Structural exploration

Predicted Protein Structures

Find UniProt matches for SAR11 proteins and inspect available AlphaFoldDB predictions in an interactive 3D viewer.

Explore exact, close, and more distant homologous UniProt sequence matches with available AlphaFoldDB structure references, covering 2,994 of 4,577 SAR11 orthogroups.

The complete DIAMOND similarity-search results and compact structure-reference tables are provided through the Download page. See the Protein Structures Wiki for the mapping workflow and interpretation guidance.

Structure coverage

Orthogroup coverage

Exact and close matches are preferred; distant homologous matches fill OGs without either.

Exact sequence match Identity 100%; query and subject coverage 100% 30.8%
Close sequence match Identity ≥85%; query and subject coverage ≥80%; exact matches excluded 6.1%
Distant homologous match Identity ≥30%; query and subject coverage ≥80%; E-value ≤1e-5 28.6%
No qualifying reference 34.6%

3D inspection

AlphaFoldDB structure viewer

Enter a UniProt accession to view its available AlphaFoldDB prediction in Mol* and open the model in Foldseek for structural homology searches.

Search by accession, OG ID, gene name, SAR11 gene ID, genome, KO ID, or COG ID.
Open Mol* in full screen

Data note: UniProtKB/TrEMBL applies proteome redundancy reduction, so some previously registered sequences may have been removed. If a structure is unavailable, check UniParc for historical sequence records.

Accession lookup

SAR11 protein matches in UniProt

Search by orthogroup, gene, genome, accession, or annotation. Select an accession to load its AlphaFoldDB model above.

Open the match table in full screen

Sequence-match classes: Exact matches require 100% identity and 100% query and subject coverage. Close matches require identity ≥85% and both coverage values ≥80%, excluding exact matches. Distant homologous matches require identity ≥30%, both coverage values ≥80%, and E-value ≤1e-5. Only accessions with a confirmed AlphaFoldDB model are shown as structure references. Read the full methodology.