Overview
Basic information about this protein and its source genome.
- Accession
- KP13_05393
- Gene
- cho AHE45038.1
- Status
- annotated
- Amino acids
- 287
- 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)
- Y
- DEG identity (%)
- 75.175
- DEG E-value
- 7.88e-160
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 89.97
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:0006289 A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
- GO:0009380 Any of the protein complexes formed by the UvrABC excinuclease system, which carries out nucleotide excision repair. Three different complexes are formed by the 3 proteins as they proceed through the excision repair process. First a complex consisting of two A subunits and two B subunits bind DNA and unwind it around the damaged site. Then, the A subunits disassociate leaving behind a stable complex between B subunits and DNA. Now, subunit C binds to this B+DNA complex and causes subunit B to nick the DNA on one side of the complex while subunit C nicks the DNA on the other side of the complex. DNA polymerase I and DNA ligase can then repair the resulting gap.
- GO:0004519 Catalysis of the cleavage of ester linkages within nucleic acids by creating internal breaks.
- GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
- GO:0009432 An error-prone process for repairing damaged microbial DNA.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 34 | 112 | SMART | SM00465 | uri_9 |
| 34 | 112 | InterPro | IPR000305 | GIY-YIG endonuclease |
| 21 | 116 | FunFam | G3DSA:3.40.1440.10:FF:000004 | UV-repair endonuclease Cho |
| 33 | 108 | ProSiteProfiles | PS50164 | GIY-YIG domain profile. |
| 33 | 108 | InterPro | IPR000305 | GIY-YIG endonuclease |
| 31 | 108 | CDD | cd10434 | GIY-YIG_UvrC_Cho |
| 31 | 108 | InterPro | IPR047296 | UvrC/Cho-like, GIY-YIG domain |
| 21 | 116 | Gene3D | G3DSA:3.40.1440.10 | - |
| 21 | 116 | InterPro | IPR035901 | GIY-YIG endonuclease superfamily |
| 18 | 256 | PANTHER | PTHR30562 | UVRC/OXIDOREDUCTASE |
| 34 | 111 | SUPERFAMILY | SSF82771 | GIY-YIG endonuclease |
| 34 | 111 | InterPro | IPR035901 | GIY-YIG endonuclease superfamily |
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 + 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_A0A0H3GN81
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_05393
|
ColabFold | — | — | full sequence | — | Loaded |
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 |
|---|---|---|---|---|---|---|---|
| 6 | 0.419 | ||||||
| 1 | 0.236 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 1.98 | 0.042 | ||||||
| 2 | 0.72 | 0.002 |
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 |
|---|---|---|---|---|---|---|---|
| 3 | 0.456 | ||||||
| 1 | 0.28 | ||||||
| 2 | 0.244 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 1.07 | 0.007 |