lectin [uncultured Acidovorax sp.]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| lectin_2 | NF035930 | lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ... |
29-263 | 4.18e-121 | ||||
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor. : Pssm-ID: 468267 [Multi-domain] Cd Length: 238 Bit Score: 345.23 E-value: 4.18e-121
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| Name | Accession | Description | Interval | E-value | ||||
| lectin_2 | NF035930 | lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ... |
29-263 | 4.18e-121 | ||||
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor. Pssm-ID: 468267 [Multi-domain] Cd Length: 238 Bit Score: 345.23 E-value: 4.18e-121
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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 ... |
152-263 | 2.05e-29 | ||||
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: 107.84 E-value: 2.05e-29
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| Ricin_B_lectin | pfam00652 | Ricin-type beta-trefoil lectin domain; |
145-263 | 1.09e-19 | ||||
Ricin-type beta-trefoil lectin domain; Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 82.19 E-value: 1.09e-19
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| RICIN | smart00458 | Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. |
145-265 | 7.43e-15 | ||||
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 69.08 E-value: 7.43e-15
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| Name | Accession | Description | Interval | E-value | ||||
| lectin_2 | NF035930 | lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ... |
29-263 | 4.18e-121 | ||||
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor. Pssm-ID: 468267 [Multi-domain] Cd Length: 238 Bit Score: 345.23 E-value: 4.18e-121
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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 ... |
152-263 | 2.05e-29 | ||||
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: 107.84 E-value: 2.05e-29
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| beta-trefoil_Ricin_XLN-like | cd23418 | ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ... |
152-265 | 5.62e-28 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with 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. Each subdomain may contain a potential sugar-binding pocket. Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 103.97 E-value: 5.62e-28
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| beta-trefoil_Ricin_laminarinase | cd23451 | ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ... |
152-263 | 2.23e-26 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal ricin B-type lectin domain with 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. Each subdomain bears a potential sugar binding site. Pssm-ID: 467329 [Multi-domain] Cd Length: 125 Bit Score: 99.71 E-value: 2.23e-26
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| beta-trefoil_Ricin_RPI | cd23452 | ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ... |
153-264 | 9.65e-22 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine protease I (RPI) and similar proteins; RPI, also called serine protease 1, is a major serine protease exhibiting lytic activity toward living yeast cells. It has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI. RPI contains a C-terminal 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 bears a potential sugar binding site. Pssm-ID: 467330 [Multi-domain] Cd Length: 125 Bit Score: 87.57 E-value: 9.65e-22
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| beta-trefoil_Ricin_XLN-like | cd23418 | ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ... |
143-222 | 5.75e-20 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with 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. Each subdomain may contain a potential sugar-binding pocket. Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 83.17 E-value: 5.75e-20
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| Ricin_B_lectin | pfam00652 | Ricin-type beta-trefoil lectin domain; |
145-263 | 1.09e-19 | ||||
Ricin-type beta-trefoil lectin domain; Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 82.19 E-value: 1.09e-19
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| beta-trefoil_Ricin_GALNT14-like | cd23441 | ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ... |
150-263 | 3.55e-18 | ||||
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: 77.83 E-value: 3.55e-18
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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 ... |
192-265 | 2.41e-17 | ||||
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: 76.25 E-value: 2.41e-17
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| beta-trefoil_Ricin_Pgant9-like | cd23462 | ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ... |
145-265 | 7.15e-17 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function 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. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the C-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 bears a potential sugar binding site. Pssm-ID: 467340 [Multi-domain] Cd Length: 126 Bit Score: 74.71 E-value: 7.15e-17
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| beta-trefoil_Ricin_AgaB34-like | cd23458 | ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ... |
153-263 | 1.54e-16 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts 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 bears a potential sugar binding site. Pssm-ID: 467336 [Multi-domain] Cd Length: 135 Bit Score: 73.90 E-value: 1.54e-16
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| beta-trefoil_Ricin_GALNT7 | cd23437 | ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ... |
142-265 | 1.70e-16 | ||||
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: 73.48 E-value: 1.70e-16
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| RICIN | smart00458 | Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. |
145-265 | 7.43e-15 | ||||
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 69.08 E-value: 7.43e-15
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| beta-trefoil_Ricin_Pgant1-like | cd23459 | ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ... |
141-265 | 6.44e-14 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 1 (Pgant1) and similar proteins; Pgant1, also called pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, functions as a GalNAc transferase (EC 2.4.1.41) that 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. Pgant1 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers the monoglycosylated Muc5AC-3 as a substrate. Members of this subfamily contain a ricin B-type lectin domain at the C-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 bears a potential sugar binding site. Pssm-ID: 467337 [Multi-domain] Cd Length: 132 Bit Score: 66.96 E-value: 6.44e-14
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| beta-trefoil_Ricin_GALNT2 | cd23434 | ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ... |
150-263 | 1.81e-12 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, 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. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 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: 467312 [Multi-domain] Cd Length: 121 Bit Score: 62.72 E-value: 1.81e-12
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| beta-trefoil_Ricin_SCDase | cd23456 | ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ... |
152-263 | 6.36e-12 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-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: 467334 [Multi-domain] Cd Length: 122 Bit Score: 61.22 E-value: 6.36e-12
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| beta-trefoil_Ricin_GALNT10-like | cd23439 | ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ... |
142-265 | 1.02e-10 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10)-like subfamily; The GALNT10-like subfamily includes GALNT10 and GALNTL6. 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. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. 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: 467317 [Multi-domain] Cd Length: 126 Bit Score: 58.12 E-value: 1.02e-10
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| beta-trefoil_Ricin_RPI | cd23452 | ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ... |
146-221 | 1.09e-10 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine protease I (RPI) and similar proteins; RPI, also called serine protease 1, is a major serine protease exhibiting lytic activity toward living yeast cells. It has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI. RPI contains a C-terminal 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 bears a potential sugar binding site. Pssm-ID: 467330 [Multi-domain] Cd Length: 125 Bit Score: 57.91 E-value: 1.09e-10
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| Ricin_B_lectin | pfam00652 | Ricin-type beta-trefoil lectin domain; |
186-265 | 1.91e-10 | ||||
Ricin-type beta-trefoil lectin domain; Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 57.16 E-value: 1.91e-10
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| beta-trefoil_Ricin_RIPs_II_rpt2 | cd23444 | second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ... |
152-263 | 2.67e-10 | ||||
second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating proteins (RIPs); Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. They consist of a catalytic A-chain which has rRNA N-glycosidase activity and a lectin B-chain containing two ricin B-type lectin domains 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 lectin chain facilitates the internalization of the catalytic chain on binding to the cell surface. The two chains are connected by a disulfide bridge. This model corresponds to the second ricin B-type lectin domain. Members of this family includes Ricinus communis ricin, bitter gourd (Momordica charantia) seed lectin (BGSL), snake gourd (Trichosanthes anguina) seed lectin (SGSL), Sambucus ebulus ebulin I, Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf, Abrus precatorius abrin (ABR) and agglutinin-I (AAG), and Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs). Pssm-ID: 467322 [Multi-domain] Cd Length: 122 Bit Score: 56.51 E-value: 2.67e-10
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| beta-trefoil_Ricin_GALNT14-like | cd23441 | ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ... |
186-263 | 1.14e-09 | ||||
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: 55.10 E-value: 1.14e-09
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| beta-trefoil_Ricin_SCDase | cd23456 | ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ... |
191-263 | 1.46e-09 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-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: 467334 [Multi-domain] Cd Length: 122 Bit Score: 54.67 E-value: 1.46e-09
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| beta-trefoil_Ricin_AgaB34-like | cd23458 | ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ... |
194-264 | 1.50e-09 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts 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 bears a potential sugar binding site. Pssm-ID: 467336 [Multi-domain] Cd Length: 135 Bit Score: 55.02 E-value: 1.50e-09
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| beta-trefoil_Ricin_AH | cd23415 | ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ... |
148-263 | 2.37e-08 | ||||
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: 51.28 E-value: 2.37e-08
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| beta-trefoil_Ricin_GALNT1-like | cd23433 | ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ... |
145-263 | 2.83e-08 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1)-like subfamily; The GALNT1-like subfamily includes GALNT1 and GALNT13. They 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. GALNT1 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT13 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. 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: 467311 [Multi-domain] Cd Length: 127 Bit Score: 51.16 E-value: 2.83e-08
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| beta-trefoil_Ricin_AgaB34-like | cd23458 | ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ... |
152-221 | 3.77e-08 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts 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 bears a potential sugar binding site. Pssm-ID: 467336 [Multi-domain] Cd Length: 135 Bit Score: 51.17 E-value: 3.77e-08
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| beta-trefoil_Ricin_Pgant3-like | cd23460 | ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ... |
151-263 | 7.87e-08 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 3 (Pgant3) and similar proteins; Pgant3, also called pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, functions as a GalNAc transferase (EC 2.4.1.41) that 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. Pgant3 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers EA2 as a substrate and has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Pgant3 plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. It may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Together with Pgant35A, Pgant3 regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles. Members of this subfamily contain a ricin B-type lectin domain at the C-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 bears a potential sugar binding site. Pssm-ID: 467338 [Multi-domain] Cd Length: 121 Bit Score: 49.75 E-value: 7.87e-08
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| beta-trefoil_Ricin_RIPs_II_rpt1 | cd23443 | first ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ... |
182-257 | 1.11e-07 | ||||
first ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating proteins (RIPs); Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. They consist of a catalytic A-chain which has rRNA N-glycosidase activity and a lectin B-chain containing two ricin B-type lectin domains 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 lectin chain facilitates the internalization of the catalytic chain on binding to the cell surface. The two chains are connected by a disulfide bridge. This model corresponds to the first ricin B-type lectin domain. Members of this subfamily includes Ricinus communis ricin, bitter gourd (Momordica charantia) seed lectin (BGSL), snake gourd (Trichosanthes anguina) seed lectin (SGSL), Sambucus ebulus ebulin I, Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf, Abrus precatorius abrin (ABR) and agglutinin-I (AAG), and Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs). Pssm-ID: 467321 [Multi-domain] Cd Length: 123 Bit Score: 49.21 E-value: 1.11e-07
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| beta-trefoil_Ricin_CELIII-like_rpt2 | cd23420 | second ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2 ... |
143-265 | 2.30e-07 | ||||
second ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2+-dependent hemolytic lectin CEL-III and similar proteins; CEL-III is a Ca2+-dependent and galactose-specific lectin that exhibits hemolytic and hemagglutinating activities. It functions as an oligomer that forms an ion-permeable pore in the cell membrane. CEL-III consists of three domains: two N-terminal ricin B-type lectin domains, and a C-terminal pore-forming domain. The ricin B-type lectin domains show a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. The model corresponds to the second ricin B-type lectin domain. Pssm-ID: 467299 [Multi-domain] Cd Length: 133 Bit Score: 48.70 E-value: 2.30e-07
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| beta-trefoil_Ricin_CRYBG2 | cd23465 | ricin B-type lectin domain, beta-trefoil fold, found in beta/gamma crystallin ... |
200-263 | 2.46e-07 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in beta/gamma crystallin domain-containing protein 2 (CRYBG2) and similar proteins; CRYBG2, also called absent in melanoma 1-like protein (AIM1L), is a beta/gamma-crystallin family protein with a ricin B-type lectin domain at the C-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: 467343 Cd Length: 136 Bit Score: 48.71 E-value: 2.46e-07
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| beta-trefoil_Ricin_GALNT3-like | cd23435 | ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ... |
136-265 | 2.85e-07 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3)-like subfamily; The GALNT3-like subfamily includes GALNT3, GALNT4, GALNT6 and GALNT12. 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. GALNT3 has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. It probably glycosylates fibronectin in vivo as well as FGF23. It plays a central role in phosphate homeostasis. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT12 has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with non-glycosylated Muc2 and Muc7. It displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. It may play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs. Members of this family 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 are 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: 467313 [Multi-domain] Cd Length: 128 Bit Score: 48.48 E-value: 2.85e-07
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| beta-trefoil_Ricin_cinnamomin_rpt2 | cd23493 | second ricin B-type lectin domain, beta-trefoil fold, found in Cinnamomum camphora type II ... |
164-263 | 6.58e-07 | ||||
second ricin B-type lectin domain, beta-trefoil fold, found in Cinnamomum camphora type II ribosome-inactivating protein (RIP) cinnamomin and similar proteins; RIPs are a group of ribotoxins that inhibit mammalian protein biosynthesis by irreversible inactivation of their 60S ribosomal subunit. Type II RIPs in plant cells comprise part of the plant's defense system towards animals. Cinnamomin is a type II RIP isolated from Cinnamomum camphora seeds. It shows inhibitory effects on cultured carcinoma cells and on the larva of the bollworm and mosquito. There are three cinnamomin isoforms (I, II, III). They are composed of two polypeptide chains (A- and B-chain) linked by a disulfide bond. The A-chain displays specific activity as an RNA N-glycosidase that blocks protein synthesis, whereas the B-chain is responsible for the binding to galactose-terminated receptors on cell membranes. The B-chain contains two ricin B-type lectin domains 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 model corresponds to the second ricin B-type lectin domain. Pssm-ID: 467371 Cd Length: 125 Bit Score: 47.36 E-value: 6.58e-07
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| beta-trefoil_Ricin_SCDase_rpt2 | cd23500 | second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ... |
193-263 | 7.78e-07 | ||||
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-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. The model corresponds to the second lectin domain. Pssm-ID: 467378 [Multi-domain] Cd Length: 128 Bit Score: 47.07 E-value: 7.78e-07
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| beta-trefoil_Ricin_SCDase_rpt2 | cd23500 | second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ... |
150-263 | 1.60e-06 | ||||
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-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. The model corresponds to the second lectin domain. Pssm-ID: 467378 [Multi-domain] Cd Length: 128 Bit Score: 46.30 E-value: 1.60e-06
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| beta-trefoil_Ricin_SaAF-like | cd23457 | ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca ... |
154-262 | 1.61e-06 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca alpha-L-arabinofuranosidase (SaAF) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called non-reducing end alpha-L-arabinofuranosidase, or arabinosidase, catalyzes the hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. It acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Members of this subfamily contain a ricin B-type lectin domain that adopts 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 bears a potential sugar binding site. Pssm-ID: 467335 [Multi-domain] Cd Length: 139 Bit Score: 46.64 E-value: 1.61e-06
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| beta-trefoil_Ricin_AglA | cd23425 | ricin B-type lectin domain, beta-trefoil fold, found in alpha-galactosidase A (AglA) and ... |
153-263 | 1.72e-06 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in alpha-galactosidase A (AglA) and similar proteins; AglA (EC 3.2.1.22), also called melibiase A, hydrolyzes a variety of simple alpha-D-galactosides as well as more complex molecules such as oligosaccharides and polysaccharides. It belongs to the glycosyl hydrolase 27 (GH27) family. AglA contains an N-terminal GH27 catalytic domain, an alpha galactosidase C-terminal beta sandwich domain in the middle region, and a carbohydrate-binding domain at the C-terminus. The carbohydrate-binding domain is also known as 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 contain a potential sugar-binding pocket. Pssm-ID: 467303 [Multi-domain] Cd Length: 116 Bit Score: 45.90 E-value: 1.72e-06
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| beta-trefoil_Ricin_ebulin-like_rpt1 | cd23483 | first ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and ... |
179-265 | 2.11e-06 | ||||
first ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and similar proteins; The family includes Sambucus ebulus ebulin I and Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf. Ebulin l is a type II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus. It is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. It is considered a nontoxic type II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type II RIP like ricins. Ebulin l binds an A-chain substrate analogue, pteroic acid. It binds bind galactose and lactose in subdomain 1alpha in a similar manner to that of ricin. In contrast, it binds only the monosaccharide galactose, and not the disaccharide lactose in subdomain 2gamma. SNAV is a non-toxic GalNAc-specific type II RIP which strongly inhibits mammalian protein synthesis but does not affect plant nor bacterial protein synthesis. SNAI is a Neu5Ac(alpha2-6)Gal/GalNAc-specific agglutinin. It also acts as a type II RIP that strongly inhibits mammalian but not plant ribosomes. SNAI' is another NeuAc(alpha2,6)Gal/GalNAc binding type II RIP from elderberry (Sambucus nigra) bark. It is a minor bark protein which closely resembles the major Neu5Ac(alpha2,6)Gal/GalNAc binding type II RIP, SNAI, with respect to its carbohydrate-binding specificity and ribosome-inactivating activity but has a different molecular structure due to a single cysteine residue present in the B chain of SNAI but absent from SNAI'. SNAIf is a fruit-specific SNAI. It functions as a fetuin-binding fruit lectin. Like Ebulin l, SNAV, SNAI, SNAI' and SNAIf consist of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain. It may also be responsible for cell agglutination (lectin activity). The B chain contains two ricin B-type lectin domains 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. This model corresponds to the first ricin B-type lectin domain. Pssm-ID: 467361 [Multi-domain] Cd Length: 127 Bit Score: 45.96 E-value: 2.11e-06
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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 ... |
226-265 | 2.19e-06 | ||||
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: 45.82 E-value: 2.19e-06
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| beta-trefoil_Ricin_EW29-like | cd23449 | ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ... |
152-264 | 2.55e-06 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa galactose-binding lectin (EW29) and similar proteins; EW29 is a galactose-binding lectin from the earthworm Lumbricus terrestris. It contains two ricin B-type lectin domains 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 second ricin B-type lectin domain may harbor two sugar-binding pockets in subdomains alpha and gamma. EW29 uses these two sugar-binding sites for its function as a single domain-type hemagglutinin. Pssm-ID: 467327 [Multi-domain] Cd Length: 128 Bit Score: 45.74 E-value: 2.55e-06
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| beta-trefoil_Ricin_1,3Gal43A | cd23446 | ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ... |
153-263 | 2.88e-06 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as 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. Each subdomain bears a potential sugar binding site. Pssm-ID: 467324 [Multi-domain] Cd Length: 137 Bit Score: 45.84 E-value: 2.88e-06
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| beta-trefoil_Ricin_GALNT11 | cd23440 | ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ... |
152-263 | 2.95e-06 | ||||
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: 45.45 E-value: 2.95e-06
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| beta-trefoil_Ricin_EW29-like | cd23449 | ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ... |
192-263 | 3.04e-06 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa galactose-binding lectin (EW29) and similar proteins; EW29 is a galactose-binding lectin from the earthworm Lumbricus terrestris. It contains two ricin B-type lectin domains 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 second ricin B-type lectin domain may harbor two sugar-binding pockets in subdomains alpha and gamma. EW29 uses these two sugar-binding sites for its function as a single domain-type hemagglutinin. Pssm-ID: 467327 [Multi-domain] Cd Length: 128 Bit Score: 45.36 E-value: 3.04e-06
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| beta-trefoil_Ricin_GllA-1 | cd23454 | GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; ... |
191-263 | 3.61e-06 | ||||
GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; Gellin proteins act as central effectors of wound-induced protoplasmic gelation. They possess ten related N-terminal beta-trefoil domains (Gll-1 to Gll-10) that contribute to distinct gelation-related activities. The beta-trefoil domains show low sequence similarity to members of the functionally diverse ricin B lectin domain family. They are 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 bears a potential sugar binding site. Gellin from M. circinelloides has been called GellinA (also known as GllA). The model corresponds to GllA-1 domain, which is a remote family member of the ricin B-type lectin domain. Pssm-ID: 467332 [Multi-domain] Cd Length: 136 Bit Score: 45.38 E-value: 3.61e-06
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| beta-trefoil_Ricin_SCDase | cd23456 | ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ... |
227-265 | 6.07e-06 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-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: 467334 [Multi-domain] Cd Length: 122 Bit Score: 44.27 E-value: 6.07e-06
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| beta-trefoil_Ricin_AH | cd23415 | ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ... |
192-265 | 6.17e-06 | ||||
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: 44.35 E-value: 6.17e-06
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| RicinB_lectin_2 | pfam14200 | Ricin-type beta-trefoil lectin domain-like; |
193-242 | 6.80e-06 | ||||
Ricin-type beta-trefoil lectin domain-like; Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 43.52 E-value: 6.80e-06
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| beta-trefoil_Ricin-like_rpt1 | cd23480 | first ricin B-type lectin domain, beta-trefoil fold, found in Ricinus communis ricin, ... |
146-242 | 1.88e-05 | ||||
first ricin B-type lectin domain, beta-trefoil fold, found in Ricinus communis ricin, agglutinin and similar proteins; This subfamily includes ricin and agglutinin (RCA), which are toxic lectins from Ricinus communis. Ricin is highly toxic to animal cells, and to a lesser extent to plant cells. As a prototype AB toxin, ricin is composed of two polypeptide chains (A- and B-chain) linked by a disulfide bond. Ricin A chain acts as an RNA N-glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. Ricin B functions as a lectin that mediates cell binding via different oligosaccharide residues on the cell surface, including N-acetylglucosamine and galactose residues found in glycolipids and glycoproteins. It is also responsible for cell agglutination. Agglutinin shows high sequence similarity with ricin. It is only a weak toxin but a strong hemagglutinin. By contrast, ricin is a potent toxin but a weak hemagglutinin. Like ricin, agglutinin consists of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The B chain of ricin and agglutinin contains two ricin B-type lectin domains 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. This model corresponds to the first ricin B-type lectin domain. Pssm-ID: 467358 [Multi-domain] Cd Length: 137 Bit Score: 43.51 E-value: 1.88e-05
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| beta-trefoil_Ricin_hemolysin | cd23423 | ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ... |
192-265 | 4.16e-05 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar proteins; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cytolysis by forming heptameric pores in target host membranes. After binding to target membranes, the protein assembles into a heptameric pre-pore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation. Hemolysin may be called "cytolysin" or "cytolytic toxin", according to a specific action for certain cells. For example, this subfamily includes Vibrio vulnificus cytolysin that attack blood cell membranes and cause cell rupture, thereby liberating hemoglobins. Members of this subfamily 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 putative sugar-binding pocket. Pssm-ID: 467301 [Multi-domain] Cd Length: 119 Bit Score: 41.98 E-value: 4.16e-05
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| RicinB_lectin_2 | pfam14200 | Ricin-type beta-trefoil lectin domain-like; |
227-264 | 6.59e-05 | ||||
Ricin-type beta-trefoil lectin domain-like; Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 40.83 E-value: 6.59e-05
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| beta-trefoil_Ricin_XLN-like | cd23418 | ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ... |
225-265 | 6.95e-05 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with 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. Each subdomain may contain a potential sugar-binding pocket. Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 41.57 E-value: 6.95e-05
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| beta-trefoil_Ricin_CRYBG | cd23430 | ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin ... |
192-263 | 9.91e-05 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin domain-containing protein (CRYBG) family; The CRYBG family includes three members: CRYBG1, CRYBG2, and CRYBG3/vlAKAP. CRYBG1, also called absent in melanoma 1 protein (AIM1), may function as a suppressor of malignant melanoma. It may exert its effects through interactions with the cytoskeleton. CRYBG2 is also called absent in melanoma 1-like protein (AIM1L). CRYBG3/vlAKAP, also called very large A-kinase anchor protein, is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). CRYBG proteins belong to the beta/gamma-crystallin family. They all contain a ricin B-type lectin domain with a beta-trefoil fold at the C-terminus. The beta-trefoil fold 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: 467308 [Multi-domain] Cd Length: 133 Bit Score: 41.42 E-value: 9.91e-05
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| beta-trefoil_Ricin_vlAKAP | cd23463 | ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein ... |
184-263 | 1.82e-04 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein (vlAKAP) and similar proteins; vlAKAP, also called beta/gamma crystallin domain-containing protein 3 (CRYBG3), is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). vlAKAP belongs to the beta/gamma-crystallin family. It contains a ricin B-type lectin domain at the C-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: 467341 Cd Length: 136 Bit Score: 40.50 E-value: 1.82e-04
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| RicinB_lectin_2 | pfam14200 | Ricin-type beta-trefoil lectin domain-like; |
152-211 | 2.48e-04 | ||||
Ricin-type beta-trefoil lectin domain-like; Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 38.90 E-value: 2.48e-04
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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) ... |
192-263 | 2.75e-04 | ||||
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: 39.89 E-value: 2.75e-04
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| beta-trefoil_Ricin_GllA-1 | cd23454 | GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; ... |
152-222 | 2.91e-04 | ||||
GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; Gellin proteins act as central effectors of wound-induced protoplasmic gelation. They possess ten related N-terminal beta-trefoil domains (Gll-1 to Gll-10) that contribute to distinct gelation-related activities. The beta-trefoil domains show low sequence similarity to members of the functionally diverse ricin B lectin domain family. They are 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 bears a potential sugar binding site. Gellin from M. circinelloides has been called GellinA (also known as GllA). The model corresponds to GllA-1 domain, which is a remote family member of the ricin B-type lectin domain. Pssm-ID: 467332 [Multi-domain] Cd Length: 136 Bit Score: 39.99 E-value: 2.91e-04
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| beta-trefoil_Ricin_RIPs_II_rpt2 | cd23444 | second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ... |
146-223 | 3.17e-04 | ||||
second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating proteins (RIPs); Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. They consist of a catalytic A-chain which has rRNA N-glycosidase activity and a lectin B-chain containing two ricin B-type lectin domains 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 lectin chain facilitates the internalization of the catalytic chain on binding to the cell surface. The two chains are connected by a disulfide bridge. This model corresponds to the second ricin B-type lectin domain. Members of this family includes Ricinus communis ricin, bitter gourd (Momordica charantia) seed lectin (BGSL), snake gourd (Trichosanthes anguina) seed lectin (SGSL), Sambucus ebulus ebulin I, Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf, Abrus precatorius abrin (ABR) and agglutinin-I (AAG), and Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs). Pssm-ID: 467322 [Multi-domain] Cd Length: 122 Bit Score: 39.56 E-value: 3.17e-04
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| beta-trefoil_Ricin_HA17-like | cd23445 | ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating ... |
151-180 | 3.29e-04 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating proteins, HA17 and HA33, and similar proteins; The subfamily includes Clostridium botulinum hemagglutinating proteins HA17 and HA33, Lysinibacillus sphaericus mosquitocidal toxin (MTX) and Pieris brassicae pierisin. The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of the neurotoxin. It may increase internalization of the neurotoxin into the bloodstream of the host. The hemagglutinin complex, composed of HA-70 (also known as HA3), HA-33 (also known as HA1) and HA-17 (also known as HA2), agglutinates erythrocytes, whereas the individual components do not. HA-33 is involved in recognition of cell-surface carbohydrates. HA-17 and HA-70 are involved in paracellular barrier disruption by E-cadherin binding. MTX acts as an ADP-ribosyl transferase. Pierisin, also called NAD--DNA ADP-ribosyltransferase, pierisin-2, or pierisin-B, catalyzes the ADP ribosylation of double-stranded DNA by targeting the N2 amino group of dG residues. It induces apoptosis in a range of human cell lines. Members of this subfamily contain at least one 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. Pssm-ID: 467323 [Multi-domain] Cd Length: 133 Bit Score: 39.61 E-value: 3.29e-04
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| beta-trefoil_Ricin_MLs_rpt1 | cd23485 | first ricin B-type lectin domain, beta-trefoil fold, found in Viscum album B chain of ... |
182-265 | 4.01e-04 | ||||
first ricin B-type lectin domain, beta-trefoil fold, found in Viscum album B chain of beta-galactoside-specific lectins and similar proteins; This subfamily includes Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs), which inhibit growth of the human tumor cell line Molt4. They contain A and B chains. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). The B chain contains two ricin B-type lectin domains 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. This model corresponds to the first ricin B-type lectin domain. Pssm-ID: 467363 Cd Length: 134 Bit Score: 39.59 E-value: 4.01e-04
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| beta-trefoil_Ricin_SCDase_rpt2 | cd23500 | second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ... |
148-221 | 4.25e-04 | ||||
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-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. The model corresponds to the second lectin domain. Pssm-ID: 467378 [Multi-domain] Cd Length: 128 Bit Score: 39.37 E-value: 4.25e-04
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| beta-trefoil_Ricin_laminarinase | cd23451 | ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ... |
152-181 | 6.23e-04 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal ricin B-type lectin domain with 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. Each subdomain bears a potential sugar binding site. Pssm-ID: 467329 [Multi-domain] Cd Length: 125 Bit Score: 38.85 E-value: 6.23e-04
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| beta-trefoil_Ricin_GALNT14 | cd23478 | ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ... |
186-263 | 8.05e-04 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14) and similar proteins; GALNT14 (EC 2.4.1.41), also called polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, protein-UDP acetylgalactosaminyltransferase 14, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, 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. 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. GALNT14 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: 467356 Cd Length: 140 Bit Score: 38.70 E-value: 8.05e-04
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| beta-trefoil_Ricin_GALNT15 | cd23442 | ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ... |
152-263 | 9.76e-04 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 15 (GALNT15) and similar proteins; GALNT15 (EC 2.4.1.41), also called polypeptide GalNAc transferase 15, GalNAc-T15, polypeptide GalNAc transferase-like protein 2, GalNAc-T-like protein 2, pp-GaNTase-like protein 2, polypeptide N-acetylgalactosaminyltransferase-like protein 2, protein-UDP acetylgalactosaminyltransferase-like protein 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2, 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. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, GALNT15 can transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. It prefers Muc1a as its substrate. GALNT15 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: 467320 [Multi-domain] Cd Length: 124 Bit Score: 38.19 E-value: 9.76e-04
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| beta-trefoil_Ricin_abrin-like_rpt1 | cd23484 | first ricin B-type lectin domain, beta-trefoil fold, found in Abrus precatorius abrin, ... |
191-265 | 1.01e-03 | ||||
first ricin B-type lectin domain, beta-trefoil fold, found in Abrus precatorius abrin, agglutinin-I and similar proteins; This subfamily includes Abrus precatorius abrin (ABR) and agglutinin-I (AAG), which share a high degree of sequence similarity and belong to the type II ribosome-inactivating protein (RIP) family. Type II RIPs inhibit protein synthesis in eukaryotic cells and can also induce apoptosis. They are two-polypeptide proteins with a toxic A chain and a lectin-like B chain linked by a disulfide bond. The A chain of abrin and agglutinin-I is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. Agglutinin-I is less toxic than abrin. The B chain is a galactose-specific lectin that facilitates the binding to the cell membrane that precedes endocytosis. The B-chain contains two ricin B-type lectin domains 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. This model corresponds to the first ricin B-type lectin domain. Pssm-ID: 467362 Cd Length: 137 Bit Score: 38.46 E-value: 1.01e-03
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| beta-trefoil_Ricin_BGSL_rpt1 | cd23481 | first ricin B-type lectin domain, beta-trefoil fold, found in bitter gourd (Momordica ... |
184-256 | 1.09e-03 | ||||
first ricin B-type lectin domain, beta-trefoil fold, found in bitter gourd (Momordica charantia) seed lectin (BGSL) and similar proteins; Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. BGSL is a non-toxic four-chain type II RIP resulting from covalent association through a disulfide bridge between two identical copies of a two-chain unit. The two-chain unit consists of a catalytic A-chain and a lectin B-chain. The catalytic A-chain cannot firmly bind adenine due to the substitution of an aromatic residue involved in ensuring the proper orientation of the base in toxic RIPs, by a glycyl residue. BGSL is a galactose-specific lectin containing two ricin B-type lectin domains in its B-chain. 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. This model corresponds to the first ricin B-type lectin domain. In BGSL, sugar does not bind at the 2gamma site. Its 1alpha site binds sugar, which is similar to that in snake gourd (Trichosanthes anguina) seed lectin (SGSL). Pssm-ID: 467359 Cd Length: 132 Bit Score: 38.21 E-value: 1.09e-03
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| beta-trefoil_Ricin_GALNT8 | cd23472 | ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ... |
163-263 | 1.42e-03 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8) and similar proteins; GALNT8 (EC 2.4.1.41), also called polypeptide GalNAc transferase 8, GalNAc-T8, pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8, may 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. GALNT8 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: 467350 Cd Length: 146 Bit Score: 38.26 E-value: 1.42e-03
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| beta-trefoil_Ricin_GALNT13 | cd23467 | ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ... |
145-263 | 1.55e-03 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 13 (GALNT13) and similar proteins; GALNT13 (EC 2.4.1.41), also called polypeptide GalNAc transferase 13, GalNAc-T13, pp-GaNTase 13, protein-UDP acetylgalactosaminyltransferase 13, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, 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 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. GALNT13 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). The 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: 467345 Cd Length: 127 Bit Score: 37.70 E-value: 1.55e-03
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| beta-trefoil_Ricin_MytiLec-like | cd23417 | ricin B-type lectin domain, beta-trefoil fold, found in Mytilus galloprovincialis lectin ... |
193-255 | 3.19e-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: 36.93 E-value: 3.19e-03
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| beta-trefoil_Ricin_AgaB34-like | cd23458 | ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ... |
227-263 | 3.80e-03 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts 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 bears a potential sugar binding site. Pssm-ID: 467336 [Multi-domain] Cd Length: 135 Bit Score: 36.53 E-value: 3.80e-03
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| beta-trefoil_Ricin_MytiLec-like | cd23417 | ricin B-type lectin domain, beta-trefoil fold, found in Mytilus galloprovincialis lectin ... |
152-237 | 4.09e-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: 4.09e-03
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| beta-trefoil_Ricin_SaAF-like | cd23457 | ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca ... |
195-264 | 4.73e-03 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca alpha-L-arabinofuranosidase (SaAF) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called non-reducing end alpha-L-arabinofuranosidase, or arabinosidase, catalyzes the hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. It acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Members of this subfamily contain a ricin B-type lectin domain that adopts 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 bears a potential sugar binding site. Pssm-ID: 467335 [Multi-domain] Cd Length: 139 Bit Score: 36.63 E-value: 4.73e-03
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| beta-trefoil_Ricin_SGSL_rpt1 | cd23482 | first ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes ... |
144-230 | 5.00e-03 | ||||
first ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes anguina) seed lectin (SGSL) and similar proteins; Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. SGSL is a non-toxic three-chain type II RIP consisting of Aalpha, Abeta and B chains with Abeta and B being disulfide-linked. The Aalpha and Abeta chains constitute the rRNA glycosidase domain and the B chain contains two ricin B-type carbohydrate-binding lectin domains. SGSL may have no glycosidase activity due to small changes in both the nucleotide binding and carbohydrate binding capabilities. It binds galactose and derivatives with a preference for the beta-anomeric forms. It also binds prophyrins. SGSL has hemagglutinating activity towards rabbit and human erythrocytes. 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. This model corresponds to the first ricin B-type lectin domain. Pssm-ID: 467360 Cd Length: 135 Bit Score: 36.26 E-value: 5.00e-03
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| beta-trefoil_Ricin_MLs_rpt2 | cd23492 | second ricin B-type lectin domain, beta-trefoil fold, found in Viscum album B chain of ... |
144-263 | 5.81e-03 | ||||
second ricin B-type lectin domain, beta-trefoil fold, found in Viscum album B chain of beta-galactoside-specific lectins and similar proteins; This subfamily includes Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs), which inhibit growth of the human tumor cell line Molt4. They contain A and B chains. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). The B chain contains two ricin B-type lectin domains 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 model corresponds to the second ricin B-type lectin domain. Pssm-ID: 467370 Cd Length: 124 Bit Score: 36.07 E-value: 5.81e-03
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| beta-trefoil_Ricin_CRYBG | cd23430 | ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin ... |
205-263 | 6.87e-03 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin domain-containing protein (CRYBG) family; The CRYBG family includes three members: CRYBG1, CRYBG2, and CRYBG3/vlAKAP. CRYBG1, also called absent in melanoma 1 protein (AIM1), may function as a suppressor of malignant melanoma. It may exert its effects through interactions with the cytoskeleton. CRYBG2 is also called absent in melanoma 1-like protein (AIM1L). CRYBG3/vlAKAP, also called very large A-kinase anchor protein, is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). CRYBG proteins belong to the beta/gamma-crystallin family. They all contain a ricin B-type lectin domain with a beta-trefoil fold at the C-terminus. The beta-trefoil fold 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: 467308 [Multi-domain] Cd Length: 133 Bit Score: 36.03 E-value: 6.87e-03
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| beta-trefoil_Ricin_GALNT16 | cd23479 | ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ... |
150-263 | 7.63e-03 | ||||
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 16 (GALNT16) and similar proteins; GALNT16 (EC 2.4.1.41), also called polypeptide GalNAc transferase 16, GalNAc-T16, polypeptide GalNAc transferase-like protein 1, GalNAc-T-like protein 1, pp-GaNTase-like protein 1, polypeptide N-acetylgalactosaminyltransferase-like protein 1, protein-UDP acetylgalactosaminyltransferase-like protein 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1, 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. GALNT16 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: 467357 Cd Length: 129 Bit Score: 35.55 E-value: 7.63e-03
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| beta-trefoil_Ricin_MLs_rpt1 | cd23485 | first ricin B-type lectin domain, beta-trefoil fold, found in Viscum album B chain of ... |
146-195 | 7.70e-03 | ||||
first ricin B-type lectin domain, beta-trefoil fold, found in Viscum album B chain of beta-galactoside-specific lectins and similar proteins; This subfamily includes Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs), which inhibit growth of the human tumor cell line Molt4. They contain A and B chains. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). The B chain contains two ricin B-type lectin domains 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. This model corresponds to the first ricin B-type lectin domain. Pssm-ID: 467363 Cd Length: 134 Bit Score: 35.73 E-value: 7.70e-03
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| beta-trefoil_Ricin_SGSL_rpt1 | cd23482 | first ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes ... |
184-265 | 8.31e-03 | ||||
first ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes anguina) seed lectin (SGSL) and similar proteins; Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. SGSL is a non-toxic three-chain type II RIP consisting of Aalpha, Abeta and B chains with Abeta and B being disulfide-linked. The Aalpha and Abeta chains constitute the rRNA glycosidase domain and the B chain contains two ricin B-type carbohydrate-binding lectin domains. SGSL may have no glycosidase activity due to small changes in both the nucleotide binding and carbohydrate binding capabilities. It binds galactose and derivatives with a preference for the beta-anomeric forms. It also binds prophyrins. SGSL has hemagglutinating activity towards rabbit and human erythrocytes. 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. This model corresponds to the first ricin B-type lectin domain. Pssm-ID: 467360 Cd Length: 135 Bit Score: 35.88 E-value: 8.31e-03
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