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 O69268
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O69268-F1 | Predicted | AlphaFoldDB |
No variants for O69268
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O69268 | |||||
No associated diseases with O69268
3 regional properties for O69268
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Heat shock protein 70, conserved site | 7 - 14 | IPR018181-1 |
| conserved_site | Heat shock protein 70, conserved site | 166 - 179 | IPR018181-2 |
| conserved_site | Heat shock protein 70, conserved site | 307 - 321 | IPR018181-3 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP-dependent protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
| unfolded protein binding | Binding to an unfolded protein. |
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 |
| MSKIIGIDLG | TTNSCVSVLE | GGEPKVIPNP | EGNRTTPSVV | AFKNGERQVG | EVAKRQSVTN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PNTIISIKSK | MGTAEKVTVE | DKDYTPQEVS | AMILQYLKGY | AEDYLGEKVT | KAVITVPAYF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NDAQRQATKD | AGKIAGLEVE | RIINEPTAAA | LRYGLDKQDQ | DQKVLVFDLG | GGTFDVSILE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LGDGVFEVLA | TAGDNKLGGD | DFDDAIIEYL | VAEFKKENGI | DLSKDKMAMQ | RLKDAAEKAK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KDLSGVTSTQ | ISLPFITAGE | AGPLHLEISL | TRAKFDEITL | PLVNRTVGPV | RQALSDAGLS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TSEIDQVILV | GGSTRIPAVQ | EAVRKETNKE | PHRGVNPDEV | VAMGAAVQGG | VLTGDVKDVV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LLDVTPLSLG | IETMGGVFTK | LIDRNTTIPT | SKSQVFSTAA | DNQPAVDIHV | LQGERSMAAD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NKTLGRFQLA | DIPPAPRGVP | QIEVTFDIDK | NGIVSVKAKD | LGTNKEQTIV | IQSDSGLSEA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EIERMVKDAE | ANRDADAKRK | EEADLRNEAD | QLVFQVDKTI | TDLGEQITED | EKKSVEDARD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ELKKALEAGE | LEGIKAAKEK | LEGVLQPLVM | KVYEQAAAAA | QARQGGEADA | GAGKKDDGVV |
| 610 | |||||
| DADFEEVKDD | K |