MRE11_COPC7
ID MRE11_COPC7 Reviewed; 731 AA.
AC Q9UVN9; A8P0I4;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Double-strand break repair protein MRE11;
GN Name=MRE11; ORFNames=CC1G_10319;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10757758; DOI=10.1093/genetics/154.3.1125;
RA Gerecke E.E., Zolan M.E.;
RT "An mre11 mutant of Coprinus cinereus has defects in meiotic chromosome
RT pairing, condensation and synapsis.";
RL Genetics 154:1125-1139(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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 (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Forms a complex with RAD50. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU83914.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF178433; AAD55951.1; -; Genomic_DNA.
DR EMBL; AACS02000006; EAU83914.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001837898.2; XM_001837846.2.
DR AlphaFoldDB; Q9UVN9; -.
DR SMR; Q9UVN9; -.
DR STRING; 5346.XP_001837898.2; -.
DR EnsemblFungi; EAU83914; EAU83914; CC1G_10319.
DR GeneID; 6014460; -.
DR KEGG; cci:CC1G_10319; -.
DR eggNOG; KOG2310; Eukaryota.
DR HOGENOM; CLU_009535_3_1_1; -.
DR InParanoid; Q9UVN9; -.
DR OrthoDB; 834694at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase; Manganese;
KW Meiosis; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..731
FT /note="Double-strand break repair protein MRE11"
FT /id="PRO_0000138681"
FT REGION 543..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..660
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 731 AA; 80647 MW; 09281A77D69F4916 CRC64;
MSDYEEDTRP PPNIETADPE DTIKILLATD NHIGYLERDP IRGQDSINTF REILQLAVKN
EVDFILLAGD LFHENKPSRD CLYQTLALLR EYTLGDKPIQ VELLSDPDEG KAAGFSFPAI
NYEDPNFNIS IPVFSIHGNH DDPQGPGVNG ALCALDVLSV SGLLNYMGKF DLPTSDADAA
TTGIAVRPVL LRKGSTKLGM YGVGNVKDQR MHFELRSNRV RMYMPKDKDE WFNILLVHQN
RVKHGPQEYV PEGMFDDSVD LVVWGHEHDC RIIPEPVAGK NYYITQPGSS VATSLADGEA
IEKHVALLEI KGKEFQLTPI PLRTVRPFVI SEVVLEDAAE EEGLDVNDQM EITKYLKQKV
NDLIDQAQAL WEERNARSIE AGDEEIPPML PLVRLKVDTT NVTQTSNPIR FGQEFQGRVA
NPRDLLVFHR SKKAGKRGAG KVDIDQPELS IDDPDLTVSE KLAKVRVKTL VREYLAAQEL
QLLGENGMSD AIQMFVEKDD IHAIQTHVNK SLKTMLKNIK SDEVDEDDLD DLLAKAKQRQ
EEEYLEATRA GESAKGKGKA KATDDDGGAA SDDSMLMDID TGGGATFNMS DDDDDDEPPP
PPKRRAATSR ATTTKKAPAK APAKKATTTT ARGRGKKAAP PSSDDEVIEL DDDEDEISEE
EVVAKPVKRT SRAAVLSQSQ APAKKAPAKK KTPARQTQTQ LSFAPAGRSS RAAASKARSK
MVFDDDDDDD D