Protein Family Models

This is a short helical bundle domain found associated with the catalytic domain of the TcdB toxin from C. difficile [1]. The function of this domain is unknown, but it may be involved in substrate recognition. [1]. 16054646. Structural basis for the function of Clostridium difficile toxin B. Reinert DJ, Jank T, Aktories K, Schulz GE;. J Mol Biol. 2005;351:973-981. (from Pfam)

Date:

2024-10-16

This domain represents the N-terminal glycosyltransferase from a set of toxins found in some bacteria. This domain in TcdB glycosylates the host RhoA protein. [1]. 16054646. Structural basis for the function of Clostridium difficile toxin B. Reinert DJ, Jank T, Aktories K, Schulz GE;. J Mol Biol. 2005;351:973-981. (from Pfam)

Date:

2024-10-16

This family of proteins is functionally uncharacterised. This protein is found in bacteria. Proteins in this family are typically between 286 to 3225 amino acids in length. This protein is found associated with Pfam:PF04488. This protein is found associated with Pfam:PF04488. (from Pfam)

Date:

2024-08-14

The DXD motif is a short conserved motif found in many families of glycosyltransferases, which add a range of different sugars to other sugars, phosphates and proteins. DXD-containing glycosyltransferases all use nucleoside diphosphate sugars as donors and require divalent cations, usually manganese. The DXD motif is expected to play a carbohydrate binding role in sugar-nucleoside diphosphate and manganese dependent glycosyltransferases [1]. [1]. 9653120. Activity of the yeast MNN1 alpha-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases. Wiggins CA, Munro S;. Proc Natl Acad Sci U S A 1998;95:7945-7950. (from Pfam)

Date:

2024-10-16

The HMM represents a cysteine protease domain found in proteins of bacteria that include plant pathogens (Pseudomonas syringae), root nodule bacteria, and intracellular pathogens (e.g. Yersinia pestis, Haemophilus ducreyi, Pasteurella multocida, Chlamydia trachomatis) of animal hosts. The domain features a catalytic triad of Cys, His, and Asp. Sequences can be extremely divergent outside of a few well-conserved motifs, and additional members may exist that are detected by this model. YopT, a virulence effector protein of Yersinia pestis, cleaves and releases host cell Rho GTPases from the membrane, thereby disrupting the actin cytoskeleton. Members of the family from pathogenic bacteria are likely to be pathogenesis factors.

Date:

2024-05-30