P32529: DNA-directed RNA polymerase I subunit RPA12 (RPA12)

DNA-directed RNA polymerase I subunit RPA12 (RPA12) is a 125-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P32529.

Gene
RPA12
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
125 residues
Mean pLDDT
83.8
Model
AF-P32529-F1 v6
Model created
1 Aug 2025
PDB structures
44

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Model confidence (pLDDT)

The mean pLDDT of this model is 83.8 (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 accurate46%
70 to 90Confident: backbone generally right39%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. Proposed to contribute to the polymerase catalytic activity and form the polymerase active center together with the two largest subunits. Subunit RPA12 contributes a catalytic zinc ribbon that is required for RNA cleavage by Pol I. Involved in transcriptional termination

Subunit structure

Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the…

Subcellular location

Nucleus, nucleolus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6RUIEM2.7 ÅI=1-125
9G1VEM2.7 ÅI=1-125
4C2MX-ray2.8 ÅI/X=1-125
9G27EM2.8 ÅI=1-125
6RQLEM2.9 ÅI=1-125
4C3IX-ray3.0 ÅI=1-125
6RWEEM3.0 ÅI=1-125
6RRDEM3.1 ÅI=1-125
6HLQEM3.18 ÅI=1-125
6HLREM3.18 ÅI=1-125
9G2BEM3.2 ÅI=1-125
6HLSEM3.21 ÅI=1-125
4C3HX-ray3.27 ÅI=1-125
9G29EM3.3 ÅI=1-125
4C3JX-ray3.35 ÅI=1-125
5N61EM3.4 ÅI=1-125
9G23EM3.4 ÅI=1-125
9G26EM3.4 ÅI=1-125
6HKOEM3.42 ÅI=1-125
6RUOEM3.5 ÅI=1-125

Showing 20 of 44 experimental structures (best resolution first).

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