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, ...
175-491
1.22e-149
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: 429.88 E-value: 1.22e-149
Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1, ...
21-124
2.49e-39
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: 138.17 E-value: 2.49e-39
beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16; Beta-GRP (beta-1, ...
175-491
1.22e-149
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: 429.88 E-value: 1.22e-149
Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1, ...
21-124
2.49e-39
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: 138.17 E-value: 2.49e-39
beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16; Beta-GRP (beta-1, ...
175-491
1.22e-149
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: 429.88 E-value: 1.22e-149
Coelomic cytolytic factor, member of glycosyl hydrolase family 16; Subgroup of glucanases of ...
175-491
5.09e-59
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: 197.47 E-value: 5.09e-59
Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1, ...
21-124
2.49e-39
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: 138.17 E-value: 2.49e-39
Laminarinase, member of the glycosyl hydrolase family 16; Laminarinase, also known as glucan ...
177-490
8.36e-24
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: 99.62 E-value: 8.36e-24
glycosyl hydrolase family 16; The O-Glycosyl hydrolases are a widespread group of enzymes that ...
269-430
1.67e-04
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: 42.81 E-value: 1.67e-04
glycosylphosphatidylinositol-glucanosyltransferase; Group of fungal GH16 members related to ...
376-398
1.36e-03
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: 39.84 E-value: 1.36e-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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Functional characterization of the conserved domain architecture found on the query.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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