RHS repeat-associated core domain. This model represents a conserved unique core sequence shared by large numbers of proteins. It is occasional in the Archaea Methanosarcina barkeri) but common in bacteria and eukaryotes. Most fall into two large classes. One class consists of long proteins in which two classes of repeats are abundant: an FG-GAP repeat (pfam01839) class, and an RHS repeat (pfam05593) or YD repeat (TIGR01643). This class includes secreted bacterial insecticidal toxins and intercellular signalling proteins such as the teneurins in animals. The other class consists of uncharacterized proteins shorter than 400 amino acids, where this core domain of about 75 amino acids tends to occur in the N-terminal half. Over twenty such proteins are found in Pseudomonas putida alone; little sequence similarity or repeat structure is found among these proteins outside the region modeled by this domain.

Uncharacterized conserved protein RhsA, contains 28 RHS repeats [General function prediction only].

RHS Repeat. RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. 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.

YD repeat (two copies). This model 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.

RHS Repeat. RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. 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.

ChainG, TccC2 [Photorhabdus luminescens]

CrystalStructure of TcdB2-TccC3-Cdc42 [Photorhabdus luminescens]

CrystalStructure of TcdB2-TccC3 without hypervariable C-terminal region [Photorhabdus luminescens]

CrystalStructure of TcdB2-TccC3 [Photorhabdus luminescens]

CrystalStructure of TcdB2-TccC3-TEV [Photorhabdus luminescens]

tRNA nuclease WapA OS=Bacillus subtilis (strain 168) OX=224308 GN=wapA PE=1 SV=2

tRNA3(Ser)-specific nuclease WapA OS=Bacillus spizizenii (strain DSM 15029 / JCM 12233 / NBRC 101239 / NRRL B-23049 / TU-B-10) OX=1052585 GN=wapA PE=1 SV=1

tRNA(Glu)-specific nuclease WapA OS=Bacillus subtilis subsp. natto (strain BEST195) OX=645657 GN=wapA PE=1 SV=2

Double-stranded DNA deaminase toxin A OS=Burkholderia cenocepacia (strain H111) OX=1055524 GN=dddA PE=1 SV=1

Protein RhsD OS=Escherichia coli (strain K12) OX=83333 GN=rhsD PE=2 SV=3