Protein Family Models

RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding (e.g. [1]). Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain [2]. [1]. 10341219. Teneurin-1, a vertebrate homologue of the Drosophila pair-rule gene ten-m, is a neuronal protein with a novel type of heparin-binding domain. Minet AD, Rubin BP, Tucker RP, Baumgartner S, Chiquet-Ehrismann R;. J Cell Sci 1999;112:2019-2032. [2]. 23913273. The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device. Busby JN, Panjikar S, Landsberg MJ, Hurst MR, Lott JS;. Nature. 2013;501:547-550. (from Pfam)

Date:

2024-10-29

This HMM describes two tandem copies of a 21-residue extracellular repeat found in Gram-negative, Gram-positive, and animal proteins. The repeat is named for a YD dipeptide, the most strongly conserved motif of the repeat. These repeats appear in general to be involved in binding carbohydrate; the chicken teneurin-1 YD-repeat region has been shown to bind heparin.

Date:

2024-10-29