ID   MRE11_CHICK             Reviewed;         700 AA.
AC   Q9IAM7;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   04-NOV-2026, entry version 131.
DE   RecName: Full=Double-strand break repair protein MRE11;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:P49959};
GN   Name=MRE11;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=10581236; DOI=10.1093/emboj/18.23.6619;
RA   Yamaguchi-Iwai Y., Sonoda E., Sasaki M.S., Morrison C., Haraguchi T.,
RA   Hiraoka Y., Yamashita Y.M., Yagi T., Takata M., Price C., Kakazu N.,
RA   Takeda S.;
RT   "Mre11 is essential for the maintenance of chromosomal DNA in vertebrate
RT   cells.";
RL   EMBO J. 18:6619-6629(1999).
CC   -!- FUNCTION: Core component of the MRN complex, which plays a central role
CC       in double-strand break (DSB) repair, DNA recombination, maintenance of
CC       telomere integrity and meiosis (By similarity). The MRN complex is
CC       involved in the repair of DNA double-strand breaks (DSBs) via
CC       homologous recombination (HR), an error-free mechanism which primarily
CC       occurs during S and G2 phases (By similarity). The complex (1) mediates
CC       the end resection of damaged DNA, which generates proper single-
CC       stranded DNA, a key initial steps in HR, and is (2) required for the
CC       recruitment of other repair factors and efficient activation of ATM and
CC       ATR upon DNA damage (By similarity). Within the MRN complex, MRE11
CC       possesses both single-strand endonuclease activity and double-strand-
CC       specific 3'-5' exonuclease activity (By similarity). After DSBs, MRE11
CC       is loaded onto DSBs sites and cleaves DNA by cooperating with
CC       RBBP8/CtIP to initiate end resection (By similarity). MRE11 first
CC       endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent
CC       non-homologous end joining (NHEJ) and licence HR (By similarity). It
CC       then generates a single-stranded DNA gap via 3' to 5' exonucleolytic
CC       degradation to create entry sites for EXO1- and DNA2-mediated 5' to 3'
CC       long-range resection, which is required for single-strand invasion and
CC       recombination (By similarity). RBBP8/CtIP specifically promotes the
CC       endonuclease activity of MRE11 to clear protein-DNA adducts and
CC       generate clean double-strand break ends (By similarity). The MRN
CC       complex is also required for DNA damage signaling via activation of the
CC       ATM and ATR kinases: the nuclease activity of MRE11 is not required to
CC       activate ATM and ATR (By similarity). In telomeres the MRN complex may
CC       modulate t-loop formation (By similarity).
CC       {ECO:0000250|UniProtKB:P49959}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P49959};
CC   -!- SUBUNIT: Component of the MRN complex composed of two heterodimers
CC       RAD50 and MRE11 associated with a single NBN.
CC       {ECO:0000250|UniProtKB:Q9W6K1}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49959}.
CC       Chromosome {ECO:0000250|UniProtKB:P49959}. Chromosome, telomere
CC       {ECO:0000250|UniProtKB:P49959}. Note=Localizes to DNA double-strand
CC       breaks (DSBs). {ECO:0000250|UniProtKB:P49959}.
CC   -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000305}.
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DR   EMBL; AF166094; AAF31354.1; -; mRNA.
DR   RefSeq; NP_990109.2; NM_204778.2.
DR   SMR; Q9IAM7; -.
DR   STRING; 9031.ENSGALP00000027766; -.
DR   PaxDb; 9031-ENSGALP00000027766; -.
DR   GeneID; 395555; -.
DR   KEGG; gga:395555; -.
DR   CTD; 4361; -.
DR   VEuPathDB; HostDB:geneid_395555; -.
DR   eggNOG; KOG2310; Eukaryota.
DR   InParanoid; Q9IAM7; -.
DR   OMA; AARPSYM; -.
DR   OrthoDB; 30417at2759; -.
DR   PhylomeDB; Q9IAM7; -.
DR   Reactome; R-GGA-217106; Chk1-controlled and DNA-damage induced centrosome duplication.
DR   Reactome; R-GGA-351442; ATM mediated response to DNA double-strand break.
DR   Reactome; R-GGA-351444; Recruitment of repair and signaling proteins to double-strand breaks.
DR   PRO; PR:Q9IAM7; -.
DR   CDD; cd00840; MPP_Mre11_N; 1.
DR   FunFam; 3.30.110.110:FF:000001; Double-strand break repair protein; 1.
DR   FunFam; 3.60.21.10:FF:000011; Double-strand break repair protein; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.30.110.110; Mre11, capping domain; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP.
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   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.
DR   NCBIfam; TIGR00583; mre11; 1.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030870; C:Mre11 complex; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005657; C:replication fork; ISS:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; ISS:UniProtKB.
DR   GO; GO:0008296; F:3'-5'-DNA exonuclease activity; IEA:InterPro.
DR   GO; GO:0004520; F:DNA endonuclease activity; ISS:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0000014; F:single-stranded DNA endonuclease activity; IBA:GO_Central.
DR   GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR   GO; GO:0110025; P:DNA strand resection involved in replication fork processing; ISS:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR   GO; GO:0042138; P:meiotic DNA double-strand break formation; IBA:GO_Central.
DR   GO; GO:0097552; P:mitochondrial double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR   GO; GO:0062176; P:R-loop processing; ISS:UniProtKB.
DR   GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   AlphaFoldDB; Q9IAM7; -.
DR   FunCoup; Q9IAM7; 2148.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase;
KW   Manganese; Meiosis; Metal-binding; Nuclease; Nucleus; Reference proteome;
KW   Telomere.
FT   CHAIN           1..700
FT                   /note="Double-strand break repair protein MRE11"
FT                   /id="PRO_0000138676"
FT   REGION          505..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           569..592
FT                   /note="GAR"
FT                   /evidence="ECO:0000250|UniProtKB:P49959"
FT   COMPBIAS        521..533
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..586
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..604
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..648
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..677
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q61216"
FT   BINDING         20
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P49959"
FT   BINDING         22
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P49959"
FT   BINDING         60
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P49959"
FT   BINDING         60
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P49959"
FT   BINDING         128
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P49959"
FT   BINDING         217
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P49959"
FT   BINDING         245
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P49959"
FT   BINDING         247
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P49959"
SQ   SEQUENCE   700 AA;  80024 MW;  53039A0FFEFE5292 CRC64;
     MSAVSLQDDE DTFKILIATD IHLGYLEKDA VRGNDTFVTF NEILEHAQKN EVDFILLGGD
     LFHENKPSRK TIHTCLESLR KYCMGDRPVS FEVLSDQAVN FQLSKFPWVN YQDENLNIFM
     PIFSIHGNHD DPTGVDALCA LDILSCAGLL NHFGRSTSVE KIDISPILLR KGRTKIALYG
     LGAIPDERLY RMFVNKQVTM LRPKEDEDSW FNMFVIHQNR SKHGATNYIP EQFLDDFINL
     AVWGHEHECK ITPAQNEQQH FYVTQPGSSV VTSLSPGEAV KKHIGLLRVK GKKMKMQRIA
     LETVRTFYME DVVLADHPEL FNPDNPKVTQ AIQAFCMEKV EMMLDNAERE RLGNPRQPQK
     PLIILRVDYT GGFEPFIVHR FSQKYMDRVA NPKDIIHFFR HREQKEKNDN DINFGKLLSR
     PASEEVTLRV EDLVKQYFQT AEKKVQLSLL TERRMGEAVQ EFVDKEEKDA IEELVKFQLE
     KTQRFLKERH IDAEEEKIDE EVRKFRESRR KNTEEEDEEV REAMTRARAH RSEGVVLDSA
     SSDEGLMDTG MKASGDSDDD IPTTLSRGRG RGRARGARGQ NSAARGSSRR GRGNTSQGSS
     TSSRTYKSVP DKNSSIMDAF RSLKPEPSQS TSKFFSEDII DDEMDLEESP ISLSSKTNQR
     SSAMSSFSKR GSQSQMSRGV DFESDEDDPF KNTATSRRKK
//