Overview
Basic information about this protein and its source genome.
- Accession
- KP13_31743
- Gene
- AHE44752.1
- Status
- annotated
- Amino acids
- 270
- 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
- 91.22
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.
Enzyme Commission (EC)
1Gene Ontology (GO)
3- GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
- GO:0008236 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
- GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 51 | 162 | Gene3D | G3DSA:2.40.10.10 | - |
| 51 | 162 | InterPro | IPR043504 | Peptidase S1, PA clan, chymotrypsin-like fold |
| 36 | 239 | Gene3D | G3DSA:2.40.10.10 | - |
| 36 | 239 | InterPro | IPR043504 | Peptidase S1, PA clan, chymotrypsin-like fold |
| 5 | 15 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 26 | 264 | SUPERFAMILY | SSF50494 | Trypsin-like serine proteases |
| 26 | 264 | InterPro | IPR009003 | Peptidase S1, PA clan |
| 1 | 21 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 22 | 270 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 214 | 225 | ProSitePatterns | PS00135 | Serine proteases, trypsin family, serine active site. |
| 214 | 225 | InterPro | IPR033116 | Serine proteases, trypsin family, serine active site |
| 1 | 21 | SignalP_EUK | SignalP-noTM | SignalP-noTM |
| 30 | 252 | PANTHER | PTHR15462 | SERINE PROTEASE |
| 16 | 21 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 209 | 225 | PRINTS | PR00839 | V8 serine protease family signature |
| 209 | 225 | InterPro | IPR008256 | Peptidase S1B |
| 41 | 58 | PRINTS | PR00839 | V8 serine protease family signature |
| 41 | 58 | InterPro | IPR008256 | Peptidase S1B |
| 175 | 188 | PRINTS | PR00839 | V8 serine protease family signature |
| 175 | 188 | InterPro | IPR008256 | Peptidase S1B |
| 66 | 83 | PRINTS | PR00839 | V8 serine protease family signature |
| 66 | 83 | InterPro | IPR008256 | Peptidase S1B |
| 229 | 241 | PRINTS | PR00839 | V8 serine protease family signature |
| 229 | 241 | InterPro | IPR008256 | Peptidase S1B |
| 77 | 82 | ProSitePatterns | PS00134 | Serine proteases, trypsin family, histidine active site. |
| 77 | 82 | InterPro | IPR018114 | Serine proteases, trypsin family, histidine active site |
| 46 | 241 | Pfam | PF00089 | Trypsin |
| 46 | 241 | InterPro | IPR001254 | Serine proteases, trypsin domain |
| 1 | 21 | SignalP_GRAM_POSITIVE | SignalP-TM | SignalP-TM |
| 1 | 4 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
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_A0A0H3GMY0
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_31743
|
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 |
|---|---|---|---|---|---|---|---|
| 1 | 0.212 |
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 | 10.89 | 0.584 |
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 | 0.285 |
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 | 8.74 | 0.467 |