DICHOT prediction of structural domains and intrinsically disordered regions is now available. Try sample 6.


We apologize that FUJI db has been down due to the hardware failure since mid-October. It is back now.

FUJI Database

To any user-specified protein the Functionally Annotated Japanese Protein Structural Information (FUJI) database expeditiously identifies various relevant data including structural information and displays them. For details of instruction on the use and database description, refer to the following outlines.

This work was supported by the Targeted Proteins Research Program (TPRP) from the Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan.

[Use the FUJI database]

How to use

Step1.Input the amino acid sequence of a protein.

Step1 Input an amino acid sequence in one letter symbols and specify the species classification and the number of homologs to output in the next step.

Step2.Homolog search and determination of the most conserved region.

Step2 Homologs are displayed together with structurally aligned regions and the most conserved region. The user can not only modify the homologs and re-identify the most conserved region, but also edit the region itself.

Step3.Linear display of the protein.

Step3 Alignments to PDB and SCOP structures are displayed linearly, with the N-terminus shown at the left. In the same screen are shown Pfam and SMART domain alignments, the most conserved region, predicted disordered, SEG, and coiled-coil regions, the prediction of a signal sequence, trans-membrane domains, subcellular localization, and function.

Step4.Three dimensional display of the protein.

Step4 If structural alignments exist, the aligned regions are displayed three dimensionally. Unaligned regions, gaps in PDB coordinates, the inside and outside of the protein molecule, and the most conserved region are also presented.