Q96J94: Piwi-like protein 1 (PIWIL1)

Piwi-like protein 1 (PIWIL1) is a 861-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96J94.

Gene
PIWIL1
Organism
Homo sapiens
Length
861 residues
Mean pLDDT
85.6
Model
AF-Q96J94-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.6 (confident 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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate69%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Endoribonuclease that plays a central role in postnatal germ cells by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Directly binds methylated piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Strongly prefers a uridine in the first position of their guide (g1U…

Subunit structure

Interacts (via Piwi domain) with DICER1, suggesting that it forms ribonucleoprotein RISC complexes; this interaction is regulated by HSP90AB1 activity (PubMed:14749716). Interacts with MAEL, KIF17, PABPC1, PRMT5 and WDR77. Interacts (when methylated on arginine residues) with TDRD1, TDRKH/TDRD2, RNF17/TDRD4, TDRD6, TDRD7 and TDRD9. Interacts with CLOCK. Interacts with MOV10L1. Interacts with…

Subcellular location

Cytoplasm

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3O7VX-ray2.1 ÅX=276-399
3O3IX-ray2.8 ÅX=277-399
6PI7X-ray2.8 ÅG=2-17
3O6EX-ray2.9 ÅX=277-399
2L5CNMRA=266-399
2L5DNMRA=266-399

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