Protein target profile
tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC
Accession: KP13_01033
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
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
- 2.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.
Essentiality
- Essential (DEG)
- N
- DEG identity (%)
- 0.0 Higher values support similarity to known essential genes.
Structure confidence
- ColabFold pLDDT
- 96.3 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.
MKQNAIQPANLEFNAEGTPVSRDFDDVYFSNDNGLEETRYVFLGGNRLPERFPSHPRPLMIVAESGFGTGLNFLTLWQAFDVFVRDNPDVTLQRLHFISFEKYPLKAEDLRLAHQRWPELAPWAQQLQAQWPSAFGGCHRLLLDGGRVTLDLWFGDINELTRELDDSLNQQVDAWFLDGFAPAKNPDMWTQDLFSAMARLARPGGTLATFTSAGFVRRGLQEAGFTMRKSKGFGRKREMLTGEMAQTLSFPARVPWFARSSSDAREAAIIGGGIASALLSLALLRRGWQVTLYCADEAPAQGASGNRQGALYPLLSQHDPALARFFPAAFTFARRMYDALPVMFDHQWCGVTQLGWDEKSTHKIAQMLALNLPPDIACAVTAEQVAGLTGVDTGCGGITYPAGGWLCPQQLTAELLALAATRGLHVHYGYPVETLSAEGDGWLLNQQRYHQAVVLANGHRITGFAQTAQLPVYPVGGQVSHIPTTPRLAALRQVLCYDGYLTPQNPQNQQHCIGASYHRGKTDTTFSEEDQQHNRQRLIDCFPGAEWPQDVDISANDARCGVRCATRDHLPMVGNVPDYAATLTQYASLHEQPDIADSAPVCRNLFMLGALGSRGLCTAPLSAELLAAQMSAEPLPLDSDTLAALNPNRLWVRKLLKGKAVK
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Subcellular localization
- Localization
- Cytoplasmic
Gene Ontology (GO)
9- GO:0016645 Catalysis of an oxidation-reduction (redox) reaction in which a CH-NH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
- GO:0008168 Catalysis of the transfer of a methyl group to an acceptor molecule.
- GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
- GO:0008033 The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group.
- GO:0004808 Catalysis of the reaction: 5-aminomethyl-2-thiouridine34 in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine34 in tRNA + H+ + S-adenosyl-L-homocysteine. This enzyme specifically adds the terminal methyl group of 5-[(methylamino)methyl]-2-thiouridylate.
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
- GO:0032259 The process in which a methyl group is covalently attached to a molecule.
- GO:0002098 The process in which a uridine at position 34 of a tRNA is post-transcriptionally modified. The wobble nucleoside of the tRNA sequence (position 34) corresponds to the first position of the anticodon.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 9 | 250 | Gene3D | G3DSA:3.40.50.150 | Vaccinia Virus protein VP39 |
| 9 | 250 | InterPro | IPR029063 | S-adenosyl-L-methionine-dependent methyltransferase superfamily |
| 348 | 566 | Gene3D | G3DSA:3.30.9.10 | - |
| 267 | 658 | NCBIfam | TIGR03197 | FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC |
| 267 | 658 | InterPro | IPR017610 | tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC, C-terminal |
| 472 | 548 | SUPERFAMILY | SSF54373 | FAD-linked reductases, C-terminal domain |
| 267 | 628 | Pfam | PF01266 | FAD dependent oxidoreductase |
| 267 | 628 | InterPro | IPR006076 | FAD dependent oxidoreductase |
| 19 | 243 | NCBIfam | NF033855 | tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD |
| 19 | 243 | InterPro | IPR047785 | tRNA mnm(5)s(2)U biosynthesis bifunctional protein MnmC, N-terminal |
| 262 | 658 | PANTHER | PTHR13847 | SARCOSINE DEHYDROGENASE-RELATED |
| 118 | 244 | Pfam | PF05430 | S-adenosyl-L-methionine-dependent methyltransferase |
| 118 | 244 | InterPro | IPR008471 | MnmC-like methyltransferase |
| 9 | 249 | FunFam | G3DSA:3.40.50.150:FF:000107 | tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC |
| 267 | 655 | SUPERFAMILY | SSF51905 | FAD/NAD(P)-binding domain |
| 267 | 655 | InterPro | IPR036188 | FAD/NAD(P)-binding domain superfamily |
| 62 | 239 | SUPERFAMILY | SSF53335 | S-adenosyl-L-methionine-dependent methyltransferases |
| 62 | 239 | InterPro | IPR029063 | S-adenosyl-L-methionine-dependent methyltransferase superfamily |
| 7 | 653 | Hamap | MF_01102 | tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC [mnmC]. |
| 7 | 653 | InterPro | IPR023032 | tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC |
| 265 | 655 | Gene3D | G3DSA:3.50.50.60 | - |
| 265 | 655 | InterPro | IPR036188 | FAD/NAD(P)-binding domain superfamily |
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_A0A0H3GWE4
|
AlphaFold DB | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_01033
|
ColabFold | — | — | full sequence | — | Loaded |