Descriptions

Bacteriophage T4 Mre11 and Rad50 form a stable Mre11/Rad50 (MR) complex and work cooperatively in repairing DNA double-strand breaks. In the absence of Rad50, the C-terminal Rad50 binding domain (RBD) of Mre11 is autoinhibited caused by the negatively charged linker. Rad50 association and deletion of the C-terminus of Mre11 both enhance DNA binding and the nuclease activity of Mre11.

Autoinhibitory domains (AIDs)

Target domain

7-219 (Nuclease domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

15 structures for Q9X1X0

Entry ID Method Resolution Chain Position Source
2Q8U X-ray 220 A A/B 1-324 PDB
3QF7 X-ray 190 A C/D 343-385 PDB
3QG5 X-ray 340 A C/D 7-385 PDB
3THN X-ray 281 A A 7-325 PDB
3THO X-ray 261 A B 7-385 PDB
4NZV X-ray 190 A A/B 2-324 PDB
4O24 X-ray 230 A A/B 2-324 PDB
4O43 X-ray 240 A A/B 2-324 PDB
4O4K X-ray 210 A A/B 2-324 PDB
4O5G X-ray 230 A A/B 2-324 PDB
4W9M X-ray 270 A D/F/J/L 347-383 PDB
6ASC X-ray 215 A A/B 2-324 PDB
6X1Y X-ray 235 A A/B 2-324 PDB
6X1Z X-ray 190 A A/B 2-324 PDB
AF-Q9X1X0-F1 Predicted AlphaFoldDB

No variants for Q9X1X0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9X1X0

No associated diseases with Q9X1X0

2 regional properties for Q9X1X0

Type Name Position InterPro Accession
domain Calcineurin-like phosphoesterase domain, ApaH type 7 - 219 IPR004843
domain Mre11 nuclease, N-terminal metallophosphatase domain 8 - 241 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

5 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).
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.
metal ion binding Binding to a metal ion.

3 GO annotations of biological process

Name Definition
DNA recombination Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
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.
DNA replication termination The process in which DNA replication at a replication fork ceases; occurs when the replication fork reaches a specific termination site or when two replication forks meet.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MINLKELKIL HTSDWHLGVT SWTSSRPVDR REELKKALDK VVEEAEKREV DLILLTGDLL
70 80 90 100 110 120
HSRNNPSVVA LHDLLDYLKR MMRTAPVVVL PGNHDWKGLK LFGNFVTSIS SDITFVMSFE
130 140 150 160 170 180
PVDVEAKRGQ KVRILPFPYP DESEALRKNE GDFRFFLESR LNKLYEEALK KEDFAIFMGH
190 200 210 220 230 240
FTVEGLAGYA GIEQGREIII NRALIPSVVD YAALGHIHSF REIQKQPLTI YPGSLIRIDF
250 260 270 280 290 300
GEEADEKGAV FVELKRGEPP RYERIDASPL PLKTLYYKKI DTSALKSIRD FCRNFPGYVR
310 320 330 340 350 360
VVYEEDSGIL PDLMGEIDNL VKIERKSRRE IEEVLRESPE EFKEELDKLD YFELFKEYLK
370 380
KREENHEKLL KILDELLDEV KKSEA