ID A0A022R8D2_ERYGU Unreviewed; 723 AA.
AC A0A022R8D2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Mre11 DNA-binding domain-containing protein {ECO:0000259|SMART:SM01347};
DE Flags: Fragment;
GN ORFNames=MIMGU_mgv1a022393mg {ECO:0000313|EMBL:EYU35145.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU35145.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU35145.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family.
CC {ECO:0000256|ARBA:ARBA00009028, ECO:0000256|RuleBase:RU003447}.
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DR EMBL; KI630629; EYU35145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022R8D2; -.
DR STRING; 4155.A0A022R8D2; -.
DR eggNOG; KOG2310; Eukaryota.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0030870; C:Mre11 complex; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0008296; F:3'-5'-DNA exonuclease activity; IEA:InterPro.
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:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
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:0000723; P:telomere maintenance; IBA:GO_Central.
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 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU003447};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU003447};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759,
KW ECO:0000256|RuleBase:RU003447};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|RuleBase:RU003447};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003447};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU003447};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254, ECO:0000256|RuleBase:RU003447};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU003447};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU003447};
KW Reference proteome {ECO:0000313|Proteomes:UP000030748}.
FT DOMAIN 296..449
FT /note="Mre11 DNA-binding"
FT /evidence="ECO:0000259|SMART:SM01347"
FT REGION 510..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..672
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000882-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EYU35145.1"
SQ SEQUENCE 723 AA; 80584 MW; D7B032FE489985F8 CRC64;
EDKGDMLRIL VATDCHLGYM EKDEVRRHDS FQAFEEICSI AEQKKVDFVL LGGDLFHENK
PSRSTLVKAI EILRRHCLND KPVQFQVVSD QIVNFANSFG HVNYEDPHFN VGLPVFSIHG
NHDDPAGVDN LSAVDILSAC NLVNYFGKMV LEGSGVGQIT LYPILIKKGS TSVALYGLGN
IRDERLNRMF QTPHAVQWMR PEAQEGCQVS DWFNILTLHQ NRVKTNPKNA INEHFLPRFL
DFVVWGHEHE CLVDPQEVPG MGFHITQPGS SVATSLIDGE SKPKHVLLLE IKGNQYRPTK
IPLESVRPFE YVEVVLKDEP DIDHNDQNSI LEHLDKVVRN LIERAKQKAI KNSELKLPLV
RIKVDYSGFM TINPQRFGQK YVGKVANPQD ILIFSKASNK HSSGGKIDDS ERLRPEELNQ
ANIEALVAES NLKMEILPVN DLDVALHNFV NKDDKMAFYS CLQYNLEETR SKIAQDSDVQ
KFEEEDIIVK VGECLEERVK ERTLKPNDAQ QFTFSGQASE NVRSRSTQGL GSAASFSDDE
DATVFPGSMS TKKGKQSQSS KPPRNSSEAG KTTGRGRGRG RGRGRGSDTL KQTTLEATMG
LRPSQRSASA AASASFRSLD DEDEVDSDSN DETAKLDVND IAESSDDGDT IGNSRKRAAP
RGRGRGRGST TASKRGKKTD SSSSSSLHRL LSSRDDDDED DDMAKKLNKS QPRVTRNYGA
LRK
//
