Overview
Basic information about this protein and its source genome.
- Accession
- PA2618
- Gene
- bpt PA2618
- Status
- annotated
- Amino acids
- 235
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 42.391
- Human E-value
- 5.66e-18
- 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.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
6- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0004057 Catalysis of the reaction: an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-tRNA(Arg) = H+ + N-terminal L-arginyl-L-amino acid-[protein] + tRNA(Arg).
- GO:0008914 Catalysis of the reaction: L-leucyl-tRNA(Leu) + N-terminal L-arginyl-[protein] = H+ + N-terminal L-leucyl-L-arginyl-[protein] + tRNA(Leu). Can also transfer the leucyl residue on an N-terminal L-lysyl residue.
- GO:0010498 The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds that is mediated by the proteasome.
- GO:0071596 The chemical reactions and pathways resulting in the breakdown of a protein or peptide covalently tagged with ubiquitin, via the N-end rule pathway. In the N-end rule pathway, destabilizing N-terminal residues (N-degrons) in substrates are recognized by E3 ligases (N-recognins), whereupon the substrates are linked to ubiquitin and then delivered to the proteasome for degradation.
- GO:0016598 The conjugation of arginine to the N-terminal aspartate or glutamate of a protein; required for the degradation of the protein via the ubiquitin pathway.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 235 | PIRSF | PIRSF037208 | ATE_prok |
| 1 | 235 | InterPro | IPR017138 | Aspartate/glutamate leucyltransferase |
| 5 | 232 | Hamap | MF_00689 | Aspartate/glutamate leucyltransferase [bpt]. |
| 5 | 232 | InterPro | IPR017138 | Aspartate/glutamate leucyltransferase |
| 78 | 233 | SUPERFAMILY | SSF55729 | Acyl-CoA N-acyltransferases (Nat) |
| 78 | 233 | InterPro | IPR016181 | Acyl-CoA N-acyltransferase |
| 15 | 85 | Pfam | PF04376 | Arginine-tRNA-protein transferase, N terminus |
| 15 | 85 | InterPro | IPR007471 | N-end aminoacyl transferase, N-terminal |
| 105 | 226 | Pfam | PF04377 | Arginine-tRNA-protein transferase, C terminus |
| 105 | 226 | InterPro | IPR007472 | N-end rule aminoacyl transferase, C-terminal |
| 8 | 93 | PANTHER | PTHR21367 | ARGININE-TRNA-PROTEIN TRANSFERASE 1 |
| 8 | 93 | InterPro | IPR030700 | N-end rule aminoacyl transferase |
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
PA2618
|
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 | 0.741 | ||||||
| 2 | 0.674 |