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
- No hit
- Gut microbiome similarity
- 4.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.
Essentiality
- Essential (DEG)
- Y
- DEG identity (%)
- 95.758 Higher values support similarity to known essential genes.
- DEG E-value
- 0.0 Smaller values mean stronger essential-gene similarity.
Structure confidence
- ColabFold pLDDT
- 87.67 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.
Cross-references
External database identifiers for this protein, its structures, ligands, and metabolic reactions.
Sequence
Sequence
Primary amino-acid sequence viewer.
MNKEILAVVEAVSNEKALPREKIFEALESALATATKKKYEQEIDVRVEIDRKSGDFDTFRRWLVVEEVTQPTREITLEAARFEDESMNVGDYVEDQIESVTFDRITTQTAKQVIVQKVREAERAMVVDQFREHEGEIITGVVKKVNRDNITLDLGNNAEAVILREDMLPRENFRPGDRIRGVLYAVRPEARGAQLFVTRSKPEMLIELFRIEVPEIGEEVLEIKAAARDPGSRAKIAVKTNDKRIDPVGACVGMRGARVQAVSTELGGERIDIVLWDDNPAQFVINAMAPADVASIVVDEDKHTMDIAVEAGNLAQAIGRNGQNVRLASQLSGWELNVMTVDDLQAKHQAEAHAAIDTFTKYLDIDEDFATVLVEEGFSSLEELAYVPMKELLEIDGLDEATVEALRERAKNALTTLALAQEESLGDNKPADDLLNLEGLDRALAFKLAARGVCTLEDLAEQGVDDLADIEGMTDEKAGELIMAARNICWFGDEA
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Subcellular localization
- Localization
- Cytoplasmic
Gene Ontology (GO)
9- GO:0003676 Binding to a nucleic acid.
- GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
- GO:0003700 A transcription regulator activity that modulates transcription of gene sets via selective and non-covalent binding to a specific double-stranded genomic DNA sequence (sometimes referred to as a motif) within a cis-regulatory region. Regulatory regions include promoters (proximal and distal) and enhancers. Genes are transcriptional units, and include bacterial operons.
- GO:0031564 A positive regulation of gene expression mechanism that allows RNA polymerase to continue transcription beyond a termination site, thus allowing expression of downstream genes under specific conditions.
- GO:0003723 Binding to an RNA molecule or a portion thereof.
- GO:0031554 Any process that modulates the frequency, rate, extent, or location of DNA-templated transcription termination, the process in which transcription is completed; the formation of phosphodiester bonds ceases, the RNA-DNA hybrid dissociates, and RNA polymerase releases the DNA.
- GO:0006353 The completion of transcription: the RNA polymerase pauses, the RNA-DNA hybrid dissociates, followed by the release of the RNA polymerase from its DNA template.
- GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
- GO:0003746 Functions in chain elongation during polypeptide synthesis at the ribosome.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 230 | 297 | Pfam | PF13184 | NusA-like KH domain |
| 230 | 297 | InterPro | IPR025249 | KH domain, NusA-like |
| 279 | 343 | SUPERFAMILY | SSF54814 | Prokaryotic type KH domain (KH-domain type II) |
| 279 | 343 | InterPro | IPR009019 | K homology domain superfamily, prokaryotic type |
| 278 | 346 | FunFam | G3DSA:3.30.300.20:FF:000005 | Transcription termination/antitermination protein NusA |
| 1 | 387 | PANTHER | PTHR22648 | TRANSCRIPTION TERMINATION FACTOR NUSA |
| 1 | 387 | InterPro | IPR030842 | Transcription termination/antitermination protein NusA, bacterial |
| 278 | 343 | Gene3D | G3DSA:3.30.300.20 | - |
| 278 | 343 | InterPro | IPR015946 | K homology domain-like, alpha/beta |
| 135 | 198 | Gene3D | G3DSA:2.40.50.140 | - |
| 135 | 198 | InterPro | IPR012340 | Nucleic acid-binding, OB-fold |
| 431 | 490 | FunFam | G3DSA:1.10.150.20:FF:000015 | Transcription termination/antitermination protein NusA |
| 202 | 276 | CDD | cd02134 | KH-II_NusA_rpt1 |
| 2 | 410 | Hamap | MF_00945_B | Transcription termination/antitermination protein NusA [nusA]. |
| 2 | 410 | InterPro | IPR030842 | Transcription termination/antitermination protein NusA, bacterial |
| 352 | 421 | Gene3D | G3DSA:1.10.150.20 | - |
| 365 | 414 | NCBIfam | TIGR01954 | transcription termination factor NusA, C-terminal duplication |
| 365 | 414 | InterPro | IPR010214 | Transcription termination factor NusA, C-terminal duplication |
| 440 | 489 | NCBIfam | TIGR01954 | transcription termination factor NusA, C-terminal duplication |
| 440 | 489 | InterPro | IPR010214 | Transcription termination factor NusA, C-terminal duplication |
| 302 | 338 | ProSiteProfiles | PS50084 | Type-1 KH domain profile. |
| 1 | 129 | FunFam | G3DSA:3.30.1480.10:FF:000001 | Transcription termination/antitermination protein NusA |
| 4 | 342 | NCBIfam | TIGR01953 | transcription termination factor NusA |
| 4 | 342 | InterPro | IPR010213 | Transcription termination factor NusA |
| 432 | 486 | Pfam | PF14520 | Helix-hairpin-helix domain |
| 4 | 123 | Pfam | PF08529 | NusA N-terminal domain |
| 4 | 123 | InterPro | IPR013735 | Transcription factor NusA, N-terminal |
| 431 | 490 | Gene3D | G3DSA:1.10.150.20 | - |
| 133 | 200 | SMART | SM00316 | S1_6 |
| 133 | 200 | InterPro | IPR022967 | RNA-binding domain, S1 |
| 135 | 200 | ProSiteProfiles | PS50126 | S1 domain profile. |
| 135 | 200 | InterPro | IPR003029 | S1 domain |
| 135 | 198 | FunFam | G3DSA:2.40.50.140:FF:000092 | Transcription termination/antitermination protein NusA |
| 403 | 423 | Coils | Coil | Coil |
| 1 | 126 | SUPERFAMILY | SSF69705 | Transcription factor NusA, N-terminal domain |
| 1 | 126 | InterPro | IPR036555 | NusA, N-terminal domain superfamily |
| 199 | 277 | FunFam | G3DSA:3.30.300.20:FF:000002 | Transcription termination/antitermination protein NusA |
| 429 | 492 | SUPERFAMILY | SSF47794 | Rad51 N-terminal domain-like |
| 429 | 492 | InterPro | IPR010995 | DNA repair Rad51/transcription factor NusA, alpha-helical |
| 352 | 421 | FunFam | G3DSA:1.10.150.20:FF:000018 | Transcription termination/antitermination protein NusA |
| 132 | 199 | CDD | cd04455 | S1_NusA |
| 201 | 278 | SUPERFAMILY | SSF54814 | Prokaryotic type KH domain (KH-domain type II) |
| 201 | 278 | InterPro | IPR009019 | K homology domain superfamily, prokaryotic type |
| 134 | 195 | Pfam | PF00575 | S1 RNA binding domain |
| 134 | 195 | InterPro | IPR003029 | S1 domain |
| 1 | 129 | Gene3D | G3DSA:3.30.1480.10 | - |
| 1 | 129 | InterPro | IPR036555 | NusA, N-terminal domain superfamily |
| 355 | 415 | SUPERFAMILY | SSF47794 | Rad51 N-terminal domain-like |
| 355 | 415 | InterPro | IPR010995 | DNA repair Rad51/transcription factor NusA, alpha-helical |
| 279 | 339 | CDD | cd22529 | KH-II_NusA_rpt2 |
| 132 | 199 | SUPERFAMILY | SSF50249 | Nucleic acid-binding proteins |
| 132 | 199 | InterPro | IPR012340 | Nucleic acid-binding, OB-fold |
| 199 | 277 | Gene3D | G3DSA:3.30.300.20 | - |
| 199 | 277 | InterPro | IPR015946 | K homology domain-like, alpha/beta |
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
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
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_A0A0H3GW50
|
AlphaFold DB | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_01101
|
ColabFold | — | — | full sequence | — | Loaded |