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, 8 hours ago.
About this proteome
Extracted from UniProtKB
Thermophilic, methanogenic, autotrophic and strict anaerobic organism. It was originally isolated from a sediment sample collected from the sea floor surface at the base of a 2600 m-deep "white smoker" chimney located on the East Pacific Rise. It grows at pressures of up to more than 200 atm and over a temperature range of 48 to 94 degrees Celsius, with an optimum near 85 degrees Celsius.
What is included
This atlas covers the reviewed entries of this proteome — the manually curated Swiss-Prot section of UniProtKB. Every entry in this proteome is reviewed, so nothing is left out.
- UniProt proteome
- UP000000805
- Taxonomy
- 243232 · METJA
- Proteome type
- Reference proteome
- Strain
- ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440
- Superkingdom
- archaea
- Genome assembly
- GCA_000091665.1 · ENA/EMBL
- Completeness (BUSCO)
- 98% · 941/958
Source: UniProt proteome UP000000805, last modified 5 Dec 2025. Retrieved 19 Aug 2026 (2 days, 7 hours ago) and cached for a week.
What do we provide?
Sequence-based predictions that help explain the behaviour of the proteins in the hyperthermophilic methanogen 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.