Pre-mRNA-splicing factor CWC22 homolog (CWC22) is a 908-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9HCG8.
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The mean pLDDT of this model is 65.1 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 32% |
| 70 to 90 | Confident: backbone generally right | 20% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 45% |
What pLDDT means and how to read it
Required for pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:12226669, PubMed:22961380, PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Promotes exon-junction complex (EJC) assembly (PubMed:22959432, PubMed:22961380). Hinders EIF4A3 from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs. Through its role in EJC assembly, required for nonsense-mediated mRNA decay
Component of the pre-catalytic spliceosome B and the catalytic spliceosome C complexes (PubMed:11991638, PubMed:22961380, PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106). Component of the minor spliceosome, which splices U12-type introns (PubMed:33509932). Interacts with EIF4A3 and PRPF19 in an RNA-independent manner. Direct interaction with EIF4A3 is mediated by the MIF4G…
Nucleus, Nucleus speckle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4C9B | X-ray | 2.0 Å | B=116-406 |
| 8C6J | EM | 2.8 Å | H=149-648 |
| 7DVQ | EM | 2.89 Å | V=1-908 |
| 6ICZ | EM | 3.0 Å | V=1-908 |
| 8I0R | EM | 3.0 Å | V=1-908 |
| 8I0T | EM | 3.0 Å | V=1-908 |
| 8I0V | EM | 3.0 Å | V=1-908 |
| 7QTT | EM | 3.1 Å | W=1-908 |
| 6YVH | X-ray | 3.19 Å | A/B/D/F=119-406 |
| 6QDV | EM | 3.3 Å | H=1-908 |
| 8I0U | EM | 3.3 Å | V=1-908 |
| 9FMD | EM | 3.3 Å | H=1-908 |
| 6ZYM | EM | 3.4 Å | T=1-908 |
| 8I0W | EM | 3.4 Å | V=1-908 |
| 5XJC | EM | 3.6 Å | V=1-908 |
| 7W59 | EM | 3.6 Å | V=1-908 |
| 7W5A | EM | 3.6 Å | V=1-908 |
| 5YZG | EM | 4.1 Å | V=1-908 |
| 8I0S | EM | 4.2 Å | V=1-908 |
| 7W5B | EM | 4.3 Å | V=1-908 |
Showing 20 of 27 experimental structures (best resolution first).
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