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 40 minutes ago.
About this proteome
Extracted from UniProtKB
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / IFO 14742 / NCIMB 2012 / DS2) is a moderate halophilic archaeon isolated from bottom sediment from the Dead Sea. It is named in honour of Benjamin Volcani who pioneered the microbiology of the Dead Sea. H.volcanii possesses the properties of the halobacteria, but differs from the known species in two important respects; the cells are disc shaped and often cupped when grown under optimum conditions, and the optimum requirements for sodium chloride is in the range 1.7-2.5 molar which is about half of that generally reported for the halobacteria. The optimum sodium chloride concentration for growth is close to that found in the Dead Sea and the tolerance for magnesium chloride is very high (adapted from PMID: 1190944 and 20333302). A number of strains of DS2 have been derived for use in transformation, among them are DS70 (see PMID 11283291), WFD11 (see PMID 2825193) and WR 340 (see PMID 12533452).
What is included
This atlas covers the reviewed entries of this proteome — the manually curated Swiss-Prot section of UniProtKB. That is 5.2% of it. The other 3,718 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
- UP000008243
- Taxonomy
- 309800 · HALVD
- Proteome type
- Reference proteome
- Strain
- ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
- Superkingdom
- archaea
- Genome assembly
- GCA_000025685.1 · ENA/EMBL
- Completeness (BUSCO)
- 99% · 899/904
Source: UniProt proteome UP000008243, last modified 5 Dec 2025. Retrieved 19 Aug 2026 (3 days, 1 hour ago) and cached for a week.
What do we provide?
Sequence-based predictions that help explain the behaviour of the proteins in the halophilic archaeon 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.