MRE11_ORYSI
ID MRE11_ORYSI Reviewed; 705 AA.
AC Q25AA3; B8AUX1;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Double-strand break repair protein MRE11;
DE Short=OsMre11;
GN ORFNames=H0410G08.11 {ECO:0000312|EMBL:CAH67656.1},
GN OsI_17582 {ECO:0000312|EMBL:EEC78093.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Guang-Lu-Ai No.4;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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:0000250|UniProtKB:P32829}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8U1N9};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:Q8U1N9};
CC -!- SUBUNIT: Component of the MRN complex composed of two heterodimers
CC RAD50/MRE11 associated with a single NBN. Interacts with NBS1 (By
CC similarity). {ECO:0000250|UniProtKB:Q09683,
CC ECO:0000250|UniProtKB:Q7XQR9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q23255}.
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEC78093.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL512546; CAH67656.1; -; Genomic_DNA.
DR EMBL; CM000129; EEC78093.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q25AA3; -.
DR SMR; Q25AA3; -.
DR STRING; 39946.Q25AA3; -.
DR PRIDE; Q25AA3; -.
DR Proteomes; UP000007015; Chromosome 4.
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; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..705
FT /note="Double-strand break repair protein MRE11"
FT /id="PRO_0000430943"
FT REGION 505..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..630
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT BINDING 15
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT BINDING 17
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT BINDING 220
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT BINDING 250
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8U1N9"
FT CONFLICT 1
FT /note="M -> R (in Ref. 2; EEC78093)"
FT CONFLICT 154
FT /note="G -> S (in Ref. 2; EEC78093)"
FT CONFLICT 522
FT /note="L -> LV (in Ref. 2; EEC78093)"
SQ SEQUENCE 705 AA; 79126 MW; 30E8BADD896D9FD0 CRC64;
MGDESNTLRV LVATDCHLGY MEKDEIRRFD SFEAFEEICS LAEQNKVDFV LLGGDLFHEN
KPSRSTLVKT IEILRRYCLN DQPVKFQVVS DQTINFPNRF GQVNYEDPNF NVGLPVFTIH
GNHDDPAGVD NLSAIDILSA CNLVNYFGKM DLGGSGVGEI AVYPVLVKKG TTFVALYGLG
NIRDERLNRM FQTPHAVQWM RPETQDGMSV SDWFNILVLH QNRIKTNPKS AINEHFLPRF
LDFIVWGHEH ECLIDPQEVP GMGFHITQPG SSVATSLIDG EAKPKHVLLL EIKGNQYRPT
KIPLRSVRPF HYAEVVLKDE VDVDPNDQAS VLEHLDKIVR NLIKKSSQPT ASRPETKLPL
IRIKVDYSGF STINPQRFGQ KYVGKVANPQ DILIFSKSAK KRQTTGVGNI DDSEKLRPEE
LNQQTIEALV AENNLKMEIL PVDDLDIALH DFVSKDDKMA FYACLQRNLE ETRTKLNSEA
DKFKIEEEDI IVKVGECMQE RVKERSLRSK EDSRFTSSSQ NLDTGGRSVT AQSNLNSFSD
DEDTREMLLG ARTTNAGRKA SGFTRPSKDA TDVAKTGTSR RGRGRGTASM KQTTLNFSQS
RSSAAIRSEE VQSSSDEENE TNEANEVVES SEPEESPQQT GRKRAAPRGG RGRGRGATAK
RGRKADISSI QSMLMSKDDD DDDEDDRPKK PPPRVTRNYG AVRRR
