Q95NM6
Gene name |
cps-6 (C41D11.8) |
Protein name |
Endonuclease G, mitochondrial |
Names |
Endo G, Ced-3 protease suppressor 6 |
Species |
Caenorhabditis elegans |
KEGG Pathway |
cel:CELE_C41D11.8 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
5 structures for Q95NM6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3S5B | X-ray | 180 A | A/B | 63-303 | PDB |
| 4QN0 | X-ray | 274 A | A/B/C/D | 64-302 | PDB |
| 5GKC | X-ray | 189 A | A/B | 63-305 | PDB |
| 5GKP | X-ray | 230 A | A/B | 63-305 | PDB |
| AF-Q95NM6-F1 | Predicted | AlphaFoldDB |
No variants for Q95NM6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q95NM6 | |||||
No associated diseases with Q95NM6
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial inner membrane | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
8 GO annotations of molecular function
| Name | Definition |
|---|---|
| double-stranded DNA endodeoxyribonuclease activity | Catalysis of the hydrolysis of ester linkages within a double-stranded deoxyribonucleic acid molecule by creating internal breaks. |
| endodeoxyribonuclease activity | Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks. |
| endonuclease activity | Catalysis of the hydrolysis of ester linkages within nucleic acids by creating internal breaks. |
| endoribonuclease activity | Catalysis of the hydrolysis of ester linkages within ribonucleic acid by creating internal breaks. |
| metal ion binding | Binding to a metal ion. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
| sequence-specific DNA binding | Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding. |
| single-stranded DNA endodeoxyribonuclease activity | Catalysis of the hydrolysis of ester linkages within a single-stranded deoxyribonucleic acid molecule by creating internal breaks. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| apoptotic DNA fragmentation | The cleavage of DNA during apoptosis, which usually occurs in two stages: cleavage into fragments of about 50 kbp followed by cleavage between nucleosomes to yield 200 bp fragments. |
| DNA catabolic process, endonucleolytic | The chemical reactions and pathways resulting in the breakdown of DNA, involving the hydrolysis of internal 3',5'-phosphodiester bonds in one or two strands of deoxyribonucleotides. |
| RNA catabolic process | The chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. |
3 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIGKVAGTAA | IAGISFLAGK | YSNDDLPIFR | NVQSATNVPM | NQIQVSEPMT | VKPASLNADA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MGPSRSAEIM | KHGYPGFTNV | RTYEDFVLSY | DYKTRTAHWV | CEHLTPERLK | HAEGVDRKLC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EFKPDITFPQ | KFLSQNTDYK | CSGFDRGHLA | AAGNHRKSQL | AVDQTFYLSN | MSPQVGRGFN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RDKWNDLEMH | CRRVAKKMIN | SYIITGPLYL | PKLEGDGKKY | IKYQVIGDNN | VAVPTHFFKV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ALFEVTPGKF | ELESYILPNA | VIEDTVEISK | FHVPLDAVER | SAGLEIFARL | DPKSIVKENG |
| AKKGGLLW |