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 P30609
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P30609-F1 | Predicted | AlphaFoldDB |
No variants for P30609
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P30609 | |||||
No associated diseases with P30609
1 regional properties for P30609
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Cytochrome P450, conserved site | 449 - 458 | IPR017972 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| iron ion binding | Binding to an iron (Fe) ion. |
| oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen | Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from reduced flavin or flavoprotein and one other donor, and one atom of oxygen is incorporated into one donor. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIEQVLHYWY | YVLPAFIIFH | WIVSAIHTNS | LRRKLGAKPF | THTQLDGFYG | FKFGRDFLKA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KRIGRQVDLI | NSRFPDDIDT | FSSYTFGNHV | IFTRDPENIK | ALLATQFNDF | SLGGRIKFFK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PLLGYGIFTL | DGEGWKHSRA | MLRPQFAREQ | LPMSPSLEPH | FNVKAYPQEQ | RWVFDIQELF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FRFTVDSATE | FLFGESVNSL | KSASIGCDEE | TELEERKKFA | EAFNKAQEYI | STRVALQQLY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| WFVNNSEFKE | CNEIVHKFTN | YYVQKALDAT | PEELEKQSGY | VFLYELVKQT | RDPNVLRDHH |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SISLLAGRDT | TAGLLSFAVF | ELARNPHIWA | KLREDVESQF | GLGEESRIEE | ITFESLKRCE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YLKAVMNETL | RLHPSVPRNA | RFALKDTTLP | RGGGPDGKDP | ILVRKMSCSI | FISGTQIDPK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HYGKDAKLFR | PERWFESSTR | NLGWAYLPFN | GGPRICLGQQ | FALTEAGYIL | VRLAQSFDTL |
| 490 | 500 | ||||
| ELKPDTEYLT | KISHLTMCLF | GAFVKMD |