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 P20069
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P20069-F1 | Predicted | AlphaFoldDB |
No variants for P20069
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P20069 | |||||
No associated diseases with P20069
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. |
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. |
| 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. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| protein processing | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. |
| protein processing involved in protein targeting to mitochondrion | The cleavage of peptide bonds in proteins, usually near the N terminus, contributing to the process of import into the mitochondrion. Several different peptidases mediate cleavage of proteins destined for different mitochondrial compartments. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9DC61 | Pmpca | Mitochondrial-processing peptidase subunit alpha | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATAVWAAAR | LLRGSAALCA | RPKFGSPAHR | RFSSGATYPN | IPLSSPLPGV | PKPIFATVDG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QEKFETKVTT | LDNGLRVASQ | NKFGQFCTLG | ILINSGSRYE | AKYLSGIAHF | LEKLAFSSTA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RFDSKDEILL | TLEKHGGICD | CQTSRDTTMY | AVSADSKGLD | TVVGLLADVV | LHPRLTDEEI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EMTRMAVQFE | LEDLNMRPDP | EPLLTEMIHE | AAFRENTVGL | HRFCPVENIG | KIDREVLHSY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LKNYYTPDRM | VLAGVGVEHE | HLVECARKYL | LGVQPAWGAP | GAVWMLTAQW | HSTRGGSSRW |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RETCQMSALR | PPRFQSSHIY | GGARELLLLE | EDFIPFAVLN | MMMGGGGSFS | AGGPGKGMFS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RLYLNVLNRH | HWMYNATSYH | HSYEDTGLLC | IHASADPRQV | REMVEIITKE | FILMGRTVDL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VELERAKTQL | MSMLMMNLES | RPVIFEDVGR | QVLATHSRKL | PHELCTLIRN | VKPEDIKRVA |
| 490 | 500 | 510 | 520 | ||
| SKMLRGKPAV | AALGDLTDLP | TYEHIQAALS | SRDGRLPRTY | RLFR |