Q68FS6
Gene name |
Pyroxd1 |
Protein name |
Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 |
Names |
|
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:297708 |
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 Q68FS6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q68FS6-F1 | Predicted | AlphaFoldDB |
No variants for Q68FS6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q68FS6 | |||||
No associated diseases with Q68FS6
3 regional properties for Q68FS6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | FAD/NAD(P)-binding domain | 10 - 202 | IPR023753-1 |
| domain | FAD/NAD(P)-binding domain | 287 - 381 | IPR023753-2 |
| domain | NADH-rubredoxin oxidoreductase, C-terminal | 409 - 476 | IPR041575 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| sarcomere | The repeating unit of a myofibril in a muscle cell, composed of an array of overlapping thick and thin filaments between two adjacent Z discs. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
| oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. |
1 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEAARPAGTF | VVVGGGIAGV | TCAEQLAINF | PAEDILLVTA | SPVIKAVTNF | KQVSKVLEEF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DVEEQPSTML | ENRFPNIKVI | ESGVKQLKSD | KHCIFTEDGR | EYVYKKLCLC | AGAKPKLICE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GNPYVLGIRD | TDSAQEFQKQ | LTKARRIMIV | GNGGIALELA | YEVEVCEVIW | AIKDKAIGNT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FFDAGAAEFL | TSRLLSEKSE | AKLAHKRTIY | TVEEAKKETS | TKSKADYVGS | ALGPDWHGGL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ALKGTEEFSH | SIHIETKCEV | KKIYLQEEFK | IMKKKSLAFP | KDHHKSVTVD | KEMWPVYVEL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TNGSIYGCDF | LVSATGVTPN | VQPFLHGNDF | DLGEDGGLRV | DEQMRTSLPD | IYAAGDICTA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| CWPPSPVWQQ | MRLWTQARQM | GCYAAKCMAA | ATMGHPIDMD | FSFELFAHVT | KFFNYKVVLL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GKYNAQGLGV | DHELMLRCTR | GQEYIKVVMH | NGRMMGAVLI | GETDLEETFE | NLILNQMDLS |
| 490 | |||||
| SYGEDLLNPD | IDIEDYFD |