Promising target candidate with multiple supporting evidence streams.
Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.
Main supporting evidence
Risks to review
Terms and data sources used on this page
PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.
AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.
ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.
pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.
FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.
Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.
PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.
ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.
ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.
LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.
Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.
DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.
Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.
EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.
KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.
Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.
Prioritization evidence
Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.
Off-target risk
- Human off-target
- Hit
- Human identity (%)
- 32.941 Lower values reduce human off-target concern.
- Human E-value
- 1.45e-06
- Gut microbiome similarity
- 74.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.
Essentiality
- Essential (DEG)
- Y
- DEG identity (%)
- 57.827 Higher values support similarity to known essential genes.
- DEG E-value
- 0.0 Smaller values mean stronger essential-gene similarity.
Structure confidence
- ColabFold pLDDT
- 91.17 0-100 confidence; >70 supports local structural interpretation.
Binding-site evidence
AlphaFold DB / UniProt modelP2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
MDKIEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPAISIEQKSTSHNPRSTVGTITEIHDYLRLLYARVGEPRCPDHDVPLAAQTVSQMVDNVLAQPEGLRLMLLAPIIKERKGEHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVIDRFKVRDDLAQRLAESFETALELSGGTAIVANMDDEKAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVVQNPELSLAGGAIRGWDRRNFYYFQMLKSLAEHYKFDVEAPWGTLSANVQKVVLYGSGKESIEFKYMNDRGDTSVRRHPFEGVLHNMERRYKETESSAVREELAKFISNRPCASCDGTRLRREARHVFVENTPLPTISDMSIGHAMDFFNNLKLSGQRAKIAEKVLKEIGDRLKFLVNVGLNYLTLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRNLGNTVIVVEHDEDAIRAADHVIDIGPGAGVHGGQVVAEGPLEAIMAVPESLTGQFMSGKRKIEVPKQRVPANPEKVLKLTGARGNNLKDVTLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQRQLNGATIAEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVPESRSRGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREFFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLEVLHQLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVAECEASHTARFLKPMLK
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Subcellular localization
- Localization
- Cytoplasmic
Gene Ontology (GO)
9- GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
- 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:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
- GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
- 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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0009381 Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid at sites flanking regions of damaged DNA to which the Uvr ABC excinuclease complexes bind.
- GO:0008270 Binding to a zinc ion (Zn).
- GO:0009432 An error-prone process for repairing damaged microbial DNA.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 607 | 937 | ProSiteProfiles | PS50893 | ATP-binding cassette, ABC transporter-type domain profile. |
| 607 | 937 | InterPro | IPR003439 | ABC transporter-like, ATP-binding domain |
| 2 | 940 | PANTHER | PTHR43152 | UVRABC SYSTEM PROTEIN A |
| 6 | 579 | Gene3D | G3DSA:3.40.50.300 | - |
| 6 | 579 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 613 | 911 | SUPERFAMILY | SSF52540 | P-loop containing nucleoside triphosphate hydrolases |
| 613 | 911 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 806 | 860 | Pfam | PF00005 | ABC transporter |
| 806 | 860 | InterPro | IPR003439 | ABC transporter-like, ATP-binding domain |
| 610 | 937 | Gene3D | G3DSA:3.40.50.300 | - |
| 610 | 937 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 1 | 940 | Hamap | MF_00205 | UvrABC system protein A [uvrA]. |
| 1 | 940 | InterPro | IPR004602 | UvrABC system subunit A |
| 693 | 830 | FunFam | G3DSA:1.20.1580.10:FF:000002 | UvrABC system protein A |
| 830 | 844 | ProSitePatterns | PS00211 | ABC transporters family signature. |
| 830 | 844 | InterPro | IPR017871 | ABC transporter-like, conserved site |
| 319 | 437 | Gene3D | G3DSA:1.10.8.280 | - |
| 4 | 116 | CDD | cd03270 | ABC_UvrA_I |
| 287 | 404 | FunFam | G3DSA:1.10.8.280:FF:000001 | UvrABC system protein A |
| 389 | 487 | FunFam | G3DSA:1.20.1580.10:FF:000003 | UvrABC system protein A |
| 3 | 925 | NCBIfam | TIGR00630 | excinuclease ABC subunit UvrA |
| 3 | 925 | InterPro | IPR004602 | UvrABC system subunit A |
| 4 | 569 | SUPERFAMILY | SSF52540 | P-loop containing nucleoside triphosphate hydrolases |
| 4 | 569 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 209 | 281 | Gene3D | G3DSA:3.30.1490.20 | - |
| 209 | 281 | InterPro | IPR013815 | ATP-grasp fold, subdomain 1 |
| 290 | 399 | Pfam | PF17755 | UvrA DNA-binding domain |
| 290 | 399 | InterPro | IPR041552 | UvrA DNA-binding domain |
| 487 | 501 | ProSitePatterns | PS00211 | ABC transporters family signature. |
| 487 | 501 | InterPro | IPR017871 | ABC transporter-like, conserved site |
| 135 | 244 | FunFam | G3DSA:3.30.190.20:FF:000003 | UvrABC system protein A |
| 130 | 237 | Pfam | PF17760 | UvrA interaction domain |
| 130 | 237 | InterPro | IPR041102 | UvrA, interaction domain |
| 613 | 921 | CDD | cd03271 | ABC_UvrA_II |
| 92 | 518 | Gene3D | G3DSA:1.20.1580.10 | ABC transporter ATPase like domain |
| 693 | 830 | Gene3D | G3DSA:1.20.1580.10 | ABC transporter ATPase like domain |
3D structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.
How colors and pocket overlays are used
Pocket details Inspect a specific pocket, or open the full viewer
- Method
- -
- Score
- -
- Visible layer
- -
- Residues
- -
- Pocket properties
- -
Selecting a pocket opens its details and centers the viewer without clearing other active layers. Use Focus this pocket when you want to hide the rest; use Surface for the wider residue environment.
Binding pockets · P2Rank
Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Binding pockets · FPocket
Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Residue sets
Binding pockets · P2Rank
Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Binding pockets · FPocket
Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Residue sets
All structural evidence
Structural evidence
0 + 2Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold DB
AF_A0A0H3GGW8
|
AlphaFold DB | — | — | full sequence | — | Viewing |
|
ColabFold
VK055_3026
|
ColabFold | — | — | full sequence | — | Loaded |
Cross-references
External database identifiers for this protein, its structures, ligands, and metabolic reactions.