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   03-AUG-2022, entry version 117.
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: Component of the MRN complex, which plays a central role in
CC       double-strand break (DSB) repair, DNA recombination, maintenance of
CC       telomere integrity and meiosis. The complex possesses single-strand
CC       endonuclease activity and double-strand-specific 3'-5' exonuclease
CC       activity, which are provided by MRE11. RAD50 may be required to bind
CC       DNA ends and hold them in close proximity. This could facilitate
CC       searches for short or long regions of sequence homology in the
CC       recombining DNA templates, and may also stimulate the activity of DNA
CC       ligases and/or restrict the nuclease activity of MRE11 to prevent
CC       nucleolytic degradation past a given point. The complex may also be
CC       required for DNA damage signaling via activation of the ATM kinase. In
CC       telomeres the MRN complex may modulate t-loop formation (By
CC       similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Component of the MRN complex composed of two heterodimers
CC       RAD50/MRE11 associated with a single NBN. Component of the BASC
CC       complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50,
CC       MRE11 and NBN. Interacts with DCLRE1C/Artemis (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to discrete
CC       nuclear foci after treatment with genotoxic agents. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000305}.
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DR   EMBL; AF166094; AAF31354.1; -; mRNA.
DR   RefSeq; NP_990109.1; NM_204778.1.
DR   AlphaFoldDB; Q9IAM7; -.
DR   SMR; Q9IAM7; -.
DR   STRING; 9031.ENSGALP00000027766; -.
DR   PaxDb; Q9IAM7; -.
DR   PRIDE; Q9IAM7; -.
DR   GeneID; 395555; -.
DR   KEGG; gga:395555; -.
DR   CTD; 4361; -.
DR   VEuPathDB; HostDB:geneid_395555; -.
DR   eggNOG; KOG2310; Eukaryota.
DR   InParanoid; Q9IAM7; -.
DR   OrthoDB; 834694at2759; -.
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   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0030870; C:Mre11 complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005657; C:replication fork; ISS:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR   GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IEA:InterPro.
DR   GO; GO:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; 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; IBA:GO_Central.
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:0000723; P:telomere maintenance; IBA:GO_Central.
DR   CDD; cd00840; MPP_Mre11_N; 1.
DR   Gene3D; 3.30.110.110; -; 1.
DR   Gene3D; 3.60.21.10; -; 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   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; SSF56300; 1.
DR   TIGRFAMs; TIGR00583; mre11; 1.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase; Manganese;
KW   Meiosis; Nuclease; Nucleus; Reference proteome.
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   COMPBIAS        505..533
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..694
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
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