Descriptions

Mre11 and Rad50 form a stable complex (MR) at the C-terminal Rad50 binding domain (RBD), which works cooperatively in repairing DNA double-strand breaks. In the absence of Rad50, the RBD of Mre11 is autoinhibitory caused by the negatively charged linker bound to the capping domain, which hinders the DNA-binding site. Deletion of the entire flexible linker of Mre11 and the RBD enhances the nuclease activity of Mre11.

Autoinhibitory domains (AIDs)

Target domain

2-208 (Nuclease domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

7 structures for Q58719

Entry ID Method Resolution Chain Position Source
3AUZ X-ray 321 A A 1-313 PDB
3AV0 X-ray 310 A A 1-366 PDB
4TUG X-ray 355 A A/B/C/D/E/F 1-333 PDB
4TUI X-ray 359 A A/B/C/D/E/F 1-333 PDB
5DNY X-ray 311 A A/C 1-366 PDB
5F3W X-ray 311 A A/C 1-366 PDB
AF-Q58719-F1 Predicted AlphaFoldDB

No variants for Q58719

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q58719

No associated diseases with Q58719

2 regional properties for Q58719

Type Name Position InterPro Accession
domain Calcineurin-like phosphoesterase domain, ApaH type 3 - 189 IPR004843
domain Mre11 nuclease, N-terminal metallophosphatase domain 2 - 208 IPR041796

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

8 GO annotations of molecular function

Name Definition
3'-5' exonuclease activity Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA end binding Binding to DNA ends exposed by the creation of double-strand breaks (DSBs).
endonuclease activity Catalysis of the hydrolysis of ester linkages within nucleic acids by creating internal breaks.
exodeoxyribonuclease activity Catalysis of the sequential cleavage of mononucleotides from a free 5' or 3' terminus of a DNA molecule.
identical protein binding Binding to an identical protein or proteins.
manganese ion binding Binding to a manganese ion (Mn).
Y-form DNA binding Binding to a DNA segment shaped like a Y. This shape occurs when DNA contains a region of paired double-stranded DNA on one end and a region of unpaired DNA strands on the opposite end.

2 GO annotations of biological process

Name Definition
DNA repair The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
double-strand break repair The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MMFVHIADNH LGYRQYNLDD REKDIYDSFK LCIKKILEIK PDVVLHSGDL FNDLRPPVKA
70 80 90 100 110 120
LRIAMQAFKK LHENNIKVYI VAGNHEMPRR LGEESPLALL KDYVKILDGK DVINVNGEEI
130 140 150 160 170 180
FICGTYYHKK SKREEMLDKL KNFESEAKNY KKKILMLHQG INPYIPLDYE LEHFDLPKFS
190 200 210 220 230 240
YYALGHIHKR ILERFNDGIL AYSGSTEIIY RNEYEDYKKE GKGFYLVDFS GNDLDISDIE
250 260 270 280 290 300
KIDIECREFV EVNIKDKKSF NEAVNKIERC KNKPVVFGKI KREFKPWFDT LKDKILINKA
310 320 330 340 350 360
IIVDDEFIDM PDNVDIESLN IKELLVDYAN RQGIDGDLVL SLYKALLNNE NWKELLDEYY
NTKFRG