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 71996085 482 KKYLIKMANGTHCLSAENSQgrIANGNRVEMRKCNHMERMQQWKYSSTNELRPMGssRMCLDSLR----GISVILCHNQG 557
Cdd:cd23440   4 RKGQLKHAGSGLCLVAEDEV--SQKGSLLVLRPCSRNDKKQLWYYTEDGELRLAN--LLCLDSSEtssdFPRLMKCHGSG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 71996085 558 AHQMWQVSNAGKLYSRSVNKCATGSNDV-SALSTLKFCSLANSFQFV 603
Cdd:cd23440  80 GSQQWRFKKDNRLYNPASGQCLAASKNGtSGYVTMDICSDSPSQKWV 126

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 71996085 482 KKYLIKMANGTHCLSAENSQgrIANGNRVEMRKCNHMERMQQWKYSSTNELRPMGssRMCLDSLR----GISVILCHNQG 557
Cdd:cd23440   4 RKGQLKHAGSGLCLVAEDEV--SQKGSLLVLRPCSRNDKKQLWYYTEDGELRLAN--LLCLDSSEtssdFPRLMKCHGSG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 71996085 558 AHQMWQVSNAGKLYSRSVNKCATGSNDV-SALSTLKFCSLANSFQFV 603
Cdd:cd23440  80 GSQQWRFKKDNRLYNPASGQCLAASKNGtSGYVTMDICSDSPSQKWV 126

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 155 SDSLPAASIVVCYFNEsPSVLIRMVNSIFDRTKPEHLHEILLVDDSSewsnaTDEAIKYREKHIIQWEKVKFLKTDKNEG 234
Cdd:COG1215  25 PADLPRVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLEVIVVDDGS-----TDETAEIARELAAEYPRVRVIERPENGG 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 235 LIRAKIFGARRANGEVLVFLDSHCEVNEEWLpplldqikqnrRRVVcpiidiidaitmkyvespvctggvnwamtfkwdy 314
Cdd:COG1215  99 KAAALNAGLKAARGDIVVFLDADTVLDPDWL-----------RRLV---------------------------------- 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 315 phrSYFEDPmNYVnplksptMAGGLFAIDKEYFFEIGSYDEGMdvwGAENVEISVRIWTCGGELLIMPCSRVGHI----- 389
Cdd:COG1215 134 ---AAFADP-GVG-------ASGANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYEEapetl 199

                ....*..
gi 71996085 390 --FRRQR 394
Cdd:COG1215 200 raLFRQR 206

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085    490 NGTHCLSAENsqgriaNGNRVEMRKCNHMERMQQWKYSSTNELRPMGSSRmCLD--SLRGISVIL--CHNQGAHQMWQVS 565
Cdd:smart00458   5 NTGKCLDVNG------NKNPVGLFDCHGTGGNQLWKLTSDGAIRIKDTDL-CLTanGNTGSTVTLysCDGTNDNQYWEVN 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 71996085    566 NAGKLYSRSVNKCATGSNDVSALS-TLKFCSLANSFQF 602
Cdd:smart00458  78 KDGTIRNPDSGKCLDVKDGNTGTKvILWTCSGNPNQKW 115

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 71996085 482 KKYLIKMANGTHCLSAENSQgrIANGNRVEMRKCNHMERMQQWKYSSTNELRPMGssRMCLDSLR----GISVILCHNQG 557
Cdd:cd23440   4 RKGQLKHAGSGLCLVAEDEV--SQKGSLLVLRPCSRNDKKQLWYYTEDGELRLAN--LLCLDSSEtssdFPRLMKCHGSG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 71996085 558 AHQMWQVSNAGKLYSRSVNKCATGSNDV-SALSTLKFCSLANSFQFV 603
Cdd:cd23440  80 GSQQWRFKKDNRLYNPASGQCLAASKNGtSGYVTMDICSDSPSQKWV 126

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 155 SDSLPAASIVVCYFNEsPSVLIRMVNSIFDRTKPEHLHEILLVDDSSewsnaTDEAIKYREKHIIQWEKVKFLKTDKNEG 234
Cdd:COG1215  25 PADLPRVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLEVIVVDDGS-----TDETAEIARELAAEYPRVRVIERPENGG 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 235 LIRAKIFGARRANGEVLVFLDSHCEVNEEWLpplldqikqnrRRVVcpiidiidaitmkyvespvctggvnwamtfkwdy 314
Cdd:COG1215  99 KAAALNAGLKAARGDIVVFLDADTVLDPDWL-----------RRLV---------------------------------- 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 315 phrSYFEDPmNYVnplksptMAGGLFAIDKEYFFEIGSYDEGMdvwGAENVEISVRIWTCGGELLIMPCSRVGHI----- 389
Cdd:COG1215 134 ---AAFADP-GVG-------ASGANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYEEapetl 199

                ....*..
gi 71996085 390 --FRRQR 394
Cdd:COG1215 200 raLFRQR 206

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085   486 IKMANGTHCLSAensQGRIANGNRVEMRKCNHMERMQQWKYSSTNELRPMGSSrMCLD---SLRGISVIL--CHNQGAHQ 560
Cdd:pfam00652   5 IRNRASGKCLDV---PGGSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVASD-LCLDvgsTADGAKVVLwpCHPGNGNQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 71996085   561 MWQVSNAGK-LYSRSVNKCAT---GSNDVSALSTLKFCSLANSFQF 602
Cdd:pfam00652  81 RWRYDEDGTqIRNPQSGKCLDvsgAGTSNGKVILWTCDSGNPNQQW 126

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 162 SIVVCYFNEsPSVLIRMVNSIFDRTKPEHlhEILLVDDSSewsnaTDEAIKYREKHIIQWEKVKFLKTDKNEGLIRAKIF 241
Cdd:COG0463   5 SVVIPTYNE-EEYLEEALESLLAQTYPDF--EIIVVDDGS-----TDGTAEILRELAAKDPRIRVIRLERNRGKGAARNA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 242 GARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVCpiidiidaitmkyvespvctGGVNWAMTFKWDYPHRSYFE 321
Cdd:COG0463  77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY--------------------GSRLIREGESDLRRLGSRLF 136

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 71996085 322 DPMNYVNPLksPTMAGGLFAIDKEYFFEIGsYDEGM 357
Cdd:COG0463 137 NLVRLLTNL--PDSTSGFRLFRREVLEELG-FDEGF 169

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 163 IVVCYFNeSPSVLIRMVNSIFDRTKPehLHEILLVDDSSewsnaTDEAIKYREKHiiqWEKVKFLKTDKNEGLIRAKIFG 242
Cdd:cd04186   1 IIIVNYN-SLEYLKACLDSLLAQTYP--DFEVIVVDNAS-----TDGSVELLREL---FPEVRLIRNGENLGFGAGNNQG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 243 ARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRrvvcpiidiidaitmkyvespvcTGGVnwamtfkwdyphrsyfed 322
Cdd:cd04186  70 IREAKGDYVLLLNPDTVVEPGALLELLDAAEQDPD-----------------------VGIV------------------ 108

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71996085 323 pmnyvnplkSPTMAGGLFAIDKEYFFEIGSYDEGMDVWGaENVEISVRIWTCGGELLIMPCSRVGH 388
Cdd:cd04186 109 ---------GPKVSGAFLLVRREVFEEVGGFDEDFFLYY-EDVDLCLRARLAGYRVLYVPQAVIYH 164

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 163 IVVCYfNESPSvLIRMVNSIFDRTKPEHLHEILLVDDSSewSNATDEAIKyreKHIIQWEKVKFLKTDKNEGLIRAKIFG 242
Cdd:cd04179   2 VIPAY-NEEEN-IPELVERLLAVLEEGYDYEIIVVDDGS--TDGTAEIAR---ELAARVPRVRVIRLSRNFGKGAAVRAG 74

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 71996085 243 ARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVC 281
Cdd:cd04179  75 FKAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVI 113

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 494 CLsaeNSQGRIANGNRVEMRKCNHMERMQQWKYSSTNELRpmgSSRMCLDSLRGISVIL--CHNQGAHQMWQVSNAGK-L 570
Cdd:cd23460  13 CL---DWAGESNGDKTVALKPCHGGGGNQFWMYTGDGQIR---QDHLCLTADEGNKVTLreCADQLPSQEWSYDEKTGtI 86

                        90       100       110
                ....*....|....*....|....*....|..
gi 71996085 571 YSRSVNKCATGSNDVSALsTLKFCSLANSFQF 602
Cdd:cd23460  87 RHRSTGLCLTLDANNDVV-ILKECDSNSLWQK 117

N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71996085   316 HRSYFEDPMNYvnPLKSPTMAGGLFAIDKEYFFEIGSYDEGMDVWGAENVEISVRIWTCGGELLImPCSRVGHIF 390
Cdd:pfam02709   2 HLSVALDKFGY--KLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIER-PPGDIGRYY 73

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 494 CLSAENsqGRIANGNRVEMRKCnHMERMQQWKYSSTNELRPMGssRMCLD-----SLRGISVIL--ChNQGAHQMWQVSN 566
Cdd:cd23418  16 CLDVPG--GSTTNGTRLILWDC-HGGANQQFTFTSAGELRVGG--DKCLDaagggTTNGTPVVIwpC-NGGANQKWRFNS 89

                        90
                ....*....|...
gi 71996085 567 AGKLYSRSVNKCA 579
Cdd:cd23418  90 DGTIRNVNSGLCL 102

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 163 IVVCYFNESpSVLIRMVNSIFD--RTKPEHLHEILLVDDSSewSNATDE-AIKYREKHIiqwEKVKFLKTDKNEGLIRAK 239
Cdd:cd04188   1 VVIPAYNEE-KRLPPTLEEAVEylEERPSFSYEIIVVDDGS--KDGTAEvARKLARKNP---ALIRVLTLPKNRGKGGAV 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 71996085 240 IFGARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVC 281
Cdd:cd04188  75 RAGMLAARGDYILFADADLATPFEELEKLEEALKTSGYDIAI 116

second 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 composed of 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. The model corresponds to the second ricin B-type lectin domain.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71996085 505 ANGNRVEMRKCNHMERMQQWKYSSTNELRPMGSSRMCL---DSLRGISVIL--CHNQGAHQMWQVSNAGKLYS 572
Cdd:cd23491  16 AQGSNVWLAVCDINKKEQQWALYTDGSIRSVQNTNNCLtskDHKQGSTIVLmgCSNGWASQRWVFKNDGSIYN 88

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085   162 SIVVCYFN--ESPSVLIRMVNSifdRTKPEHLHEILLVDDSSewSNATDEAIKyrekHIIQWEKVKFLK--TDKNEGLIR 237
Cdd:pfam10111   1 SVVIPVYNgeKTHWIQERILNQ---TFQYDPEFELIIINDGS--TDKTLEEVS----SIKDHNLQVYYPnaPDTTYSLAA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085   238 AKIFGARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRR------VVCPIIDIIDAIT--MKYVESPVCTGGVnwamt 309
Cdd:pfam10111  72 SRNRGTSHAIGEYISFIDGDCLWSPDKFEKQLKIATSLALQeniqaaVVLPVTDLNDESSnfLRRGGDLTASGDV----- 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71996085   310 fkwdyphrsyFEDPMNYVNPL-KSPTMAGGLFAIDKEYFFEIGSYDEGMDVWGAENVEISVRI 371
Cdd:pfam10111 147 ----------LRDLLVFYSPLaIFFAPNSSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRL 199

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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71996085 493 HCLSAENSqgriangNRVEMRKCNHMERMQQWKYSSTNELRPMGSSRMCLDS 544
Cdd:cd23423  15 RCLTVDNN-------GRVTLESCDSGDRNQSWILDSEGRYRSRVAPDLCLDA 59

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 474 NNQILVAGKKYLIKManGTHCLSAENSQgriangNRVEMRKCNHMERmQQWKYSSTNELRPMGSSRMCLDSLRGIS-VIL 552
Cdd:cd23437  38 GNQLFRLNEAGQLAV--GEQCLTASGSG------GKVKLRKCNLGET-GKWEYDEATGQIRHKGTGKCLDLNEGTNkLIL 108

                        90
                ....*....|....*.
gi 71996085 553 --CHNQGAHQMWQVSN 566
Cdd:cd23437 109 qpCDSSSPSQKWEFNE 124

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 475 NQILVAGKKYLIKmaNGTHCLSAENSQGRiangnrVEMRKCNHMERMQQWKY-SSTNELRPMgSSRMCLD--SLRGISVI 551
Cdd:cd23433  40 NQVFSYTAKGEIR--SDDLCLDASRKGGP------VKLEKCHGMGGNQEWEYdKETKQIRHV-NSGLCLTapNEDDPNEP 110

                        90
                ....*....|....*...
gi 71996085 552 L---ChNQGAHQMWQVSN 566
Cdd:cd23433 111 VlrpC-DGGPSQKWELEG 127

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71996085 537 SSRMCLDSL------RGISVILCHNQGAHQMWQVSNAGKLysRSVNKCATGSNDVSAlsTLKFCSLANSFQF 602
Cdd:cd23460   9 ESGLCLDWAgesngdKTVALKPCHGGGGNQFWMYTGDGQI--RQDHLCLTADEGNKV--TLRECADQLPSQE 76

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71996085 493 HCLSAENSQGRiangnRVEMRKCNHMERM-QQWKYSSTNELRPMgSSRMCLD-----SLRGISVILChNQGAHQMWQ 563
Cdd:cd23459  60 SCADVQGTEES-----KVILITCHGLEKFnQKWKHTKGGQIVHL-ASGKCLDaeglkSGDDVTLAKC-DGSLSQKWT 129

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 71996085 494 CLSAENSqgriANGNRVEMRKCNHMERMQQWKYSSTNELRPMGSSRMCLDSLRGISVILCHNQGAHQMWQ 563
Cdd:cd23385  53 CLGVSSS----SPSSPLRLFECDSEDELQKWKCSKDGLLLLKGLGLLLLYDKSGKNVVVSKGSGLSSRWK 118

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71996085 494 CLSAENsqgrIANGNRVEMRKCNHMERMQQWKysstnelrPMGSSRM------CLDSLRGISVI-LCHNQGAHQMWQV 564
Cdd:cd23479  61 CLAITS----FSPGSKVILELCNQKDGRQKWK--------LKGSFIQhqvsglCLDSQSGRVVInQCQADLASQQWEL 126

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996085 522 QQWKYSSTNELRpmgSSRMCL---DSLRGISVIL--CHNQGAHQMWQV-SNAGKLYSRSVNKCATGSNDVSALSTLKFCS 595
Cdd:cd23434  35 QEWSFTKDGQIK---HDDLCLtvvDRAPGSLVTLqpCREDDSNQKWEQiENNSKLRHVGSNLCLDSRNAKSGGLTVETCD 111

                ....*.
gi 71996085 596 LANSFQ 601
Cdd:cd23434 112 PSSGSQ 117