Q4UK22
Gene name |
nuoG (RF_1262) |
Protein name |
NADH-quinone oxidoreductase subunit G |
Names |
NADH dehydrogenase I subunit G, NDH-1 subunit G |
Species |
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi) |
KEGG Pathway |
rfe:RF_1262 |
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 Q4UK22
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q4UK22-F1 | Predicted | AlphaFoldDB |
No variants for Q4UK22
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q4UK22 | |||||
No associated diseases with Q4UK22
8 regional properties for Q4UK22
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site | 31 - 48 | IPR000283-1 |
| conserved_site | NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site | 98 - 110 | IPR000283-2 |
| conserved_site | NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site | 145 - 155 | IPR000283-3 |
| domain | 2Fe-2S ferredoxin-type iron-sulfur binding domain | 1 - 78 | IPR001041 |
| domain | Molybdopterin oxidoreductase | 271 - 585 | IPR006656 |
| domain | Molybdopterin oxidoreductase, 4Fe-4S domain | 215 - 271 | IPR006963 |
| domain | NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial-like | 623 - 659 | IPR015405 |
| domain | NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding | 78 - 123 | IPR019574 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
5 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. |
| metal ion binding | Binding to a metal ion. |
| NADH dehydrogenase (ubiquinone) activity | Catalysis of the reaction: NADH + ubiquinone + 5 H(+)(in) <=> NAD(+) + ubiquinol + 4 H(+)(out). |
| quinone binding | Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| ATP synthesis coupled electron transport | The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIKLNIDGSE | IEVSEGSTVY | QACTQAGKEI | PHFCYHERLK | IAGNCRMCLV | EMEKSPKPIA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SCAMPVSNGM | VIHTDTPMVK | KAREGVMEFL | LINHPLDCPI | CDQGGECDLQ | DQAFRYGKGT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NRFHENKRSI | KDKYMGPLIK | TAMTRCIQCT | RCIRFANDIA | GIEEMGAIHR | GEHMEVTSYL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EQTLDSEMSG | NMIDICPVGA | LNSKPYAFKA | RKWELKHTAS | IGVHDAEGSN | IRIDSRGDEV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MRILPRVNEE | INEEWLSDKN | RFSYDGLKYQ | RLDLPYIRKN | GKLVEASWSE | ALKTIADKIK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SVKPEKIAAI | AGSLVSVEAM | FMLKTLLQKL | GSNNYSVNQF | DYKFDTTQRG | NYLFNTTIAG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VEKADLCLLI | GANLRQIAPV | LNSRIGQRVR | AGSLKVARIG | EGHNQTYRIQ | DLGSDIKIIE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ELAIGTHEFT | KALKAAKYPM | IIVGDGVYAR | DDGYAILSLI | HKIVAEYNIM | RDDFQGFNML |
| 490 | 500 | 510 | 520 | 530 | 540 |
| HNHASIVGGL | DIGFNTPIKL | EELELTYLLG | ADELPFDKLK | SAFIIYQGHH | GDSGAANADV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ILPAAAYTEQ | SGIYVNLEGR | PQIAEKAVAP | VGVAKEDIEI | IKELAGSLKI | DIGMDNLQEV |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RVRLAKEYKI | FANIDKIVES | KFAKFSFKDK | LSKEPITMGP | INYYMTDVIS | KNSVTMAKCV |
| 670 | |||||
| EAKEKRNERA | A |