Overview
Basic information about this protein and its source genome.
- Accession
- PA5002
- Gene
- PA5002
- Status
- annotated
- Amino acids
- 472
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- Localization
- Cytoplasmic
Selected Druggability evidence
Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
MSARKQQLLKRHRRNKRIGLLVALLALLAVGLLVSPWLLPILLVALWVAHEAWFADHLFYSPGEDYRYRFAEGVESLPVRLADGRLRVDGELREGDTLVLGIGVRAGWLGRFLEPSVLLEGGAEADAQAFERGVNGLRYLNLTGLAGPLGEGRIRLRGRHCRLVGEPTLWRARHPDYRDRRVMVIAPHADDAELAAFGLYSQAREAWIVTLTAGEIETEHYRRMGLDGIAAARLKGRLRAWDSQAVPTWGGVPAERCVQLGYFCLQLPAMQANPGEVVPSREADLADIRPFRQFNRLRLASDADGLSTWNNLLADLRELILLARPEVIVLPHPHFDPHPDHVRAQEAVREALQGLDWQPQALLHYANHLHDNDRWPMGDAHMGVSLPPLTEECSPLLPWTLALERTRQVDKAMALGMMHDLQPRPPFKRRLRRRLQGWLAGRRWPAYGEDEFMRKAVRRHELFWVESLDGEA
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
3- GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
- GO:0016811 Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amide.
- GO:0006506 The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 19 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
| 175 | 457 | Gene3D | G3DSA:3.40.50.10320 | - |
| 175 | 457 | InterPro | IPR024078 | Putative deacetylase LmbE-like domain superfamily |
| 183 | 352 | Pfam | PF02585 | GlcNAc-PI de-N-acetylase |
| 183 | 352 | InterPro | IPR003737 | N-acetylglucosaminyl phosphatidylinositol deacetylase-related |
| 170 | 357 | PANTHER | PTHR12993 | N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL DE-N-ACETYLASE-RELATED |
| 170 | 357 | InterPro | IPR003737 | N-acetylglucosaminyl phosphatidylinositol deacetylase-related |
| 179 | 447 | SUPERFAMILY | SSF102588 | LmbE-like |
| 179 | 447 | InterPro | IPR024078 | Putative deacetylase LmbE-like domain superfamily |
| 20 | 49 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 20 | 49 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 50 | 472 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA5002
|
AlphaFold | — | — | full sequence | — | Viewing |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 1 | 0.669 |