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 P12471
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P12471-F1 | Predicted | AlphaFoldDB |
No variants for P12471
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P12471 | |||||
No associated diseases with P12471
1 regional properties for P12471
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Proteasome alpha-subunit, N-terminal domain | 6 - 28 | IPR000426 |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| chloroplast thylakoid membrane | The pigmented membrane of a chloroplast thylakoid. An example of this component is found in Arabidopsis thaliana. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| photosystem I | A photosystem that contains an iron-sulfur reaction center associated with accessory pigments and electron carriers. In cyanobacteria and chloroplasts, photosystem I functions as a light-dependent plastocyanin-ferredoxin oxidoreductase, transferring electrons from plastocyanin to ferredoxin; in photosynthetic bacteria that have only a single type I photosystem, such as the green sulfur bacteria, electrons can go either to ferredoxin (Fd) -> NAD+ or to menaquinone (MK) -> Cytb/FeS -> Cytc555 -> photosystem I (cyclic photophosphorylation). |
| photosystem II | A photosystem that contains a pheophytin-quinone reaction center with associated accessory pigments and electron carriers. In cyanobacteria and chloroplasts, in the presence of light, PSII functions as a water-plastoquinone oxidoreductase, transferring electrons from water to plastoquinone, whereas other photosynthetic bacteria carry out anoxygenic photosynthesis and oxidize other compounds to re-reduce the photoreaction center. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| chlorophyll binding | Binding to a chlorophyll; a compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment. |
| metal ion binding | Binding to a metal ion. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| photosynthesis, light harvesting in photosystem I | After a photon of light is absorbed by one of the many chlorophyll molecules, in one of the light-harvesting complexes of an antenna on photosystem I, some of the absorbed energy is transferred to the pair of chlorophyll molecules in the reaction center. |
| response to light stimulus | 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 light stimulus, electromagnetic radiation of wavelengths classified as infrared, visible or ultraviolet light. |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P09756 | CAB3 | Chlorophyll a-b binding protein 3, chloroplastic | Glycine max (Soybean) (Glycine hispida) | PR |
| P09755 | CAB2 | Chlorophyll a-b binding protein 2, chloroplastic | Glycine max (Soybean) (Glycine hispida) | PR |
| Q8VZ87 | LHCB1.2 | Chlorophyll a-b binding protein 3, chloroplastic | Arabidopsis thaliana (Mouse-ear cress) | PR |
| P04778 | LHCB1.3 | Chlorophyll a-b binding protein 1, chloroplastic | Arabidopsis thaliana (Mouse-ear cress) | PR |
| P0CJ48 | LHCB1.1 | Chlorophyll a-b binding protein 2, chloroplastic | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| ASPSTPQLGV | GRVSMRKTAS | KTVSSGSPWY | GPDRVKYLGP | FSGEPPSYLT | GEFPGDYGWD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TAGLSADPET | FAKNRELEVI | HSRWAMLGAL | GCVFPELLAR | NGVKFGEASW | FKAGSQIFSE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GGLDYLGNQS | LIHAQSILAI | WATQVILMGA | VEGYRIAGGP | LGEVTDPIYP | GGSFDPLALA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DDPEAFAELK | VKEIKNGRLA | MFSMFGFFVQ | AIVTGKGPLE | NLADHLAEPV | NNNAWAYATN |
| FVPGK |