Q57557
Gene name |
MJ0092 |
Protein name |
Uncharacterized iron-sulfur protein MJ0092 |
Names |
|
Species |
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) |
KEGG Pathway |
mja:MJ_0092 |
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 Q57557
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q57557-F1 | Predicted | AlphaFoldDB |
No variants for Q57557
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q57557 | |||||
No associated diseases with Q57557
7 regional properties for Q57557
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | 2Fe-2S ferredoxin-type iron-sulfur binding domain | 2 - 84 | IPR001041 |
| domain | Cysteine-rich domain | 262 - 345 | IPR004017-1 |
| domain | Cysteine-rich domain | 377 - 460 | IPR004017-2 |
| binding_site | 2Fe-2S ferredoxin, iron-sulphur binding site | 48 - 56 | IPR006058 |
| domain | 4Fe-4S ferredoxin-type, iron-sulphur binding domain | 123 - 205 | IPR017896 |
| conserved_site | 4Fe-4S ferredoxin, iron-sulphur binding, conserved site | 186 - 197 | IPR017900 |
| domain | Succinate dehydogenase/fumarate reductase N-terminal | 4 - 98 | IPR025192 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2 iron, 2 sulfur cluster binding | Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| electron transfer activity | Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient. |
| metal ion binding | Binding to a metal ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| tricarboxylic acid cycle | A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIKITVKRFN | GEKEYLESYE | VPENITVLEA | LEYINKHYEA | NILFRASCRN | AQCGSCAVTI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NGEPRLACET | KVEDGMIIEP | LRGFKVIRDL | IVDREPYYKK | LLGIKNYLIR | KNYPEELEIL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IPKYVEENKE | LRGCIDCLSC | LSVCPAREVS | DYPGPTFMRQ | LARFAFDKRD | EDGREITAYF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ENIYNCTTCA | KCVEVCPKEI | DIVHRAIEKL | RALAFSKGYY | IENHLKVREN | VLKYNRSVVE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EELPLLKQVA | DFYPAESEKL | RVAFFTGCLV | DFRLQNVGKD | AIKVLNAHGV | SVVIPKNQVC |
| 310 | 320 | 330 | 340 | 350 | 360 |
| CGSPFFRTGQ | RDVAEMLKRK | NLEIFNKLDV | DCVVTICAGC | GSTLKNDYKE | RKFEVKDITE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VLTEVGLLKY | KPLKMRITYH | DPCHLRRGQK | IYKQPREILK | SIPELEFIDI | EARCCGAGGG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VRSGKPDIAN | LIGKSRARMI | YDANVDAVIT | VCPFCEYHIR | DSLKRFKEEN | KIDKEIDVMN |
| IVSLLAKVI |