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 Q9FUM1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9FUM1-F1 | Predicted | AlphaFoldDB |
No variants for Q9FUM1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9FUM1 | |||||
No associated diseases with Q9FUM1
4 regional properties for Q9FUM1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | 3-hydroxyacyl-CoA dehydrogenase, C-terminal | 492 - 585 | IPR006108 |
| domain | 3-hydroxyacyl-CoA dehydrogenase, NAD binding | 311 - 489 | IPR006176 |
| conserved_site | 3-hydroxyacyl-CoA dehydrogenase, conserved site | 489 - 513 | IPR006180 |
| conserved_site | Enoyl-CoA hydratase/isomerase, conserved site | 103 - 123 | IPR018376 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| glutathione transferase activity | Catalysis of the reaction: R-X + glutathione = H-X + R-S-glutathione. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. |
| translation elongation factor activity | Functions in chain elongation during polypeptide synthesis at the ribosome. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| response to chemical | 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 chemical stimulus. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MALVLHAGKT | NKNAFKTLIV | AEYTGVKVEL | APDFEMGVTN | KTPEYLKLNP | IGKVPLLETP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DGPIFESNAI | ARYVARLKAD | NPLIGSSLID | YAHIEQWIDF | GSLEIDANII | SWFRPRFGYA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VYLPPAEEAA | ISALKRALGA | LNTHLASNTY | LVGHFVTLAD | IIVTCNLFFG | FTKLMIKSFT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SEFPHVERYF | WTLVNQPKFK | KVLGDVKQTE | SVPPVPSAKK | PSQPKETKSK | AKEEPKKEAK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KEPAKPKAEA | AEEVEEAPKP | KPKNPLDLLP | PSNMVLDDWK | RLYSNTKTNF | REVAIKGFWD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MYDPEGYSLW | FCEYKYNDEN | TVSFVTLNKV | GGFLQRMDLA | RKYAFGKMLV | IGSEPPFKVK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GLWLFRGQEI | PPFVMEECYD | MELYNWTKVD | LSDENQKERV | NQVIEDQEPF | EGEALLDAKC |
| FK |