Overview
Basic information about this protein and its source genome.
- Accession
- KP13_01022
- Gene
- dedD AHE43450.1
- Status
- annotated
- Amino acids
- 216
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- DEG identity (%)
- 0.0
- Localization
- Unknown
- ColabFold pLDDT
- 66.24
Selected Druggability evidence
AlphaFold / UniProt modelSelected 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.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
5- GO:0042834 Interacting selectively and non-covalently, in a non-covalent manner, with peptidoglycan, any of a class of glycoconjugates found in bacterial cell walls.
- GO:0030428 A structure composed of peptidoglycan and often chitin in addition to other materials. It usually forms perpendicular to the long axis of a cell or hypha and grows centripetally from the cell wall to the center of the cell and often functions in the compartmentalization of a cell into two daughter cells.
- GO:0032506 A cellular process that is involved in cytokinesis (the division of the cytoplasm of a cell and its separation into two daughter cells).
- GO:0032153 The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
- GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 136 | 211 | SUPERFAMILY | SSF110997 | Sporulation related repeat |
| 136 | 211 | InterPro | IPR036680 | Sporulation-like domain superfamily |
| 2 | 213 | PANTHER | PTHR38687 | CELL DIVISION PROTEIN DEDD-RELATED |
| 134 | 213 | ProSiteProfiles | PS51724 | SPOR domain profile. |
| 134 | 213 | InterPro | IPR007730 | Sporulation-like domain |
| 136 | 211 | Gene3D | G3DSA:3.30.70.1070 | Sporulation related repeat |
| 1 | 215 | Hamap | MF_02022 | Cell division protein DedD [dedD]. |
| 1 | 215 | InterPro | IPR032898 | Cell division protein DedD |
| 11 | 16 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 1 | 16 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 1 | 16 | SignalP_EUK | SignalP-noTM | SignalP-noTM |
| 29 | 138 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 2 | 10 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 1 | 1 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 17 | 216 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 95 | 123 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 139 | 211 | FunFam | G3DSA:3.30.70.1070:FF:000001 | Cell division protein DedD |
| 137 | 210 | Pfam | PF05036 | SPOR domain |
| 137 | 210 | InterPro | IPR007730 | Sporulation-like domain |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
No pockets are loaded yet for the displayed AlphaFold model AF_A0A0H3GWD7 structure. Run experimental pocket backfill to show FPocket/P2Rank overlays on this structure.
Loading 3D structure...
Structural evidence
0 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GWD7
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_01022
|
ColabFold | — | — | full sequence | — | Loaded |