Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258566 405 IFHPLSGLCVVV----KSSEALELGPCDESNA---WNYTSTHELVLQHTGQCLQVKSVGENAQLG-TDCSKSSS--KWQL 474
Cdd:pfam00652   5 IRNRASGKCLDVpggsSAGGPVGLYPCHGSNGnqlWTLTGDGTIRSVASDLCLDVGSTADGAKVVlWPCHPGNGnqRWRY 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002258566 475 ISNsgmhvSTELTKNGTRVCLDATPDGIITTNPC--KCLTGDPN 516
Cdd:pfam00652  85 DED-----GTQIRNPQSGKCLDVSGAGTSNGKVIlwTCDSGNPN 123

Cellulase (glycosyl hydrolase family 5);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258566  70 DIAARVAAMGFNCVRL--TWPTYLATNATlaslplrwslerfgmresvagvrvnnpGLLDLPLIDVFQEVVSALARNNIM 147
Cdd:pfam00150  28 AMIDLVKDWGFNVVRLpvSWGGYVPNNPD---------------------------YLIDENWLNRVDEVVDYAIDNGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258566 148 VILDNQmTTPGWccsttdGNGFFGDKYfDPEEWLNGLKT-MATMFrKTKNVVGMSLRNELRG--PYENVSLWYRYMKEGA 224
Cdd:pfam00150  81 VIIDWH-HDGGW------PGDPNGNID-TAKAFFKKIWTqIATRY-GNNPNVIFELMNEPHGndQATWADDVKDYAQEAI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258566 225 ESVHTANPDVLVILSGLEFDNTLNFVV---PNQihlsfTGKLVFEQHWYGFSDG-GNWESQNQNDVCGMVVGFIKNKglf 300
Cdd:pfam00150 152 DAIRAAGPNNLIIVGGNSWSQNPDGAAlndPND-----DDNLIYSVHFYAPSDFsGTWFDCEDPTNLAQRLRAAANW--- 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1002258566 301 LLQQGWPLFFSEFG-FDMSGTHTGDNRYltcFLSVAAEMDLDWAIWAL 347
Cdd:pfam00150 224 ALDNGIPVFIGEFGgGNADGPCRDEAEK---WLDYLKENGISWTGWSN 268

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002258566 405 IFHPLSGLCVVV-KSSEALELGPCDESNA---WNYTSTHELVLQHTGQCLQVKSVGENAQLGT-DCSKSSSKWQ 473
Cdd:cd23385     5 IYNEDLGKCLAArSSSSKVSLSTCNPNSPnqqWKWTSGHRLFNVGTGKCLGVSSSSPSSPLRLfECDSEDELQK 78

Cellulase (glycosyl hydrolase family 5);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258566  70 DIAARVAAMGFNCVRL--TWPTYLATNATlaslplrwslerfgmresvagvrvnnpGLLDLPLIDVFQEVVSALARNNIM 147
Cdd:pfam00150  28 AMIDLVKDWGFNVVRLpvSWGGYVPNNPD---------------------------YLIDENWLNRVDEVVDYAIDNGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258566 148 VILDNQmTTPGWccsttdGNGFFGDKYfDPEEWLNGLKT-MATMFrKTKNVVGMSLRNELRG--PYENVSLWYRYMKEGA 224
Cdd:pfam00150  81 VIIDWH-HDGGW------PGDPNGNID-TAKAFFKKIWTqIATRY-GNNPNVIFELMNEPHGndQATWADDVKDYAQEAI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258566 225 ESVHTANPDVLVILSGLEFDNTLNFVV---PNQihlsfTGKLVFEQHWYGFSDG-GNWESQNQNDVCGMVVGFIKNKglf 300
Cdd:pfam00150 152 DAIRAAGPNNLIIVGGNSWSQNPDGAAlndPND-----DDNLIYSVHFYAPSDFsGTWFDCEDPTNLAQRLRAAANW--- 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1002258566 301 LLQQGWPLFFSEFG-FDMSGTHTGDNRYltcFLSVAAEMDLDWAIWAL 347
Cdd:pfam00150 224 ALDNGIPVFIGEFGgGNADGPCRDEAEK---WLDYLKENGISWTGWSN 268

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002258566 405 IFHPLSGLCVVV-KSSEALELGPCDESNA---WNYTSTHELVLQHTGQCLQVKSVGENAQLGT-DCSKSSSKWQ 473
Cdd:cd23385     5 IYNEDLGKCLAArSSSSKVSLSTCNPNSPnqqWKWTSGHRLFNVGTGKCLGVSSSSPSSPLRLfECDSEDELQK 78

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258566 405 IFHPLSGLCVVVKSS-----EALELGPCDESNA---WNYTSTHELVL------------------------------QH- 445
Cdd:cd23440     8 LKHAGSGLCLVAEDEvsqkgSLLVLRPCSRNDKkqlWYYTEDGELRLanllcldssetssdfprlmkchgsggsqqwRFk 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002258566 446 ---------TGQCLQVKSVGENAQLGTD-CSKSSS-KWQL 474
Cdd:cd23440    88 kdnrlynpaSGQCLAASKNGTSGYVTMDiCSDSPSqKWVF 127

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258566  405 IFHPLSGLCVVVKSSEA-LELGPCDESNA---WNYTSTHELVLQHTGQCLQV-KSVGENAQLgTDCS--KSSSKWQLISN 477
Cdd:smart00458   1 IISGNTGKCLDVNGNKNpVGLFDCHGTGGnqlWKLTSDGAIRIKDTDLCLTAnGNTGSTVTL-YSCDgtNDNQYWEVNKD 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1002258566  478 SGM-HVSTELtkngtrvCLDA---TPDGIITTNPCkcltgdpNCNPESQW 523
Cdd:smart00458  80 GTIrNPDSGK-------CLDVkdgNTGTKVILWTC-------SGNPNQKW 115

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258566 405 IFHPLSGLCVVVKSSE-----ALELGPCDESNA--WNYTS----THELVLQHTGQCLQVK--SVGENAQLGT-DCSKSSS 470
Cdd:cd00161     5 IVNAASGKCLDVAGGStangaPVQQWTCNGGANqqWTLTPvgdgYYTIRNVASGKCLDVAggSTANGANVQQwTCNGGDN 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1002258566 471 -KWQLISNSG-------------MHVSTELTKNGTRVCL 495
Cdd:cd00161    85 qQWRLEPVGDgyyrivnkhsgkcLDVSGGSTANGANVQQ 123

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258566 401 PYNVIFHPLSGLCVVVKSS-------EALELGPCDESNAWNYTSTHELVLQHT--GQCLQVK--SVGENAQLG--TDCSK 467
Cdd:cd23417     1 PPGSIRHKASGKCIHPKGGscnppdgTKLVLYSDCSEDRMEFQLDSDGYLKHVcsGKCVCPKggSADNGTKLVlhSNCGD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002258566 468 SSSKWQLISN-SGMHVSTEL----------TKNGTRVCLD 496
Cdd:cd23417    81 DRAKFRRTSKgSLQHKSSGKcvhpkggspnPSNGTKLVLW 120