Q5HB88
Gene name |
nuoD |
Protein name |
NADH-quinone oxidoreductase subunit D |
Names |
NADH dehydrogenase I subunit D, NDH-1 subunit D |
Species |
Ehrlichia ruminantium (strain Welgevonden) |
KEGG Pathway |
erw:ERWE_CDS_04620 |
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 Q5HB88
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5HB88-F1 | Predicted | AlphaFoldDB |
No variants for Q5HB88
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5HB88 | |||||
No associated diseases with Q5HB88
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| NAD binding | Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. |
| NADH dehydrogenase (quinone) activity | Catalysis of the reaction: NADH + H+ + a quinone = NAD+ + a quinol. |
| 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. |
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 |
| MSDHVKITPM | TLNFGPQHPA | AHGVMRLVLE | MGGEVIERID | PHIGLLHRGT | EKLIEYKTYL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QALPYFDRLD | YVSPMAQEHA | YSLCVEKLLK | CEVPIRAKYL | RVIFCELTRI | LNHLLNISSQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ALDIGAMTPL | LWMFEEREKI | LNFYERASGA | RFHSAYIRPG | GVAADIPEDL | IHDIFQFVNT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FPKFMDDVDS | LLTENRIWKQ | RNVDIGVVSK | KQALNWGFSG | PMLRACGIPW | DLRKSQPYEI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YDELEFKIPI | GEKGDCYDRY | LVRMAEIRES | IRLVEQCLNR | IPDGPVKTDD | RKIAPPKRSE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MKKSMEALIH | HFKLYSEGYS | VPAGETYMAV | EAPKGEFGVY | IVSDGTNKPY | RCRIRAPGFA |
| 370 | 380 | 390 | |||
| HLQAIDMMAK | GHMLADLTAI | IGSLDIVFGE | IDR |