Protein Family Models

L-type (leguminous) lectin family protein binds carbohydrates using a a dome-shaped beta-barrel carbohydrate recognition domain

Date:

2023-10-25

glycoside hydrolase family 97 protein with secretion system C-terminal sorting domain

Date:

2023-10-13

1,4-alpha-glucan branching protein transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain

Date:

2023-09-25

carbohydrate binding domain-containing protein similar to Cellulomonas fimi endoglucanase CenC and Rhodothermus marinus xylanase

Date:

2023-09-05

This is a mannan-specific carbohydrate binding domain, previously known as the X4 module [1]. Unlike other carbohydrate binding modules, binding to substrate causes a conformational change [2]. (from Pfam)

Date:

2023-11-06

CBM9_2 is a family of putative endoxylanase-like proteins that belong to the Carbohydrate-binding family 9. (from Pfam)

Date:

2023-11-05

The H-type lectin domain is a unit of six beta chains, combined into a homo-hexamer. It is involved in self/non-self recognition of cells, through binding with carbohydrates [1]. It is sometimes found in association with the F5_F8_type_C domain Pfam:PF00754. (from Pfam)

Date:

2023-11-03

This domain is found at the N-terminus of beta-1,3-glucan-binding proteins involved in recognition of invading micro-organisms. It often co-occurs with Pfam:PF00722 (Glycosyl hydrolases family 16). It recognises and binds to a triple-helical beta-1,3-glucan structure [1-2]. (from Pfam)

Date:

2023-11-08

Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan [1]. (from Pfam)

Date:

2023-11-05

This is a carbohydrate binding domain which has been shown in Schizosaccharomyces pombe to be required for septum localisation [1]. (from Pfam)

Date:

2023-11-03

This domain is found at the C terminal of cellulases and in vitro binding studies have shown it to binds to crystalline cellulose [1]. (from Pfam)

Date:

2023-11-03

Fve is a major fruiting body protein from Flammulina velutipes, a mushroom possessing immunomodulatory activity. It stimulates lymphocyte mitogenesis, suppresses systemic anaphylaxis reactions and oedema, enhances transcription of IL-2, IFN-gamma and TNF-alpha, and haemagglutinates red blood cells. It appears to be a lectin with specificity for complex cell-surface carbohydrates. Fve adopts a tertiary structure consisting of an immunoglobulin-like beta-sandwich, with seven strands arranged in two beta sheets, in a Greek-key topology. It forms a non-covalently linked homodimer containing no Cys, His or Met residues; dimerisation occurs by 3-D domain swapping of the N-terminal helices and is stabilised predominantly by hydrophobic interactions [1]. (from Pfam)

Date:

2023-11-03

This entry represents a domain found in prokaryotic alpha-amylase and 4-alpha-glucanotransferase. It adopts a beta-sandwich fold, in which two layers of anti-parallel beta-sheets are arranged in a nearly parallel fashion. The exact function of this family is, as yet, unknown, however it has been proposed that they may play a role in transglycosylation reactions [1]. (from Pfam)

Date:

2023-11-03

CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerisation. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar [1]. (from Pfam)

Date:

2023-11-02

Members of this family are found in both fungi, bacteria and wood-eating arthropods. The domain is found at the N-terminus of rhamnogalacturonase B, a member of the polysaccharide lyase family 4. The domain adopts a structure consisting of a beta super-sandwich, with eighteen strands in two beta-sheets [1]. The three domains of the whole protein rhamnogalacturonan lyase (RGL4), are involved in the degradation of rhamnogalacturonan-I, RG-I, an important pectic plant cell-wall polysaccharide. The active-site residues are a lysine at position 169 in UniProtKB:Q00019 and a histidine at 229, Lys169 is likely to be a proton abstractor, His229 a proton donor in the mechanism. The substrate is a disaccharide, and RGL4, in contrast to other rhamnogalacturonan hydrolases, cleaves the alpha-1,4 linkages of RG-I between Rha and GalUA through a beta-elimination resulting in a double bond in the nonreducing GalUA residue, and is thus classified as a polysaccharide lyase (PL) [2]. (from Pfam)

Date:

2023-11-03

Date:

2023-11-01

This short domain is found in many different glycosyl hydrolase enzymes and is presumed to have a carbohydrate binding function. The domain has six aromatic groups that may be important for binding. (from Pfam)

Date:

2023-11-22

PapG, the adhesin of the P-pili, is situated at the tip and is only a minor component of the whole pilus structure. A two-domain structure has been postulated for PapG; a carbohydrate binding N-terminus (this domain) and chaperone binding C-terminus. The carbohydrate-binding domain interacts with the receptor glycan [1,2]. (from Pfam)

Date:

2023-11-01

This probable domain is found in bacterial transcriptional regulators such as DeoR and SorC. These proteins have an amino-terminal helix-turn-helix Pfam:PF00325 that binds to DNA. This domain is probably the ligand regulator binding region. SorC is regulated by sorbose and other members of this family are likely to be regulated by other sugar substrates. (from Pfam)

Date:

2023-11-02

Domain is found in pullanase - carbohydrate de-branching - proteins. It is found both to the N or the C terminii of of the alpha-amylase active site region. This domain contains several conserved aromatic residues that are suggestive of a carbohydrate binding function. (from Pfam)

Date:

2023-11-02