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| glycoside hydrolase family 16 (GH16) protein containing a C-terminal family 6 carbohydrate binding module (CBM6), such as Streptomyces sioyaensi endo-1,3-beta-glucanase with an N-terminal domain similar to endo-1,3-beta-glucanases classified in GH16 family
beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16; Beta-GRP (beta-1, ...
175-489
1.43e-150
beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16; Beta-GRP (beta-1,3-glucan recognition protein) is one of several pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. They are present in insects and lack all catalytic residues. This subgroup also contains related proteins of unknown function that still contain the active site. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
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Pssm-ID: 185688 [Multi-domain] Cd Length: 321 Bit Score: 432.19 E-value: 1.43e-150
Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1, ...
27-132
3.51e-50
Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1,3-glucan-binding proteins involved in recognition of invading micro-organizms. It often co-occurs with pfam00722 (Glycosyl hydrolases family 16). It recognizes and binds to a triple-helical beta-1,3-glucan structure.
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Pssm-ID: 464924 Cd Length: 106 Bit Score: 166.68 E-value: 3.51e-50
beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16; Beta-GRP (beta-1, ...
175-489
1.43e-150
beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16; Beta-GRP (beta-1,3-glucan recognition protein) is one of several pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. They are present in insects and lack all catalytic residues. This subgroup also contains related proteins of unknown function that still contain the active site. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
Pssm-ID: 185688 [Multi-domain] Cd Length: 321 Bit Score: 432.19 E-value: 1.43e-150
Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1, ...
27-132
3.51e-50
Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1,3-glucan-binding proteins involved in recognition of invading micro-organizms. It often co-occurs with pfam00722 (Glycosyl hydrolases family 16). It recognizes and binds to a triple-helical beta-1,3-glucan structure.
Pssm-ID: 464924 Cd Length: 106 Bit Score: 166.68 E-value: 3.51e-50
beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16; Beta-GRP (beta-1, ...
175-489
1.43e-150
beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16; Beta-GRP (beta-1,3-glucan recognition protein) is one of several pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. They are present in insects and lack all catalytic residues. This subgroup also contains related proteins of unknown function that still contain the active site. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
Pssm-ID: 185688 [Multi-domain] Cd Length: 321 Bit Score: 432.19 E-value: 1.43e-150
Coelomic cytolytic factor, member of glycosyl hydrolase family 16; Subgroup of glucanases of ...
175-489
1.24e-50
Coelomic cytolytic factor, member of glycosyl hydrolase family 16; Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
Pssm-ID: 185694 Cd Length: 330 Bit Score: 175.51 E-value: 1.24e-50
Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1, ...
27-132
3.51e-50
Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1,3-glucan-binding proteins involved in recognition of invading micro-organizms. It often co-occurs with pfam00722 (Glycosyl hydrolases family 16). It recognizes and binds to a triple-helical beta-1,3-glucan structure.
Pssm-ID: 464924 Cd Length: 106 Bit Score: 166.68 E-value: 3.51e-50
Laminarinase, member of the glycosyl hydrolase family 16; Laminarinase, also known as glucan ...
177-488
7.13e-27
Laminarinase, member of the glycosyl hydrolase family 16; Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.
Pssm-ID: 185693 [Multi-domain] Cd Length: 235 Bit Score: 108.48 E-value: 7.13e-27
glycosyl hydrolase family 16; The O-Glycosyl hydrolases are a widespread group of enzymes that ...
179-394
1.85e-12
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: 66.31 E-value: 1.85e-12
Beta-agarase, member of glycosyl hydrolase family 16; Beta-agarase is a glycosyl hydrolase ...
179-390
2.83e-06
Beta-agarase, member of glycosyl hydrolase family 16; Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.
Pssm-ID: 185687 Cd Length: 258 Bit Score: 48.89 E-value: 2.83e-06
glycosylphosphatidylinositol-glucanosyltransferase; Group of fungal GH16 members related to ...
369-390
1.67e-04
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: 42.92 E-value: 1.67e-04
lichenase, member of glycosyl hydrolase family 16; Lichenase, also known as 1,3-1, ...
359-391
1.19e-03
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: 40.33 E-value: 1.19e-03
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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