Q9P7G4
Gene name |
oma1 |
Protein name |
Mitochondrial metalloendopeptidase OMA1 |
Names |
|
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPAP14E8.04 |
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
1 structures for Q9P7G4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9P7G4-F1 | Predicted | AlphaFoldDB |
3 variants for Q9P7G4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| I_1926874_A_G | 46 | S>G | No | Jeffares_SNPs | |
| I_1926935_G_A | 66 | R>K | No | Jeffares_SNPs | |
| I_1927160_G_A | 141 | R>K | No | Jeffares_SNPs |
No associated diseases with Q9P7G4
1 regional properties for Q9P7G4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase M48 | 134 - 308 | IPR001915 |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| metalloendopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| mitochondrial protein processing | The peptide cleavage of mitochondrial proteins, including cleavage contributing to their import. |
| protein quality control for misfolded or incompletely synthesized proteins | The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins. |
| proteolysis involved in protein catabolic process | The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MFLNKYISNY | SRTRAVSCAP | VLSYKKCSYR | NFNGLLQARF | QSNNLSWSNR | NRVVYKSFQP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NPRDKRFQWI | FGALIAGGGV | YYFTHLEYVP | ISNRRRFNDV | SLDFEKRMAQ | DAYKEVMSEY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GDRMLPSYHP | TTLYVSRVLK | RIIAVSGMSD | LKWELHVIRD | PTPNAFVLPG | GKVFVFEGIL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PMCKGEDGLA | AVLAHETAHQ | VARHSAEKIA | FTRAVSCIVF | LAAASLDLSG | QLSHFLLNFG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LLLPFSRKME | TEADYIGLML | MSQACFDPNA | AKTLWERMDA | AEGQMGKALA | FASTHPSSKK |
| 310 | 320 | 330 | |||
| RIRKIEEWLP | EAQVKRETSD | CYHETWPMLQ | SFKEVHW |