Q06164: E3 ubiquitin-protein ligase substrate receptor MMS22 (MMS22)

E3 ubiquitin-protein ligase substrate receptor MMS22 (MMS22) is a 1454-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q06164.

Gene
MMS22
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
1454 residues
Mean pLDDT
63.0
Model
AF-Q06164-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 63.0 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate10%
70 to 90Confident: backbone generally right44%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions36%

What pLDDT means and how to read it

Function

Substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-MMS22). RTT101(MMS1-MMS22) promotes fork progression through damaged DNA or natural pause sites by stabilizing replication proteins like the replication fork-pausing complex (FPC) and leading-strand polymerase at stalled replication forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination is required for efficient histone deposition during replication-coupled nucleosome assembly, probably by facilitating the transfer of H3-H4 from ASF1 to other chaperones involved in histone deposition

Subunit structure

Component of a cullin-RING ligase (CRL) composed of 4 subunits: the RING protein HRT1, the cullin RTT101, a linker protein MMS1, and the substrate receptor MMS22. This complex further interacts with RTT107 and CTF4 to form RTT101-MMS1-MMS22-RTT107 and RTT101-MMS1-MMS22-CTF4 complexes respectively. Interacts (via C-ter) with MMS1 (via N-ter). Interacts with RTT107

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6J0XX-ray2.31 ÅE/F/G/H=22-37

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