Q9R6X3
Gene name |
bphB (all2899) |
Protein name |
Cyanobacterial phytochrome B |
Names |
|
Species |
Nostoc sp (strain PCC 7120 / SAG 2582 / UTEX 2576) |
KEGG Pathway |
ana:all2899 |
EC number |
2.7.13.3: Protein-histidine kinases |
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 Q9R6X3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9R6X3-F1 | Predicted | AlphaFoldDB |
No variants for Q9R6X3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9R6X3 | |||||
No associated diseases with Q9R6X3
7 regional properties for Q9R6X3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | GAF domain | 152 - 330 | IPR003018 |
| domain | Histidine kinase/HSP90-like ATPase | 639 - 751 | IPR003594 |
| domain | Signal transduction histidine kinase, dimerisation/phosphoacceptor domain | 527 - 597 | IPR003661 |
| domain | Histidine kinase domain | 536 - 751 | IPR005467 |
| domain | Phytochrome, central region | 332 - 513 | IPR013515 |
| domain | PAS fold-2 | 17 - 124 | IPR013654 |
| domain | Phytochrome chromophore attachment domain | 152 - 310 | IPR016132 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.13.3 | Protein-histidine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| phosphorelay sensor kinase activity | Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response. |
| photoreceptor activity | The function of absorbing and responding to incidental electromagnetic radiation, particularly visible light. The response may involve a change in conformation. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| detection of visible light | The series of events in which a visible light stimulus is received by a cell and converted into a molecular signal. A visible light stimulus is electromagnetic radiation that can be perceived visually by an organism; for organisms lacking a visual system, this can be defined as light with a wavelength within the range 380 to 780 nm. |
| regulation of DNA-templated transcription | Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNINDITIPF | QVDLSNCSKE | PIHIPGLIQP | HGVLLVLQEV | DLTILQVSNN | TFNILGRHPE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QLLNQHLSCL | LEAEQLSLLK | DCLAQEDLQI | INPLEFIIKS | HNESISFDVI | AHRSNNLLIL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ELEANLSDKT | HSFFRFYHLV | KLAMLKLQGT | ATTTEISQIL | AQEVRKITGF | DRVMVYRFDE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QWNGKVIAEV | KPEYLTSYLG | LNYPASDIPQ | QARKLYSQNW | LRLIPDAKYQ | PVPIVPINNP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LNDQPLDLSR | SVLRSVSPLH | IEYMQNMGVT | ASMSISIMKN | QKLWGLIACH | HQSPKYIPYE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IRSACEFLGQ | MTSVEMSAKE | DSEDTEDKIQ | VKSVHSKLVQ | YMSAENDFIN | ALIDHQPNIL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DLVKAQGAAV | CFNGNSCTVG | QVPPMPDIQV | LVEWMSQNIH | EEIFATDSLA | TVYPDAEKLR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DVASGLIALS | ISRSQKNYIL | WFRPEVVRTV | DWGGNPHKPV | EVIANGEIRL | SPRKSFDLWK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ETVLLKSQPW | KSHEVNAALE | LRSAIIGIVL | QKADELAQLN | IELERSNQEL | DAFAYIASHD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LKEPLRGIHN | YSNFLMEDYG | EIIDAPGKEK | LLTLIRLTQR | MEDLIDSLLH | FSRLGRVDLS |
| 610 | 620 | 630 | 640 | 650 | 660 |
| MQDTDLNEIV | HRILDMLSGR | IEETGVEIRI | LQLLPVVYCD | RIQIGEVFSN | LIANSIKYND |
| 670 | 680 | 690 | 700 | 710 | 720 |
| KANKWIEIGY | IDNPPLPPTF | YVRDNGIGIR | EKHFETIFRI | FKRLHSPSKY | GGGTGAGLTI |
| 730 | 740 | 750 | |||
| AKKIVERHGG | KIWVESTYGE | GSTFYFTLQD | V |