Q4WPF8
Gene name |
ccp1 (AFUA_4G09110) |
Protein name |
Cytochrome c peroxidase, mitochondrial |
Names |
CCP |
Species |
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
KEGG Pathway |
afm:AFUA_4G09110 |
EC number |
1.11.1.5: Peroxidases |
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 Q4WPF8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q4WPF8-F1 | Predicted | AlphaFoldDB |
No variants for Q4WPF8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q4WPF8 | |||||
No associated diseases with Q4WPF8
Functions
| Description | ||
|---|---|---|
| EC Number | 1.11.1.5 | Peroxidases |
| 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 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| cytochrome-c peroxidase activity | Catalysis of the reaction: 2 ferrocytochrome c + hydrogen peroxide = 2 ferricytochrome c + 2 H2O. |
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| metal ion binding | Binding to a metal ion. |
| peroxidase activity | Catalysis of the reaction: a donor + a peroxide = an oxidized donor + 2 H2O. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to oxidative stress | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. |
| hydrogen peroxide catabolic process | The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2). |
| response to reactive oxygen species | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASAARSASR | AFLRSTPTTS | SFRPAVRAAR | FALPAQGFRA | AGRRGYASEA | NSGKSSSNVF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LWAGLAVAGG | AGAYLYLNGS | DSVTSKTFVP | GKEDYQKVYD | AIARRLADET | DYDDGSYGPV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LVRLAWHASG | TYDKETGTGG | SNGATMRFAP | ESDHGANAGL | KIARDFLEPI | KAQFPWISYS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DLWTLAGACA | IQELGGPTIP | WRPGRQDKDV | AACTPDGRLP | DASKDQRHIR | DIFYRMGFND |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QEIVALIGAH | ALGRAHPDRS | GYDGPWDFSP | TVFTNEFFRL | LVDEKWQNRK | WNGPAQFTDK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TTKTLMMLPA | DLALIKDKEF | KKHVERYARD | SDAFFKDFSD | AFVKLLELGV | PFTSKAEDRY |
| VFKTSE |