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 O06465
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O06465-F1 | Predicted | AlphaFoldDB |
No variants for O06465
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O06465 | |||||
No associated diseases with O06465
5 regional properties for O06465
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| active_site | Pyridine nucleotide-disulphide oxidoreductase, class-II, active site | 344 - 364 | IPR008255 |
| domain | Thioredoxin-like fold | 125 - 195 | IPR012336 |
| domain | FAD/NAD(P)-binding domain | 213 - 503 | IPR023753 |
| domain | AhpF, N-terminal domain, C-terminal TRX-fold subdomain | 106 - 194 | IPR044141 |
| domain | AhpF, N-terminal domain, N-terminal TRX-fold subdomain | 1 - 95 | IPR044142 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| alkyl hydroperoxide reductase activity | Catalysis of the reaction: octane hydroperoxide + NADH + H+ = H2O + NAD+ + 1-octanol. |
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
| 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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| response to reactive oxygen species | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLDANLKTQL | TAYLERVTRP | IQINASIDDS | AGSREMLDLL | EELVLLSDKI | SLDIHRDDNQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RKPSFALTTP | GQDISLRFAG | LPMGHEFTSL | VLALLQVGGH | PSKAAAELIE | QVQHLEGDYQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FETYFSLSCQ | NCPDVVQALN | LAAVLNPRIK | HVAIDGAWFQ | DEVQARQIMS | VPTVYLNGEL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FDQGRMTLEQ | IVAKLDTNAA | KRDAAKIAAK | EAFDVLVVGG | GPAGSAAAVY | AARKGIRTGV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AAERFGGQVL | DTMSIENFIS | VPETEGPKMA | AALEQHVRQY | DVDIMNLQRA | EQLIPAGADG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LIEIKLANGA | SLKSKTVILS | TGARWRQMNV | PGEDQYKNKG | VAYCPHCDGP | LFKGKRVAVI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GGGNSGVEAA | IDLAGIVAHV | TLVEFDDKLR | ADEVLQRKLR | SLHNVRIITS | AQTTEVLGDG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QKVTGLVYKD | RTGGDIQHIE | LEGVFVQIGL | LPNTEFLRGT | VALSPRGEII | VDDRGQTDVP |
| 490 | 500 | 510 | 520 | ||
| GVFAAGDATT | VPYKQIVIAM | GEGSKAALSA | FDHLIRTSAP | ATADSVAQAA |