ID Q4GX60_TRITU Unreviewed; 699 AA.
AC Q4GX60;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Double-strand break repair protein {ECO:0000256|PIRNR:PIRNR000882};
GN Name=mre11 {ECO:0000313|EMBL:CAJ15652.1};
OS Triticum turgidum (Poulard wheat) (Rivet wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4571 {ECO:0000313|EMBL:CAJ15652.1};
RN [1] {ECO:0000313|EMBL:CAJ15652.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Immature spikelet {ECO:0000313|EMBL:CAJ15652.1};
RX PubMed=17262197; DOI=10.1007/s00122-006-0493-x;
RA De Bustos A., Perez R., Jouve N.;
RT "Characterization of the gene Mre11 and evidence of silencing after
RT polyploidization in Triticum.";
RL Theor. Appl. Genet. 114:985-999(2007).
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 ---------------------------------------------------------------------------
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; AM049172; CAJ15651.1; -; Genomic_DNA.
DR EMBL; AM049173; CAJ15652.1; -; mRNA.
DR AlphaFoldDB; Q4GX60; -.
DR EnsemblPlants; TRITD2Bv1G245540.1; TRITD2Bv1G245540.1; TRITD2Bv1G245540.
DR Gramene; TRITD2Bv1G245540.1; TRITD2Bv1G245540.1; TRITD2Bv1G245540.
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 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
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 297..452
FT /note="Mre11 DNA-binding"
FT /evidence="ECO:0000259|SMART:SM01347"
FT REGION 551..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 462..489
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 582..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..625
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..687
FT /note="Basic and acidic 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 699 AA; 77987 MW; 8F9DB6DF9FA6755F CRC64;
MEDDRDMLRI LVATDCHLGY MEKDEIRRFD SFEAFEEICS LAKQKEVDFV LLGGDLFHEN
KPSRSTLVKT IEILRRYCLN DLPVKFQVVS DQTVNFPNRF GHVNYEDPHF NVGLPVFTIH
GNHDDPAGVD NLSAIDILSA CNLVNYFGKM DLGGSGVGQI AVHPVLVKKG TTTVALYGLG
NIRDERLNRM FQTPHSVQWM RPESQEGLSV SDWFNILVLH QNRIKTNPKS AINEHFLPRF
LDFVVWGHEH ECLIDPQEVP GMGFHITQPG SSVATSLIDG EAKPKHVLLL EIKGNQYRPN
KIPLMTVRPF EYAEVVLKDE ADVDPNDQAS VLEHLDKIVR NLIEKSSQPA ASRSEAKLPL
VRIKVDYSGF STINPQRFGQ KYVGKVANPQ DILIFSKAAK KRQTTTGENI DESEKLRPEE
LNQQTIEALV AENNLKMEIL PVDDLDIALH DFVSKDDKTA FYACLQRNLD ETRKKLNSEA
EKFKIEEEDI IVKVGECMQE RVKEISLRSK GDTGLASSTQ NLDTIRGKSV AAESSLNTFS
DDEDTRELLL GTRSTRSTAG FTRPSKDATG AARGGASKRG SGKGSLKQTT LTFSQSRSSA
AIRSEEVDSS SDEDAANEVN EVVENSDPED SFPQSGRKRP APRGRGRARG TTTAKRGRKA
DTGSMPSMVM SKDDDSDEDD KPKKPPPRVT RNYGAVKRR
//
