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 P93528
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P93528-F1 | Predicted | AlphaFoldDB |
No variants for P93528
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P93528 | |||||
No associated diseases with P93528
12 regional properties for P93528
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PAS domain | 618 - 741 | IPR000014-1 |
| domain | PAS domain | 748 - 873 | IPR000014-2 |
| domain | GAF domain | 216 - 409 | IPR003018 |
| domain | Histidine kinase/HSP90-like ATPase | 1007 - 1122 | IPR003594 |
| domain | Signal transduction histidine kinase, dimerisation/phosphoacceptor domain | 896 - 959 | IPR003661 |
| domain | Histidine kinase domain | 902 - 1122 | IPR005467 |
| domain | Phytochrome, central region | 412 - 587 | IPR013515 |
| domain | PAS fold-2 | 68 - 183 | IPR013654 |
| domain | PAS fold | 621 - 734 | IPR013767-1 |
| domain | PAS fold | 751 - 873 | IPR013767-2 |
| domain | Phytochrome chromophore attachment domain | 216 - 389 | IPR016132 |
| domain | Phytochrome A/B/C/D/E-like, histidine-kinase-related domain | 1006 - 1118 | IPR044767 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
4 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. |
| protein-tetrapyrrole linkage | The covalent linking of a tetrapyrrole to a protein. |
| red, far-red light phototransduction | The sequence of reactions within a cell required to convert absorbed photons from red or far-red light into a molecular signal; the red, far-red light range is defined as having a wavelength within the range 660-730 nm. |
| regulation of DNA-templated transcription | Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P14714 | PHYC | Phytochrome C | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSPLNNRGT | CSRSSSARSR | HSARVVAQTP | VDAQLHAEFE | SSQRNFDYSS | SVSAAIRPSV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| STSTVSTYHQ | TMQRGLYIQP | FGCLLAVHPD | TFTLLAYSEN | APEMLDLTPH | AVPTIDQRDA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LAVGADVRTL | FRSQSSVALH | KAATFGEVNL | LNPILVHART | SGKPFYAILH | RIDVGLVIDL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EPVNPVDVPV | TAAGALKSYK | LAAKAISRLQ | SLPSGNLSLL | CDVLVREVSE | LTGYDRVMAY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KFHEDEHGEV | ISECRRSDLE | PYLGLHYPAT | DIPQASRFLF | MKNKVRMICD | CSATLVKIIQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DDSLAQPLSL | CGSTLRASHG | CHAQYMANMG | SVASLVMSVT | ISNDEEEDVD | TGSDQQPKGR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KLWGLVVCHH | TSPRFVPFPL | RYACEFLLQV | FGIQLNKEVE | LAAQAKERHI | LRTQTLLWDM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LLRDAPVGIF | TQSPNVMDLV | KCDGVALYYQ | NQLLLLGSTP | SESEIKSIAT | WLQENHDGST |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GLSTDSLVEA | GYPGAAALRE | VVCGMAAIKI | SSKDFIFWFR | SHTTKEIKWG | GAKHEPVDAD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DNGRKMHPRS | SFKAFLEVVK | WRSVPWEDVE | MDAIHSLQLI | LRGSLQDEDA | NRNNVRSIVK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| APPDDTKKIQ | GLLELRTVTN | EMVRLIETAT | APVLAVDIAG | NINGWNNKAA | ELTGLPVMEA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| IGRPLIDLVV | VDSIEVVKRI | LDSALQGIEE | QNLEIKLKAF | HEQECNGPII | LMVNSCCSRD |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LSEKVIGVCF | VGQDLTTQKM | IMDKYTRIQG | DYVAIVKNPS | ELIPPIFMIN | DLGSCLEWNK |
| 790 | 800 | 810 | 820 | 830 | 840 |
| AMQKITGIQR | EDVIDKLLIG | EVFTLHDYGC | RVKDHATLTK | LSILMNAVIS | GQDPEKLLFG |
| 850 | 860 | 870 | 880 | 890 | 900 |
| FFDTDGKYIE | SLLTVNKRIN | AEGKITGAIC | FLHVASPELQ | HALQVQKMSE | QAATNSFKEL |
| 910 | 920 | 930 | 940 | 950 | 960 |
| TYIHQELRNP | LNGMQFTCNL | LEPSELTEEQ | RKLLSSNILC | QDQLKKILHD | TDLESIEQCY |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| MEMNTVEFNL | EEALNTVLMQ | GIPLGKEKRI | SIERDWPVEI | SRMYLYGDNL | RLQQVLADYL |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| ACALQFTQPA | EGPIVLQVIP | KKENIGSGMQ | IAHLEFRIVH | PAPGVPEALI | QEMFRHNPEV |
| 1090 | 1100 | 1110 | 1120 | 1130 | |
| SREGLGLYIC | QKLVKTMSGT | VQYLREADTS | SFIILIEFPV | AQLSSKRSKP | STSKF |