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 Q6UEF1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6UEF1-F1 | Predicted | AlphaFoldDB |
No variants for Q6UEF1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6UEF1 | |||||
No associated diseases with Q6UEF1
No regional properties for Q6UEF1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q6UEF1 | |||
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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 |
|---|---|
| aflatoxin biosynthetic process | The chemical reactions and pathways resulting in the formation of aflatoxin, a fungal metabolite found as a contaminant in moldy grains that induces liver cancer. Aflatoxin induces a G to T transversion at codon 249 of p53, leading to its inactivation. Aflatoxin is converted to a chemical carcinogen by P450. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGSHAPAVAG | KPDPKKGPYQ | ATPWNIQLSA | TDTPGFTHVG | NLERRSADRA | SDLVMNNHSK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FHTFHDEIVG | FHNHISHHVL | TLWALGATPD | EMQAAYDFNK | PFQLLTYYND | PSVNIKLRDP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EFFRQGLGNF | ELYGDYVRFF | QAEVAAKGTQ | TVLHDYLFKG | DTLTEDLLAR | LFSGFLHPLI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NLGFALEFQQ | PFLAAECLAS | TCMHPPYPAE | FLTATEQHVE | CNGRPRSLPI | LSIAEGMRLD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PVVATAVGPE | DGNNRIADAL | LKRALKELIP | HLSYFQVEPT | EHDLARKTAE | ILQASAYICG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AAQHPRKVEA | LDFVMLHSLT | AAVFFPTIIK | QEWISIETRA | RLLEWKGRSD | LITYAALGCP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KLYPDRITGY | QPKQAATGWS | DVVQRARVYQ | DDGHACKVIR | ALMCAENVCQ | PFEGEEGFPL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KKADFLTVAH | MTMDSVERMS | DPNWVRQTEK | VKQMSAQGRG | QHSQVSAIML | RWVRWCGTEG |
| 490 | |||||
| AWDDFPDLEE | LSPSA |