Descriptions

Mre11(gp47) harbors a C-terminal Rad50 binding domain (RBD) to which Rad50 (gp46) binds. The Mre11-Rad50 complex works cooperatively in repairing DNA double-strand breaks.
In the absence of Rad50, the RBD (308-339) of Mre11 is autoinhibitory caused by the negatively charged linker (289-307) bound to the capping domain, which hinders the DNA-binding site in the nuclease domain. Deletion of the entire flexible linker of Mre11 and the RBD (290-339) enhances the nuclease activity of Mre11. Complex formation with Rad50 relieves the autoinhibition. Putative nuclease domain was predicted using a DNA-binding domain prediction tool.

Autoinhibitory domains (AIDs)

Target domain

1-200 (Nuclease domain)

Relief mechanism

Partner binding

Assay

Deletion assay, Mutagenesis experiment, Peptide inhibitor test

Target domain

1-200 (Nuclease domain)

Relief mechanism

Partner binding

Assay

Deletion assay, Peptide inhibitor test

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

0 structures for P04521

Entry ID Method Resolution Chain Position Source

No variants for P04521

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P04521

No associated diseases with P04521

1 regional properties for P04521

Type Name Position InterPro Accession
domain Calcineurin-like phosphoesterase domain, ApaH type 1 - 106 IPR004843

Functions

Description
EC Number
Subcellular Localization
PANTHER Family PTHR30337 COMPONENT OF ATP-DEPENDENT DSDNA EXONUCLEASE
PANTHER Subfamily PTHR30337:SF0 NUCLEASE SBCCD SUBUNIT D
PANTHER Protein Class DNA metabolism protein
exodeoxyribonuclease
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
exonuclease activity Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' or 5' end.

3 GO annotations of biological process

Name Definition
degradation of host chromosome by virus The catabolic breakdown of the DNA of a host chromosome by a virus. This occurs during infection of bacteria by some phages. It frees up a large pool of nucleoside 5'-triphophates for use in viral DNA synthesis.
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.
suppression by virus of host gene expression Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of gene expression in the host organism. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein. Some protein processing events may be included when they are required to form an active form of a product from an inactive precursor form.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKILNLGDWH LGVKADDEWI RGIQIDGIKQ AIEYSKKNGI TTWIQYGDIF DVRKAITHKT
70 80 90 100 110 120
MEFAREIVQT LDDAGITLHT IVGNHDLHYK NVMHPNASTE LLAKYPNVKV YDKPTTVDFD
130 140 150 160 170 180
GCLIDLIPWM CEENTGEILE HIKTSSASFC VGHWELNGFY FYKGMKSHGL EPDFLKTYKE
190 200 210 220 230 240
VWSGHFHTIS EAANVRYIGT PWTLTAGDEN DPRGFWMFDT ETERTEFIPN NTTWHRRIHY
250 260 270 280 290 300
PFKGKIDYKD FTNLSVRVIV TEVDKNLTKF ESELEKVVHS LRVVSKIDNS VESDDSEEVE
310 320 330
VQSLQTLMEE YINAIPDITD SDREALIQYA NQLYVEATQ