVQ GEAVTKHVAI LSVTGKTFEV EKIPLRTVRP
FVTKEIFLAT DERFKGLGRK QDNRQDITKR LMLIVEDMIK EANSIWQSIH GGSEGDEDED
EEQPLPLIRL KVEYTAPEGS NYEVENPQRF SNRFAGKVAN QNDVVYFYRK KAGTARKAKE
IQELPGSVAE ALESVDAIKV DTLVQEFFAQ QSLKILPQAP FGDAVNQFVS KDDRHAVEMF
VLDSLTHQVK GLLQLDDEKI TEGLDAHIDD FRKVMEKKFV SGQQKQEQRK RRFKEKPEGW
DSDLDGHWTA QPGAIEELPS SPEPTGSGPS RTRPTSGITF SDDDADLFGD GPSLANAPAP
PKKATGAATK PTKKAAPSKR AAAPAKKPAA PKKAPVRGRR KANPFQDSDN EEEDEDVIME
DDDAEPPRKS TRETRSRGAP KTRQTTLNFS QSQRATKPLQ KAIEISDDEI SEDDAFESMP
ATRSRRR
//
