Q8EBC3
Gene name |
cysA1 |
Protein name |
Sulfate/thiosulfate import ATP-binding protein CysA 1 |
Names |
Sulfate-transporting ATPase 1 |
Species |
Shewanella oneidensis (strain MR-1) |
KEGG Pathway |
son:SO_3602 |
EC number |
7.3.2.3: Linked to the hydrolysis of a nucleoside triphosphate |
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 Q8EBC3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8EBC3-F1 | Predicted | AlphaFoldDB |
No variants for Q8EBC3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8EBC3 | |||||
No associated diseases with Q8EBC3
5 regional properties for Q8EBC3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ABC transporter-like, ATP-binding domain | 3 - 237 | IPR003439 |
| domain | AAA+ ATPase domain | 27 - 214 | IPR003593 |
| domain | Sulphate transport system permease protein 1 | 1 - 242 | IPR005666 |
| conserved_site | ABC transporter-like, conserved site | 137 - 151 | IPR017871 |
| domain | TOBE-like domain | 287 - 346 | IPR024765 |
Functions
| Description | ||
|---|---|---|
| EC Number | 7.3.2.3 | Linked to the hydrolysis of a nucleoside triphosphate |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| ATP-binding cassette (ABC) transporter complex | A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ABC-type sulfate transporter activity | Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + sulfate(out) = ADP + phosphate + sulfate(in). |
| ABC-type thiosulfate transporter activity | Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + thiosulfate(out) = ADP + phosphate + thiosulfate(in). |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| sulfate transport | The directed movement of sulfate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSIRLTNISK | KFGQFQALSP | LNLDIQEGEM | IGLLGPSGSG | KTTLLRIIAG | LEGADSGHIH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FGNRDVTQVH | VRDRRVGFVF | QNYALFRHMT | VADNVAFGLE | VIPKKQRPSA | AEIQKRVSHL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LEMVQLGHLA | QRYPEQLSGG | QKQRIALARA | LATQPEVLLL | DEPFGALDAK | VRKELRRWLR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SLHDELKFTS | VFVTHDQDEA | LELSDRVVVM | SNGNIEQVNT | PIELYAQPNS | RFVFDFLGNV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NRFEANWQQN | RWTNGDAFIV | PPEQTPLQQN | GALYVRSHEL | ALADKPNSQA | HIPFTIVAIT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PIGAEVRVEL | APIGWQSEEL | WEAKFTHHHL | QELGLQKGSV | VYATPRTGYF | FGKQGDGSPI |
| 370 | |||||
| RQSWPFLPPG | SLAFDI |