Target candidate with partial support; inspect missing evidence before prioritizing.
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
- 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.
Essentiality
- Essential (DEG)
- Y
- DEG identity (%)
- 78.699 Higher values support similarity to known essential genes.
- DEG E-value
- 0.0 Smaller values mean stronger essential-gene similarity.
Structure confidence
- ColabFold pLDDT
- 92.79 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.
MLRVYHSNRLDVLEALMEFIVERQRLDDPFQAEMVLVQSTGMAQWLQMTLAARFGIAANIEFPLPASFIWDMFVRVLKDIPGESAFSKQSMSWKLMTLLPQHLEEDDFILLRQYLSDDGDKRKLFQLAARVADLYDQYLVYRPEWLMRWEAGQRVEGLGDAQQWQAPLWQALVSYTAELGQPQWHRANLYQRFISTLEKADEPPAGLPSRVFICGISALPPVYLQALQALGKHVDVYVLFTNPCRYYWGDIKDPAFLAKLLSRQRRHHREARALPLFRDTEQAPGLFNDAGEQDVGNPLLASWGKLGRDYIYLLAGLERYEELDAFVDIAPDNLLHNLQSDILELRNAAVAGQSAEAFAHSRDKRPLALDDRSLSIHVCHSPQREVEVLHDRLLAMLEADPTLTPRDIIVMVADIDSYSPYIQAVFGAASGDRWLPWAISDRRARESHPVLQAFITLLSLPDSRFASEDVLALLDVPVLAARFNITEEGLRYLRQWVNESGVRWGMDDDNVRELDLPATGQHTWRFGLTRMLLGYAMDSREGEWQSVLPYDESSGLIAELVGNLASLLMQLNLWRRGLAQQRPLAEWLPVCRDLLNDFFLPDSETEAALALIEQQWLAVIDSGLEAQYGEQVPLTLLRDELAQRLDQQRISQRFLAGPVNICTLMPMRSIPFKVVCLLGMNDGVYPRTLPPLGFDLMSQKPQRGDRSRRDDDRYLFLEALMSAEQTLYISYIGRSIQDNSERFPSVLVQELVDYIGQSHCLAGDEELDCDASEARVKAHITHLHTRMPFDVANFQEDENKSYAREWLAAAGQQGEAHSDFIQPLTAPPIDSLPFDQLLRFWQHPVRAFFQQRLRVNFRAEEDDIPDDEPFTLEGLSRYQLNQQLLNTLIEEQDVSAMFRRFRAAGELPYGAFGELVWETQRLEMQALAERVMAERQQAQSMEIDLQCGGVNLTGWLQQVQPDGLLRWRPSLLSVSQGMQLWLEHLVYCASGGTGESRLFVRKEGEWRFPALAPAEAQAYLNELVDGYLLGMSQPLLLLPESGGAWLKACYDAEKDVILMDEETQQKARSKFLQTYEGNMVVSGEGADIWYQRLWRSLEPAHYEEIIAQTQRYLLPLYRYHRSTQI
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Subcellular localization
- Localization
- Unknown
Gene Ontology (GO)
6- GO:0009338 An enzyme complex that catalyzes exonucleolytic cleavage (in the presence of ATP) in either 5' to 3' or 3' to 5' direction to yield 5'-phosphooligonucleotides. Exodeoxyribonuclease V shows a preference for double-stranded DNA and possesses DNA-dependent ATPase activity. It acts endonucleolytically on single-stranded circular DNA.
- GO:0008854 Catalysis of the exonucleolytic cleavage (in the presence of ATP) in either 5' to 3' or 3' to 5' direction to yield 5'-phosphooligonucleotides.
- GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
- GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
- GO:0003678 Unwinding of a DNA helix, driven by ATP hydrolysis.
- GO:0000724 The error-free repair of a double-strand break in DNA in which the broken DNA molecule is repaired using homologous sequences. A strand in the broken DNA searches for a homologous region in an intact chromosome to serve as the template for DNA synthesis. The restoration of two intact DNA molecules results in the exchange, reciprocal or nonreciprocal, of genetic material between the intact DNA molecule and the broken DNA molecule.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 831 | 1049 | Pfam | PF17946 | RecC C-terminal domain |
| 831 | 1049 | InterPro | IPR041500 | RecC, C-terminal |
| 362 | 812 | SUPERFAMILY | SSF52540 | P-loop containing nucleoside triphosphate hydrolases |
| 362 | 812 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 616 | 811 | Gene3D | G3DSA:3.40.50.300 | - |
| 616 | 811 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 327 | 477 | Gene3D | G3DSA:3.40.50.300 | - |
| 327 | 477 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 607 | 811 | FunFam | G3DSA:3.40.50.300:FF:001153 | RecBCD enzyme subunit RecC |
| 1 | 1123 | Hamap | MF_01486 | RecBCD enzyme subunit RecC [recC]. |
| 1 | 1123 | InterPro | IPR006697 | RecBCD enzyme subunit RecC |
| 924 | 944 | Coils | Coil | Coil |
| 86 | 185 | Gene3D | G3DSA:1.10.10.160 | - |
| 86 | 185 | InterPro | IPR013986 | DExx box DNA helicase domain superfamily |
| 86 | 185 | FunFam | G3DSA:1.10.10.160:FF:000003 | RecBCD enzyme subunit RecC |
| 1 | 347 | SUPERFAMILY | SSF52540 | P-loop containing nucleoside triphosphate hydrolases |
| 1 | 347 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 820 | 1119 | SUPERFAMILY | SSF52980 | Restriction endonuclease-like |
| 820 | 1119 | InterPro | IPR011335 | Restriction endonuclease type II-like |
| 2 | 344 | Pfam | PF04257 | Exodeoxyribonuclease V, gamma subunit |
| 1 | 1124 | PIRSF | PIRSF000980 | RecC |
| 1 | 1124 | InterPro | IPR006697 | RecBCD enzyme subunit RecC |
| 327 | 482 | FunFam | G3DSA:3.40.50.300:FF:001068 | RecBCD enzyme subunit RecC |
| 864 | 935 | Gene3D | G3DSA:1.10.10.990 | - |
| 1 | 1123 | PANTHER | PTHR30591 | RECBCD ENZYME SUBUNIT RECC |
| 4 | 251 | Gene3D | G3DSA:3.40.50.10930 | - |
| 834 | 1116 | CDD | cd22353 | RecC_C-like |
| 2 | 1086 | NCBIfam | TIGR01450 | exodeoxyribonuclease V subunit gamma |
| 2 | 1086 | InterPro | IPR006697 | RecBCD enzyme subunit RecC |
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_A0A0H3GX23
|
AlphaFold DB | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_02291
|
ColabFold | — | — | full sequence | — | Loaded |
Cross-references
External database identifiers for this protein, its structures, ligands, and metabolic reactions.