Traditionally, proteins are described in a single static state (a picture). It is now increasingly recognised that many proteins can adopt multiple states and move between these conformational states dynamically (a movie). Even more, not every protein has a well-defined three-dimensional structure, many are partly or fully disordered. These predictions describe backbone and side-chain dynamics, disorder, early folding events, beta-sheet aggregation and phase separation.
In this atlas
Entries here
Genes
Chromosomes
Reviewed in UniProt
Last updated 2 days, 4 hours ago.
About this proteome
Extracted from UniProtKB
Thermus thermophilus is an extremely thermophilic, halotolerant bacterium. It was isolated from a natural thermal environment in Japan. It has an optimal growth temperature of about 85 degrees Celsius. T.thermophilus has become a model organism in structural biology and some of its enzymes have a biotechnological application.
What is included
This atlas covers the reviewed entries of this proteome — the manually curated Swiss-Prot section of UniProtKB. That is 19.7% of it. The other 1,788 entries are unreviewed (TrEMBL) and are not included, which is why the count above is smaller than the proteome. You can run the same predictions on any of them yourself in the online predictors.
- UniProt proteome
- UP000000532
- Taxonomy
- 300852 · THET8
- Proteome type
- Reference proteome
- Strain
- ATCC 27634 / DSM 579 / HB8
- Superkingdom
- bacteria
- Genome assembly
- GCA_000091545.1 · ENA/EMBL
- Completeness (BUSCO)
- 91% · 109/124
Source: UniProt proteome UP000000532, last modified 5 Dec 2025. Retrieved 19 Aug 2026 (2 days, 5 hours ago) and cached for a week.
What do we provide?
Sequence-based predictions that help explain the behaviour of the proteins in the thermus thermophilus hb8 proteome. Not all of these proteins, or regions of them, have a well-defined three-dimensional structure as available from the PDB; many are dynamic or ambiguous. These predictions give clues as to how such regions behave.
- DynaMine
- backbone and side-chain dynamics
- DisoMine
- disorder
- EFoldMine
- early folding
- AgMata
- beta-sheet aggregation
- PSPer
- phase separation
How do I proceed?
Open the entry list and click a UniProt accession. Each entry page carries:
- Overview — every prediction on one plot.
- Interpretation — disorder classified as order, transition or disorder.
- Values and Statistics — the numbers behind the plots.
- Sequence — residues coloured by prediction.
- PSP — phase-separation propensity.
- Visualization 1D-3D — a 3D model coloured by prediction.
- Downloads — sequence, predictions and structures.
Prefer code? Everything is available through the REST API.