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glycosyl hydrolase 5 family protein isoform X3 [Oryza sativa Japonica Group]
List of domain hits
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Name | Accession | Description | Interval | E-value | |||||
BglC | COG2730 | Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]; |
70-350 | 2.26e-23 | |||||
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]; : Pssm-ID: 442036 [Multi-domain] Cd Length: 295 Bit Score: 100.50 E-value: 2.26e-23
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Ricin_B_lectin super family | cl47023 | Ricin-type beta-trefoil lectin domain; |
405-516 | 3.52e-08 | |||||
Ricin-type beta-trefoil lectin domain; The actual alignment was detected with superfamily member pfam00652: Pssm-ID: 481363 [Multi-domain] Cd Length: 126 Bit Score: 52.15 E-value: 3.52e-08
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Name | Accession | Description | Interval | E-value | |||||
BglC | COG2730 | Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]; |
70-350 | 2.26e-23 | |||||
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]; Pssm-ID: 442036 [Multi-domain] Cd Length: 295 Bit Score: 100.50 E-value: 2.26e-23
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Cellulase | pfam00150 | Cellulase (glycosyl hydrolase family 5); |
70-347 | 3.09e-12 | |||||
Cellulase (glycosyl hydrolase family 5); Pssm-ID: 395098 [Multi-domain] Cd Length: 272 Bit Score: 67.01 E-value: 3.09e-12
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Ricin_B_lectin | pfam00652 | Ricin-type beta-trefoil lectin domain; |
405-516 | 3.52e-08 | |||||
Ricin-type beta-trefoil lectin domain; Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 52.15 E-value: 3.52e-08
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beta-trefoil_Ricin_MRC-like | cd23385 | ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ... |
405-473 | 5.37e-07 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain. Pssm-ID: 467784 [Multi-domain] Cd Length: 119 Bit Score: 48.75 E-value: 5.37e-07
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RICIN | smart00458 | Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. |
405-523 | 4.06e-04 | |||||
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 40.19 E-value: 4.06e-04
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Name | Accession | Description | Interval | E-value | |||||
BglC | COG2730 | Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]; |
70-350 | 2.26e-23 | |||||
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]; Pssm-ID: 442036 [Multi-domain] Cd Length: 295 Bit Score: 100.50 E-value: 2.26e-23
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Cellulase | pfam00150 | Cellulase (glycosyl hydrolase family 5); |
70-347 | 3.09e-12 | |||||
Cellulase (glycosyl hydrolase family 5); Pssm-ID: 395098 [Multi-domain] Cd Length: 272 Bit Score: 67.01 E-value: 3.09e-12
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Ricin_B_lectin | pfam00652 | Ricin-type beta-trefoil lectin domain; |
405-516 | 3.52e-08 | |||||
Ricin-type beta-trefoil lectin domain; Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 52.15 E-value: 3.52e-08
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beta-trefoil_Ricin_MRC-like | cd23385 | ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ... |
405-473 | 5.37e-07 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain. Pssm-ID: 467784 [Multi-domain] Cd Length: 119 Bit Score: 48.75 E-value: 5.37e-07
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beta-trefoil_Ricin_AH | cd23415 | ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ... |
410-508 | 9.14e-07 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket. Pssm-ID: 467294 [Multi-domain] Cd Length: 120 Bit Score: 47.81 E-value: 9.14e-07
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beta-trefoil_Ricin_GALNT11 | cd23440 | ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ... |
405-474 | 4.94e-05 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 11 (GALNT11) and similar proteins; GALNT11 (EC 2.4.1.41), also called polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes its activation, modulating the balance between motile and immotile (sensory) cilia at the left-right organizer (LRO). GALNT11 displays the same enzyme activity toward MUC1, MUC4, and EA2 as GALNT1. It is not involved in glycosylation of erythropoietin (EPO). GALNT11 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. Pssm-ID: 467318 [Multi-domain] Cd Length: 127 Bit Score: 43.14 E-value: 4.94e-05
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beta-trefoil_Ricin_GALNT14-like | cd23441 | ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ... |
418-508 | 1.73e-04 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. Pssm-ID: 467319 [Multi-domain] Cd Length: 122 Bit Score: 41.23 E-value: 1.73e-04
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RICIN | smart00458 | Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. |
405-523 | 4.06e-04 | |||||
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 40.19 E-value: 4.06e-04
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beta-trefoil_Ricin_PTPRB-like | cd23409 | ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein ... |
405-493 | 7.27e-04 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e and similar proteins; PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, R-PTP-beta, vascular endothelial protein tyrosine phosphatase, or VE-PTP, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells, which requires the presence of plakoglobin. The subfamily corresponds to PTPRB isoform e, which contains an extra ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. Pssm-ID: 467787 Cd Length: 117 Bit Score: 39.34 E-value: 7.27e-04
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beta-trefoil_Ricin-like | cd00161 | ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ... |
405-495 | 4.84e-03 | |||||
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats. Pssm-ID: 467293 [Multi-domain] Cd Length: 134 Bit Score: 37.35 E-value: 4.84e-03
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beta-trefoil_Ricin_GALNT7 | cd23437 | ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ... |
412-473 | 8.62e-03 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. Pssm-ID: 467315 [Multi-domain] Cd Length: 124 Bit Score: 36.50 E-value: 8.62e-03
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beta-trefoil_Ricin_MytiLec-like | cd23417 | ricin B-type lectin domain, beta-trefoil fold, found in Mytilus galloprovincialis lectin ... |
401-496 | 9.64e-03 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Mytilus galloprovincialis lectin (MytiLec) and similar proteins; MytiLec is a D-galactose-binding lectin from the mussel Mytilus galloprovincialis with cytotoxicity against certain cancer cell types. It has hemagglutinating activity towards rabbit erythrocytes. It induces glycan-mediated cytotoxicity of human globotriaosylceramide-expressing lymphoma cells. The family also includes lectin from the mussel Mytilus californianus (MCL) and lectin from the sea mussel Crenomytilus grayanus (CGL). MCL is specific for binding D-galactose and N-Acetyl-d-galactosamine that contained carbohydrate moieties that were also inhibited by melibiose and raffinose. It can agglutinate all types of human erythrocytes, as well as rabbit red blood cells. CGL is specific for binding GalNAc/Gal-containing carbohydrate moieties. It displays antibacterial, antifungal, and antiviral activities. It also possesses anti-cancer activity through recognizing globotriose Gb3. Members of this family contain a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. Pssm-ID: 467296 Cd Length: 132 Bit Score: 36.55 E-value: 9.64e-03
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