Q753X4
Gene name |
01-Oct (AFR198W) |
Protein name |
Mitochondrial intermediate peptidase |
Names |
MIP, Octapeptidyl aminopeptidase |
Species |
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) |
KEGG Pathway |
ago:AGOS_AFR198W |
EC number |
3.4.24.59: 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 Q753X4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q753X4-F1 | Predicted | AlphaFoldDB |
No variants for Q753X4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q753X4 | |||||
No associated diseases with Q753X4
1 regional properties for Q753X4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase M3A/M3B catalytic domain | 299 - 766 | IPR001567 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.24.59 | Metalloendopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
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. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular iron ion homeostasis | Any process involved in the maintenance of an internal steady state of iron ions at the level of a cell. |
| peptide metabolic process | The chemical reactions and pathways involving peptides, compounds of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. |
| 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. |
| protein stabilization | Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MFVRFYKRLD | RQYIQSQRRW | ILSSNKCLLQ | GNKNATISPL | RRAFDDQDHW | EESQAQNTSS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EQDNKGKNSS | YFWSRSKATA | PQVAHTGLFQ | NPYLNSPEGL | RKFANKSLTE | ATALVRNLRE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DSSQEGLVRY | IIRLDQLSDI | LCRVIDLCEF | LRAAHPDEQF | VAAAQECHEQ | MFEIMNILNT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DVVLCKRLKQ | VLSDENISSK | LSSEEIRVGH | ILLEDFEKAG | AYASPEVRKQ | FIQLSQNISI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IGQDFINNTE | SLSSSYIKIP | CKDLESSGTS | HLVLRQLTKD | TMGNNYKIPT | SGYAPYTLLN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ACPSEAIRRQ | VWTAMFSCSE | KQVKRLKSLL | QLRRKLANIM | GATDYVSYQL | EGKMAKSPEN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VKNFLNTLVD | HTKPLAAGEL | EELAKLKRNV | ENLSETNTLK | LMRPWDRDYY | SSLSPNFTRP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NHRVDGFTSI | NTYFSLGVVM | QGISDLFRDI | YGISLKPVVA | QAGETWAPDV | RKLQVISETE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GIIGLIYCDL | LERPGKTTSP | SHFTVCCSRQ | IYPEENDFST | IQVGENPDGS | RFQMPVISLI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| CNFRATRHGK | NKSLCLLELS | DVETLFHEMG | HALHSMLGRT | QLQNLSGTRC | VTDFVELPSI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LMEHFAKDRR | VLLRISSNYA | TGEPIPEELL | SAFQEQNNFL | KNTETFSQIK | MSMLDQRLHS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| ITDQDDIIAV | YHGLEREMEV | LVDDQTNWCG | RFGHLFGYGA | SYYSYLMDRA | IAAKIWDHLF |
| 730 | 740 | 750 | 760 | 770 | |
| KKDPFSRSSG | EKFKEGVLKW | GGSRDAWQCI | ADALDEPRLV | KGDDWAMRFI | GEVEDM |