Protein profile
KP13_05427
translation initiation factor SUI1-like protein
Genome: KpKP13
Overview
Basic information about this protein and its source genome.
- Accession
- KP13_05427
- Gene
- AHE44982.1
- Status
- annotated
- Amino acids
- 108
- 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 (%)
- 92.593
- DEG E-value
- 1.93e-66
- Localization
- Unknown
- ColabFold pLDDT
- 71.51
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)
6- GO:0003743 Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.
- GO:0006413 The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.
- GO:0003729 Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.
- GO:0001731 The joining of the small ribosomal subunit, ternary complex, and mRNA.
- GO:0006417 Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
- GO:0002188 A gene-specific translational control mechanism where the small ribosomal subunit remains attached to the mRNA following termination of translation, then resumes scanning on the same mRNA molecule and initiates again at a downstream start site. Reinitiation depends on de novo recruitment of the ternary complex that is required to recognize the next AUG codon.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 108 | PIRSF | PIRSF037511 | Transl_init_SUI1_prok |
| 1 | 108 | InterPro | IPR005872 | Archaeal/bacterial translation initiation factor SUI1 |
| 8 | 108 | NCBIfam | TIGR01158 | stress response translation initiation inhibitor YciH |
| 8 | 108 | InterPro | IPR005872 | Archaeal/bacterial translation initiation factor SUI1 |
| 26 | 99 | PANTHER | PTHR12789 | DENSITY-REGULATED PROTEIN HOMOLOG |
| 1 | 27 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 32 | 101 | Pfam | PF01253 | Translation initiation factor SUI1 |
| 32 | 101 | InterPro | IPR001950 | SUI1 domain |
| 28 | 108 | Gene3D | G3DSA:3.30.780.10 | - |
| 5 | 104 | SUPERFAMILY | SSF55159 | eIF1-like |
| 5 | 104 | InterPro | IPR036877 | SUI1 domain superfamily |
| 31 | 106 | CDD | cd11567 | YciH_like |
| 31 | 106 | InterPro | IPR005872 | Archaeal/bacterial translation initiation factor SUI1 |
| 34 | 100 | ProSiteProfiles | PS50296 | Translation initiation factor SUI1 family profile. |
| 34 | 100 | InterPro | IPR001950 | SUI1 domain |
| 28 | 108 | FunFam | G3DSA:3.30.780.10:FF:000002 | Stress response translation initiation inhibitor |
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_A0A0H3GW60 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_A0A0H3GW60
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_05427
|
ColabFold | — | — | full sequence | — | Loaded |
Ligand evidence
Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.
No PDB structure with a co-crystallized ligand found for this exact protein.
Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.
| Ligand | Source crystal | UniProt (homolog) | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| NO2 | P58193 | 46.0 Da LogP 0.25 TPSA 52.5 | ✓ Ro5 | ✓ Clean |
N(=O)[O-]
|
Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL bioactivity data found for this exact protein.
Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL hits found through similar proteins.
Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).
No virtual-screening candidates for this protein.
PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.