Q8SQR8
Gene name |
SSE1 (ECU11_1830) |
Protein name |
Heat shock protein homolog SSE1 |
Names |
|
Species |
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) |
KEGG Pathway |
ecu:ECU11_1830 |
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 Q8SQR8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8SQR8-F1 | Predicted | AlphaFoldDB |
No variants for Q8SQR8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8SQR8 | |||||
No associated diseases with Q8SQR8
No regional properties for Q8SQR8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q8SQR8 | |||
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
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. |
| calmodulin binding | Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. |
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 |
| MEFVGIDIGN | YKTVIASSKE | NGKVYGDEQG | KRSIRTVMEL | STPVRRFGNG | VTNDVEQSLD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LRSRSFRDAL | EDKKGWGNLA | MFMKYIDRVV | KKNTPTHPPI | CMAVPAYFKE | RERRILVDIA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NTMDFKLEGL | ITDISAIAMF | ACVRRENMPS | EFLLFDFGFS | KTTAGLFSFE | KNVLKPLYMK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TVRVGSMQFD | EKLIDIIVEK | HSLEKSRLVR | EKIKRNLDKI | KTTLNSTKCC | NIQLFITENP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LEVIITQEEY | RNAVKSYLSD | LDSFVSSVIK | ETEFNGLVEV | VGGNSISFLI | KEMLRDKVEY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QVTLDVSDST | AIGAALGMAC | MSLRTRYSLH | DIVGREISIR | IQGEDVSPTV | IFKSTELVEG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NPKIVTYNRK | ESFVLEILED | GEVISTLNVV | KGETKETKAI | HVSFSIGKFG | TVCVNSVECE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ESVDYEYKPF | RISDIDLDDI | KALEMKYRDG | ELGLERIGTM | RNELETMAVG | LGDALYNKFG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KITNDEELNT | VREVAMDLFD | MPQSETVGQE | EEVRNTILSK | LEFISKKLSD | YRDAAVEDLK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KHKDMINEFR | KEYGSVFTPS | FYKLQGLLYK | VDEYLKDFDL | NLFNVKLFDE | SFIMEIKGDI |
| 610 | 620 | 630 | 640 | 650 | |
| QKYLEKAKLE | IEEKRKEEER | KSKKENAQEG | TSSKPESKEE | SEAKEDNDEE | SDVASIDE |