LamG (Laminin G) domain-containing protein may serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
21-281
1.33e-122
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
The actual alignment was detected with superfamily member cd02176:
Pssm-ID: 473984 [Multi-domain] Cd Length: 263 Bit Score: 350.73 E-value: 1.33e-122
Xyloglucan endotransglycosylase, member of glycosyl hydrolase family 16; Xyloglucan ...
21-281
1.33e-122
Xyloglucan endotransglycosylase, member of glycosyl hydrolase family 16; Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers in plant cell walls via a transglycosylation mechanism. Xyloglucan is a soluble hemicellulose with a backbone of beta-1,4-linked glucose units, partially substituted with alpha-1,6-linked xylopyranose branches. It binds noncovalently to cellulose, cross-linking the adjacent cellulose microfibrils, giving it a key structural role as a matrix polymer. Therefore, XET plays an important role in all plant processes that require cell wall remodeling.
Pssm-ID: 185685 [Multi-domain] Cd Length: 263 Bit Score: 350.73 E-value: 1.33e-122
Xyloglucan endotransglycosylase, member of glycosyl hydrolase family 16; Xyloglucan ...
21-281
1.33e-122
Xyloglucan endotransglycosylase, member of glycosyl hydrolase family 16; Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers in plant cell walls via a transglycosylation mechanism. Xyloglucan is a soluble hemicellulose with a backbone of beta-1,4-linked glucose units, partially substituted with alpha-1,6-linked xylopyranose branches. It binds noncovalently to cellulose, cross-linking the adjacent cellulose microfibrils, giving it a key structural role as a matrix polymer. Therefore, XET plays an important role in all plant processes that require cell wall remodeling.
Pssm-ID: 185685 [Multi-domain] Cd Length: 263 Bit Score: 350.73 E-value: 1.33e-122
glycosylphosphatidylinositol-glucanosyltransferase; Group of fungal GH16 members related to ...
83-222
6.91e-25
glycosylphosphatidylinositol-glucanosyltransferase; Group of fungal GH16 members related to Saccharomyces cerevisiae Crh1p. Chr1p and Crh2p are transglycosylases that are required for the linkage of chitin to beta(1-3)glucose branches of beta(1-6)glucan, an important step in the assembly of new cell wall. Both have been shown to be glycosylphosphatidylinositol (GPI)-anchored. A third homologous protein, Crr1p, functions in the formation of the spore wall. They belongs to the family 16 of glycosyl hydrolases that includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.
Pssm-ID: 185692 [Multi-domain] Cd Length: 203 Bit Score: 98.39 E-value: 6.91e-25
lichenase, member of glycosyl hydrolase family 16; Lichenase, also known as 1,3-1, ...
56-215
9.78e-23
lichenase, member of glycosyl hydrolase family 16; Lichenase, also known as 1,3-1,4-beta-glucanase, is a member of glycosyl hydrolase family 16, that specifically cleaves 1,4-beta-D-glucosidic bonds in mixed-linked beta glucans that also contain 1,3-beta-D-glucosidic linkages. Natural substrates of beta-glucanase are beta-glucans from grain endosperm cell walls or lichenan from the Islandic moss, Cetraria islandica. This protein is found not only in bacteria but also in anaerobic fungi. This domain includes two seven-stranded antiparallel beta-sheets that are adjacent to one another forming a compact, jellyroll beta-sandwich structure.
Pssm-ID: 185684 [Multi-domain] Cd Length: 212 Bit Score: 93.10 E-value: 9.78e-23
glycosyl hydrolase family 16; The O-Glycosyl hydrolases are a widespread group of enzymes that ...
42-208
1.92e-19
glycosyl hydrolase family 16; The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.
Pssm-ID: 185683 [Multi-domain] Cd Length: 210 Bit Score: 84.02 E-value: 1.92e-19
Xyloglucan endo-transglycosylase (XET) C-terminus; This family represents the C-terminus ...
235-281
1.25e-14
Xyloglucan endo-transglycosylase (XET) C-terminus; This family represents the C-terminus (approximately 60 residues) of plant xyloglucan endo-transglycosylase (XET). Xyloglucan is the predominant hemicellulose in the cell walls of most dicotyledons. With cellulose, it forms a network that strengthens the cell wall. XET catalyzes the splitting of xyloglucan chains and the linking of the newly generated reducing end to the non-reducing end of another xyloglucan chain, thereby loosening the cell wall. Note that all family members contain the pfam00722 domain.
Pssm-ID: 429210 [Multi-domain] Cd Length: 48 Bit Score: 66.54 E-value: 1.25e-14
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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