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 1701944640 477 KVLQRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSLLCLDMSETRsSDPPRLMKCHGSG 556
Cdd:cd23440     1 KVIRKGQLKHAGSGLCLVAEDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLLCLDSSETS-SDFPRLMKCHGSG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1701944640 557 GSQQWTFGKNNRLYQVSVGQCLRAVDPlGQKGSVAMAICDGSSSQQWHL 605
Cdd:cd23440    80 GSQQWRFKKDNRLYNPASGQCLAASKN-GTSGYVTMDICSDSPSQKWVF 127

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 1701944640 477 KVLQRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSLLCLDMSETRsSDPPRLMKCHGSG 556
Cdd:cd23440     1 KVIRKGQLKHAGSGLCLVAEDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLLCLDSSETS-SDFPRLMKCHGSG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1701944640 557 GSQQWTFGKNNRLYQVSVGQCLRAVDPlGQKGSVAMAICDGSSSQQWHL 605
Cdd:cd23440    80 GSQQWRFKKDNRLYNPASGQCLAASKN-GTSGYVTMDICSDSPSQKWVF 127

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 482 GRLYHLQTNKCLVAQGRpSQKGGLVVLKACDYSDPNQIWIYNEEHEL-VLNSLLCLDMSETRSSDPPRLMKCHGSGGSQQ 560
Cdd:pfam00652   3 GRIRNRASGKCLDVPGG-SSAGGPVGLYPCHGSNGNQLWTLTGDGTIrSVASDLCLDVGSTADGAKVVLWPCHPGNGNQR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1701944640 561 WTFGKNNR-LYQVSVGQCLRAVDPLGQKGSVAMAICD-GSSSQQW 603
Cdd:pfam00652  82 WRYDEDGTqIRNPQSGKCLDVSGAGTSNGKVILWTCDsGNPNQQW 126

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 154 SVVICFYNEAfSALLRTVHSVIDRTPAHLlhEIILVdddsdfddlkgelD--------EYVQKYLPG--KIKVIRNTKRE 223
Cdd:COG0463     5 SVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVV-------------DdgstdgtaEILRELAAKdpRIRVIRLERNR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 224 GLIRGRMIGAAHAT-EVLVFLDSHCEVNVMWLQPLLAAIREDRHtvvcpviDIISADTLAYSSSPVVRGGFNWGLHFKWD 302
Cdd:COG0463    69 GKGAARNAGLAAARgDYIAFLDADDQLDPEKLEELVAALEEGPA-------DLVYGSRLIREGESDLRRLGSRLFNLVRL 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1701944640 303 LVPLselgraegatapiksPTMAGGLFAMNRQYFHELGqYDSGMdiwgGENLEIsFRIWMCGGKLFIIP 371
Cdd:COG0463   142 LTNL---------------PDSTSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVP 189

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 1701944640 477 KVLQRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSLLCLDMSETRsSDPPRLMKCHGSG 556
Cdd:cd23440     1 KVIRKGQLKHAGSGLCLVAEDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLLCLDSSETS-SDFPRLMKCHGSG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1701944640 557 GSQQWTFGKNNRLYQVSVGQCLRAVDPlGQKGSVAMAICDGSSSQQWHL 605
Cdd:cd23440    80 GSQQWRFKKDNRLYNPASGQCLAASKN-GTSGYVTMDICSDSPSQKWVF 127

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 482 GRLYHLQTNKCLVAQGRpSQKGGLVVLKACDYSDPNQIWIYNEEHEL-VLNSLLCLDMSETRSSDPPRLMKCHGSGGSQQ 560
Cdd:pfam00652   3 GRIRNRASGKCLDVPGG-SSAGGPVGLYPCHGSNGNQLWTLTGDGTIrSVASDLCLDVGSTADGAKVVLWPCHPGNGNQR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1701944640 561 WTFGKNNR-LYQVSVGQCLRAVDPLGQKGSVAMAICD-GSSSQQW 603
Cdd:pfam00652  82 WRYDEDGTqIRNPQSGKCLDVSGAGTSNGKVILWTCDsGNPNQQW 126

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 477 KVLQRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSlLCLDMSETrsSDPPRLMKCHGSG 556
Cdd:cd23462     1 EALAYGEIRNLAGKLCLDAPGRKKELNKPVGLYPCHGQGGNQYWMLTKDGEIRRDD-LCLDYAGG--SGDVTLYPCHGMK 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1701944640 557 GSQQWTFGK-NNRLYQVSVGQCLRAVDPlgqKGSVAMAICDGSSS-QQWHLE 606
Cdd:cd23462    78 GNQFWIYDEeTKQIVHGTSKKCLELSDD---SSKLVMEPCNGSSPrQQWEFE 126

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 1701944640 482 GRLYHLQTNKCLVAQGRPSQkGGLVVLKACDYSDPNQIWIYNEEHELVlNSLLCLDmseTRSSDPPRLMKCHGSGGSQQW 561
Cdd:cd23460     3 GQIKHTESGLCLDWAGESNG-DKTVALKPCHGGGGNQFWMYTGDGQIR-QDHLCLT---ADEGNKVTLRECADQLPSQEW 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1701944640 562 TF-GKNNRLYQVSVGQCLRAVDplgQKGSVAMAICDGSS-SQQW 603
Cdd:cd23460    78 SYdEKTGTIRHRSTGLCLTLDA---NNDVVILKECDSNSlWQKW 118

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 151 PAASVVICFYNEAfSALLRTVHSVIDRTPAHllHEIILVDDDSdfddlKGELDEYVQKYLPGKIKVIRNTKREGLIRGRM 230
Cdd:COG1216     3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPP--FEVIVVDNGS-----TDGTAELLAALAFPRVRVIRNPENLGFAAARN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 231 IGAAHAT-EVLVFLDSHCEVNVMWLQPLLAAiredrhtvvcpvidiisadtlayssspvvrggfnwglhfkwdlvplsel 309
Cdd:COG1216    75 LGLRAAGgDYLLFLDDDTVVEPDWLERLLAA------------------------------------------------- 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 310 graegatapiksptmagGLFAMNRQYFHELGQYDSGMDIWGGEnLEISFRIWMCGGKLFIIPCSRVGHIFRKRRpyGSPE 389
Cdd:COG1216   106 -----------------ACLLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASS--GPLL 165

                         250       260
                  ....*....|....*....|....*...
gi 1701944640 390 GQDTMTHNSLRLAHVWLDEYKEQYFSLR 417
Cdd:COG1216   166 RAYYLGRNRLLFLRKHGPRPLLRLALLR 193

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 1701944640 480 QRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDpNQIWIY----NEEHELV-LNSLLCLDMSETRSSD--PPRLMKC 552
Cdd:cd00161     1 GTYRIVNAASGKCLDVAGGSTANGAPVQQWTCNGGA-NQQWTLtpvgDGYYTIRnVASGKCLDVAGGSTANgaNVQQWTC 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1701944640 553 HGsGGSQQWTF----GKNNRLYQVSVGQCLRAVDPLGQKGS-VAMAICDGSSSQQW 603
Cdd:cd00161    80 NG-GDNQQWRLepvgDGYYRIVNKHSGKCLDVSGGSTANGAnVQQWTCNGGANQQW 134

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 1701944640 488 QTNKCLVAQGRpsQKGGLVVLKACDYSDPNQIWIYNEEHeLVLNSLLCLDMSETRSSDPPRLMKCHGSGGSQQWTFGKNN 567
Cdd:cd23434     7 QGNLCLDTLGH--KAGGTVGLYPCHGTGGNQEWSFTKDG-QIKHDDLCLTVVDRAPGSLVTLQPCREDDSNQKWEQIENN 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1701944640 568 -RLYQVSVGQCLRAVDplGQKGSVAMAICDGSS-SQQW 603
Cdd:cd23434    84 sKLRHVGSNLCLDSRN--AKSGGLTVETCDPSSgSQQW 119

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 482 GRLYHLQTNKCLVAQGRP-SQKGGLVvlkACDYSDPNQIWIYNEEHELVLNSLlCLDMSetRSSDPPRLMKCHGSGGSQQ 560
Cdd:cd23467     7 GEIRNVETNQCLDNMGRKeNEKVGIF---NCHGMGGNQVFSYTADKEIRTDDL-CLDVS--RLNGPVVMLKCHHMRGNQL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1701944640 561 WTFGKNN-RLYQVSVGQCLRavDPLGQKGSV-AMAICDGSSSQQWHL 605
Cdd:cd23467    81 WEYDAERlTLRHVNSNQCLD--EPSEEDKMVpTMKDCSGSRSQQWLL 125

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 482 GRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSL--LCLdmsETRSSDPPRLMKCHGSG--- 556
Cdd:cd23435     5 GALRNKGSELCLDVNNPNGQGGKPVIMYGCHGLGGNQYFEYTSKGEIRHNIGkeLCL---HASGSDEVILQHCTSKGkdv 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1701944640 557 -GSQQWTFGKNNRLYQVSVGQCLRAVDPlgqkgSVAMAICDGSS-SQQW 603
Cdd:cd23435    82 pPEQKWLFTQDGTIRNPASGLCLHASGY-----KVLLRTCNPSDdSQKW 125

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 1701944640 147 PPDLPAASVVICFYNEAfSALLRTVHSVIDRTPAHLLHEIILVDDDSdfddlKGELDEYVQKY--LPGKIKVIRNTKREG 224
Cdd:COG1215    25 PADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGS-----TDETAEIARELaaEYPRVRVIERPENGG 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1701944640 225 LIRGRMIGAAHAT-EVLVFLDSHCEVNVMWLQPLLAAIREDR 265
Cdd:COG1215    99 KAAALNAGLKAARgDIVVFLDADTVLDPDWLRRLVAAFADPG 140

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1) and similar proteins; GALNT1 (EC 2.4.1.41), also called polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 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. It has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT1 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 is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 482 GRLYHLQTNKCLVAQGRP-SQKGGLVvlkACDYSDPNQIWIYNEEHELVLNSLlCLDMSetRSSDPPRLMKCHGSGGSQQ 560
Cdd:cd23466     7 GEIRNVETNQCLDNMARKeNEKVGIF---NCHGMGGNQVFSYTANKEIRTDDL-CLDVS--KLNGPVMMLKCHHLKGNQL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1701944640 561 WTFGKNN-RLYQVSVGQCL-RAVDPLGQKGSvaMAICDGSSSQQWHL 605
Cdd:cd23466    81 WEYDPVKlTLLHVNSNQCLdKATEEDSQVPS--IRDCNGSRSQQWLL 125

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 521 IYNEEHELvlnsllCLDMSEtrSSDPPRLMKCHGSGGSQQWTFGKNNRLYQVSVGQCLrAVDPLGQKGSVAMAICDGSS- 599
Cdd:cd23385     5 IYNEDLGK------CLAARS--SSSKVSLSTCNPNSPNQQWKWTSGHRLFNVGTGKCL-GVSSSSPSSPLRLFECDSEDe 75

                  ....*
gi 1701944640 600 SQQWH 604
Cdd:cd23385    76 LQKWK 80

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 489 TNKCLVAQGRPSQKGGLVVLKAC-DYSDPNQIWIYNEEHELvLNSLLCLDMSETRSSdPPRLMKCHGS-GGSQQWTFGKN 566
Cdd:cd23459    15 TNLCLDTLQRDEDKGYNLGLYPCqGGLSSNQLFSLSKKGEL-RREESCADVQGTEES-KVILITCHGLeKFNQKWKHTKG 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1701944640 567 NRLYQVSVGQCLRAVdPLGQKGSVAMAICDGSSSQQWHLE 606
Cdd:cd23459    93 GQIVHLASGKCLDAE-GLKSGDDVTLAKCDGSLSQKWTFE 131

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 489 TNKCL-VAQGRPSQkGGLVVLKACDYSDpNQIWIYNEEHEL-VLNslLCLDMSETRSSD--PPRLMKCHGSGGsQQWTFG 564
Cdd:cd23451    10 AGKCLdVPGSSTAD-GNPVQIYTCNGTA-AQKWTLGTDGTLrVLG--KCLDVSGGGTANgtLVQLWDCNGTGA-QKWVPR 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1701944640 565 KNNRLYQVSVGQCLRAVDPLGQKGS-VAMAICDGSSSQQW 603
Cdd:cd23451    85 ADGTLYNPQSGKCLDAPGGSTTDGTqLQLYTCNGTAAQQW 124

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 1701944640 480 QRGRLYHLQTnkCLVAqgrPSQKGG-LVVLKACDYSDPNQIWIYNEEHELV--LNSLLCLDMSETRSSDPpRLMKCHGSG 556
Cdd:cd23434    41 KDGQIKHDDL--CLTV---VDRAPGsLVTLQPCREDDSNQKWEQIENNSKLrhVGSNLCLDSRNAKSGGL-TVETCDPSS 114

                  ....*..
gi 1701944640 557 GSQQWTF 563
Cdd:cd23434   115 GSQQWKF 121

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases 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. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 155 VVICFYNEAfSALLRTVHSVIDRTPAHLlhEIILVDDdsdfddlkGELD---EYVQKYL--PGKIKVIRNTKREGLIRGR 229
Cdd:cd00761     1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDD--------GSTDgtlEILEEYAkkDPRVIRVINEENQGLAAAR 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1701944640 230 MIGAAHAT-EVLVFLDSHCEVNVMWLQPLLAAIREDrhtvvcPVIDIISAD-TLAYSSSPVVRGGFNWGLHFKWD 302
Cdd:cd00761    70 NAGLKAARgEYILFLDADDLLLPDWLERLVAELLAD------PEADAVGGPgNLLFRRELLEEIGGFDEALLSGE 138

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase-like 6 (GALNTL6) and similar proteins; GALNTL6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 17, GalNAc-T17, pp-GaNTase 17, protein-UDP acetylgalactosaminyltransferase 17, putative polypeptide N-acetylgalactosaminyltransferase 17, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17, 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. GALNTL6 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1701944640 544 SDPPRLMKCHGSGGSQQWTFGKNNRLYQVSVGQCLravDPLGQKGSVAMAICDGSS-SQQWHLE 606
Cdd:cd23477    77 NSPVTLYDCHGMKGNQLWSYRKDKTLFHPVSNSCM---DCNPADKKIFMNRCDPLSeTQQWIFE 137

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 154 SVVICFYNEA--FSALLRtvhSVIDRTPAHLLHEIILVDDdsdfddlkGELD---EYVQKY--LPGKIKVIRNTKReglI 226
Cdd:cd02525     3 SIIIPVRNEEkyIEELLE---SLLNQSYPKDLIEIIVVDG--------GSTDgtrEIVQEYaaKDPRIRLIDNPKR---I 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944640 227 R--GRMIGAAHA-TEVLVFLDSHCEVNVMWLQPLLAAIREDrhtvvcpvidiiSADTLAYSSSPVVRGGFNWGLHFkwdl 303
Cdd:cd02525    69 QsaGLNIGIRNSrGDIIIRVDAHAVYPKDYILELVEALKRT------------GADNVGGPMETIGESKFQKAIAV---- 132