Q5REK3
Gene name |
PMPCB |
Protein name |
Mitochondrial-processing peptidase subunit beta |
Names |
Beta-MPP |
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100174253 |
EC number |
3.4.24.64: Metalloendopeptidases |
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 Q5REK3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5REK3-F1 | Predicted | AlphaFoldDB |
No variants for Q5REK3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5REK3 | |||||
No associated diseases with Q5REK3
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.24.64 | Metalloendopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial processing peptidase complex | A protein complex consisting of a regulatory subunit (alpha-MPP) and a catalytic subunit (beta-MPP) that catalyzes the release of N-terminal targeting peptides from precursor proteins imported into the mitochondrion. |
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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAAAAARVVL | LPAARRRLWG | FSESLLIRGA | AGRSSYFGEN | RLRSTQAATQ | VVLNVPETRV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TCLESGLRVA | SEDSGLSTCT | VGLWIDAGSR | YENEKNNGTA | HFLEHMAFKG | TKKRSQLDLE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LEIENMGAHL | NAYTSREQTV | YYAKAFSKDL | PRAVEILADI | IQNSTLGEAE | IERERGVILR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EMQEVETNLQ | EVVFDYLHAT | AYQNTALGRT | ILGPTENIKS | ISRKDLVDYI | TTHYKGPRIV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LAAAGGVSHD | ELLDLAKFHF | GDSLCTHKGE | IPALPPCKFT | GSEIRVRDDK | MPLAHLAIAV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EAVGWAHPDT | ICLMVANTLI | GNWDRSFGGG | MNLSSKLAQL | TCHGNLCHSF | QSFNTSYTDT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GLWGLYMVCE | PSTVADMLHV | VQKEWMRLCT | SVTESEVARA | RNLLKTNMLL | QLDGSTPICE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DIGRQMLCYN | RRIPIPELEA | RIDAVNAETI | REVCTKYIYN | RSPAIAAVGP | IEQLPDFKQI |
| CSNMCWLRD |