pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932023  34 QEHLKDKLEE-YMARFSKVRIVRTKKREGLIRTRLLGASMARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVCPMID 112
Cdd:cd02510   42 KPELKLLLEEyYKKYLPKVKVLRLKKREGLIRARIAGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIID 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932023 113 VIDHNHFGYEAQAGDAmRGAFDWEMYYKRIPIPPELQRA-DPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQ 191
Cdd:cd02510  122 VIDADTFEYRGSSGDA-RGGFDWSLHFKWLPLPEEERRReSPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGEN 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932023 192 YEISFKVWMCGGEMFDVPCSRVGHIYR-KYVPYKVPSGTS-LARNLKRVAETWMDEFAEYIYQRRPEYRHLSTGDISAQK 269
Cdd:cd02510  201 LELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGSGtVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERK 280

                        250
                 ....*....|....*....
gi 767932023 270 ELRKQLKCKDFKWFMAAVA 288
Cdd:cd02510  281 ALRERLKCKSFKWYLENVY 299

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932023  34 QEHLKDKLEE-YMARFSKVRIVRTKKREGLIRTRLLGASMARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVCPMID 112
Cdd:cd02510   42 KPELKLLLEEyYKKYLPKVKVLRLKKREGLIRARIAGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIID 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932023 113 VIDHNHFGYEAQAGDAmRGAFDWEMYYKRIPIPPELQRA-DPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQ 191
Cdd:cd02510  122 VIDADTFEYRGSSGDA-RGGFDWSLHFKWLPLPEEERRReSPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGEN 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932023 192 YEISFKVWMCGGEMFDVPCSRVGHIYR-KYVPYKVPSGTS-LARNLKRVAETWMDEFAEYIYQRRPEYRHLSTGDISAQK 269
Cdd:cd02510  201 LELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGSGtVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERK 280

                        250
                 ....*....|....*....
gi 767932023 270 ELRKQLKCKDFKWFMAAVA 288
Cdd:cd02510  281 ALRERLKCKSFKWYLENVY 299

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932023  304 AWGEIRNVAANLCVDSK-HGATGTELRLDICvkDGSertwSHEQLFTFGWREDIRPgeplHTRKFCFDAIS--HNSPVTL 380
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPgGSSAGGPVGLYPC--HGS----NGNQLWTLTGDGTIRS----VASDLCLDVGStaDGAKVVL 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767932023  381 YDCHGMKGNQLWGYRKDRT-LFHPVSNSCMD---CNPAEKKIFMARCDPLSETQQW 432
Cdd:pfam00652  71 WPCHPGNGNQRWRYDEDGTqIRNPQSGKCLDvsgAGTSNGKVILWTCDSGNPNQQW 126

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932023   35 EHLKDKLEEYMARFSKVRIVRTKKREGLIRTRLLGASMARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVCPMIDVI 114
Cdd:pfam00535  39 DGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVI 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767932023  115 DhnhfgyeaqagdamRGAFDWEMYYKRIPIPPELQRADPSDPFESPVMAGGLFAVDRKWFWE 176
Cdd:pfam00535 119 F--------------GETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFALYRREALEE 166

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932023  34 QEHLKDKLEE-YMARFSKVRIVRTKKREGLIRTRLLGASMARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVCPMID 112
Cdd:cd02510   42 KPELKLLLEEyYKKYLPKVKVLRLKKREGLIRARIAGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIID 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932023 113 VIDHNHFGYEAQAGDAmRGAFDWEMYYKRIPIPPELQRA-DPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQ 191
Cdd:cd02510  122 VIDADTFEYRGSSGDA-RGGFDWSLHFKWLPLPEEERRReSPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGEN 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932023 192 YEISFKVWMCGGEMFDVPCSRVGHIYR-KYVPYKVPSGTS-LARNLKRVAETWMDEFAEYIYQRRPEYRHLSTGDISAQK 269
Cdd:cd02510  201 LELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGSGtVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERK 280

                        250
                 ....*....|....*....
gi 767932023 270 ELRKQLKCKDFKWFMAAVA 288
Cdd:cd02510  281 ALRERLKCKSFKWYLENVY 299

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10) and similar proteins; GALNT10 (EC 2.4.1.41), also called polypeptide GalNAc transferase 10, GalNAc-T10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, 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. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. GALNT10 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 767932023 299 EPPPAAWGEIRNVAANLCVDSKHGATGTELRLDICVKDGSERTWSHEQLFTFGWREDIRPGEPLHTRKFCFDAISHNSPV 378
Cdd:cd23476    1 EPPAAAWGEIRNVGTGLCADTKHGALGSPLRLEGCVKGRGEAAWNNGQVFTFGWREDIRPGDPQHTKKFCFDAISHNSPV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767932023 379 TLYDCHGMKGNQLWGYRKDRTLFHPVSNSCMDCNPAEKKIFMARCDPLSETQQWIFEHINMTVLEKFN 446
Cdd:cd23476   81 TLYDCHGMKGNQLWRYRKDKTLYHPVSNSCMDCSESDHRIFMNTCNPSSPTQQWLFEHTNSTVLEKFN 148

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 767932023 304 AWGEIRNVAANLCVDS--KHGATGTELRLDICVKDGSErtwsheQLFTFGWREDIRpgeplhTRKFCFDAISHNSPVTLY 381
Cdd:cd23462    4 AYGEIRNLAGKLCLDApgRKKELNKPVGLYPCHGQGGN------QYWMLTKDGEIR------RDDLCLDYAGGSGDVTLY 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767932023 382 DCHGMKGNQLWGYRK-DRTLFHPVSNSCMDCNPAEKKIFMARCDPLSETQQWIFE 435
Cdd:cd23462   72 PCHGMKGNQFWIYDEeTKQIVHGTSKKCLELSDDSSKLVMEPCNGSSPRQQWEFE 126

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 767932023 301 PPAAWGEIRNVAANLCVDSKHGATGTELRLDICVKDGsertwsHEQLFTFGWREDIRPGEplhtrkFCFDAISHNSPVTL 380
Cdd:cd23437    1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMG------GNQLFRLNEAGQLAVGE------QCLTASGSGGKVKL 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767932023 381 YDCHGmKGNQLWGY-RKDRTLFHPVSNSCMDCNPAEKKIFMARCDPLSETQQWIF 434
Cdd:cd23437   69 RKCNL-GETGKWEYdEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEF 122

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 767932023 306 GEIRNVAANLCVDSKHGATGTELRLDICVKDGSErtwsheQLFTFGWREDIRPGEPlhtrkfCFDAISHNSPVTLYDCHG 385
Cdd:cd23433    7 GEIRNVETNLCLDTMGRKAGEKVGLSSCHGQGGN------QVFSYTAKGEIRSDDL------CLDASRKGGPVKLEKCHG 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767932023 386 MKGNQLWGYRKDRTLF-HPVSNSCMDCNPAEKK--IFMARCDPlSETQQWIFE 435
Cdd:cd23433   75 MGGNQEWEYDKETKQIrHVNSGLCLTAPNEDDPnePVLRPCDG-GPSQKWELE 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 767932023 306 GEIRNVAANLCVDSKHGATGT-ELRLDICVKDGSERTWSheqlftfgWREDirpGEpLHTRKFCFDAIShNSPVTLYDCH 384
Cdd:cd23460    3 GQIKHTESGLCLDWAGESNGDkTVALKPCHGGGGNQFWM--------YTGD---GQ-IRQDHLCLTADE-GNKVTLRECA 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767932023 385 GMKGNQLWGYR-KDRTLFHPVSNSCMDCNPAEKKIFMARCDPLSETQQWIF 434
Cdd:cd23460   70 DQLPSQEWSYDeKTGTIRHRSTGLCLTLDANNDVVILKECDSNSLWQKWIF 120

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

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767932023   366 KFCFDAISHNSPVTLYDCHGMKGNQLWGYRKDRTLFHPVSNSCMDCN-PAEKKIFMARCDPLSETQQWIFEH 436
Cdd:smart00458   7 GKCLDVNGNKNPVGLFDCHGTGGNQLWKLTSDGAIRIKDTDLCLTANgNTGSTVTLYSCDGTNDNQYWEVNK 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 767932023 306 GEIRNVAANLCVDSKHGAT--GTELRLDICVKDGSERTWSheqlFTFgwREDIRPGeplhtRKFCFDAISHNSPV-TLYD 382
Cdd:cd23440    6 GQLKHAGSGLCLVAEDEVSqkGSLLVLRPCSRNDKKQLWY----YTE--DGELRLA-----NLLCLDSSETSSDFpRLMK 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767932023 383 CHGMKGNQLWGYRKDRTLFHPVSNSCMDCNPAEKK--IFMARCDPlSETQQWIF 434
Cdd:cd23440   75 CHGSGGSQQWRFKKDNRLYNPASGQCLAASKNGTSgyVTMDICSD-SPSQKWVF 127

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 767932023 304 AWGEIRNVAANLCVDS--KHGATGTELRLDICVKDGSERtwsheQLFTFGwrediRPGEpLHTRKFCFDAISH-NSPVTL 380
Cdd:cd23459    6 AYGQVRNPGTNLCLDTlqRDEDKGYNLGLYPCQGGLSSN-----QLFSLS-----KKGE-LRREESCADVQGTeESKVIL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767932023 381 YDCHG-MKGNQLWGYRKDRTLFHPVSNSCMDCNPAE--KKIFMARCDPlSETQQWIFEH 436
Cdd:cd23459   75 ITCHGlEKFNQKWKHTKGGQIVHLASGKCLDAEGLKsgDDVTLAKCDG-SLSQKWTFEH 132

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932023 303 AAWGEIRNvaANLCVDSKHGAT--GTELRLDICVKDGSERTWSheqlftfgWREDirpgEPLHTRKFC--FDAISHNSPV 378
Cdd:cd23441    3 LAYGQIKQ--GNLCLDSDEQLFqgPALLILAPCSNSSDSQEWS--------FTKD----GQLQTQGLCltVDSSSKDLPV 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767932023 379 TLYDChGMKGNQLWgYRKDRTLFHPVSNSCMDcNPAEKKIFMARCDPLSETQQWIFE 435
Cdd:cd23441   69 VLETC-SDDPKQKW-TRTGRQLVHSESGLCLD-SRKKKGLVVSPCRSGAPSQKWDFT 122

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767932023 368 CFDAISH--NSPVTLYDCHGMKGNQLWGYRKDRTLFHPvsNSC--MDCNPAEKKIFMARCDPLSETQQWIFEHIN 438
Cdd:cd23434   11 CLDTLGHkaGGTVGLYPCHGTGGNQEWSFTKDGQIKHD--DLCltVVDRAPGSLVTLQPCREDDSNQKWEQIENN 83

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) and similar proteins; GALNT3 (EC 2.4.1.41), also called polypeptide GalNAc transferase 3, GalNAc-T3, pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, 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. 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. GALNT3 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 767932023 302 PAAWGEIRNVAANLCVD---SKHGatGTELRLDICVKDGSErtwsheQLFTFGWREDIRpgeplHT--RKFCFDAiSHnS 376
Cdd:cd23468    2 PLIFGAIKNVGKELCLDvgeNNHG--GKPLIMYNCHGLGGN------QYFEYSTHHEIR-----HNiqKELCLHG-SQ-G 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767932023 377 PVTLYDCH--GMK----GNQLWGYRKDRTLFHPVSNSCMDCNPAEKKifMARCDPLSETQQWIF 434
Cdd:cd23468   67 SVQLKECTykGRNtavlPEEKWELQKDQLLYNPALNMCLSANGENPS--LVPCNPSDPFQQWIF 128

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 767932023 346 QLFTFGWREDIRpgeplHTRkFCFDAIS--HNSPVTLYDCHGMKGNQLWGYRK-DRTLFHPVSNSCMDCNPA-EKKIFMA 421
Cdd:cd23434   35 QEWSFTKDGQIK-----HDD-LCLTVVDraPGSLVTLQPCREDDSNQKWEQIEnNSKLRHVGSNLCLDSRNAkSGGLTVE 108

                         90
                 ....*....|...
gi 767932023 422 RCDPLSETQQWIF 434
Cdd:cd23434  109 TCDPSSGSQQWKF 121

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932023  39 DKLEEYMARFSKVRIVRTKKREGLIRTRLLGASMARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVC 108
Cdd:COG0463   47 EILRELAAKDPRIRVIRLERNRGKGAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY 116

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 767932023 304 AWGEIRNVAANLCVDSKHGAT--GTELRLDICvkdgserTWSHEQLFTFGWRED----IRpgePLHTRKfCFDA----IS 373
Cdd:cd00161    1 GTYRIVNAASGKCLDVAGGSTanGAPVQQWTC-------NGGANQQWTLTPVGDgyytIR---NVASGK-CLDVaggsTA 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767932023 374 HNSPVTLYDCHGmKGNQLWGYRKDR----TLFHPVSNSCMDCNPAEK----KIFMARCDPlSETQQW 432
Cdd:cd00161   70 NGANVQQWTCNG-GDNQQWRLEPVGdgyyRIVNKHSGKCLDVSGGSTangaNVQQWTCNG-GANQQW 134

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 15 (GALNT15) and similar proteins; GALNT15 (EC 2.4.1.41), also called polypeptide GalNAc transferase 15, GalNAc-T15, polypeptide GalNAc transferase-like protein 2, GalNAc-T-like protein 2, pp-GaNTase-like protein 2, polypeptide N-acetylgalactosaminyltransferase-like protein 2, protein-UDP acetylgalactosaminyltransferase-like protein 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, GALNT15 can transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. It prefers Muc1a as its substrate. GALNT15 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767932023 366 KFCFDAISHNS----PVTLYDCHGMKGNQLWGYRKDRTLFHPVSNSCMDCNpaEKKIFMARCDPLSETQQWIF 434
Cdd:cd23442   14 GYCADYIHGWRlaggPVELSPCSGQNGNQLFEYTSDKEIRFGSLQLCLDVR--QEQVVLQNCTKEKTSQKWDF 84

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 767932023 368 CFDAI--SHNSPVTLYDCHGMKGNQLWGYRKDRTLfhPVSNSCMDCNPAEKKIFMARCDPLSETQQWIFEHINMTVLekf 445
Cdd:cd23467   17 CLDNMgrKENEKVGIFNCHGMGGNQVFSYTADKEI--RTDDLCLDVSRLNGPVVMLKCHHMRGNQLWEYDAERLTLR--- 91

                 ....*.
gi 767932023 446 nhHANS 451
Cdd:cd23467   92 --HVNS 95

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 4 (GALNT4) and similar proteins; GALNT4 (EC 2.4.1.41), also called polypeptide GalNAc transferase 4, GalNAc-T4, pp-GaNTase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4, 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. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT4 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 767932023 302 PAAWGEIRNVA-ANLCVD---SKHGATGTELRLDICVKDGSErtwsheQLFTFGWREDIRPGEplhTRKFCFDAISHNSP 377
Cdd:cd23469    1 PGWHGAVRSMGiSSECLDynsPEHNPTGAHLSLFGCHGQGGN------QFFEYTSNKEIRFNS---VTELCAEVPDQKNY 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767932023 378 VTLYDC----HGMKGNQLWGYRKDRTLFHPVSNSCMDCNPAEK---KIFMARCDPLSETQQWIFE 435
Cdd:cd23469   72 IGMKHCpkdgSPVPANIIWHFKEDGTIYHPHSGMCISAYRTPEgraDVQMRTCDAGDKNQLWSFE 136

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 767932023 308 IRNVAANLCVDSKHGatGTELRLDICVKDGSERTW---SHEQLFTfgwredirpgepLHTRKfCFDA--ISHNSPVTLYD 382
Cdd:cd23385    5 IYNEDLGKCLAARSS--SSKVSLSTCNPNSPNQQWkwtSGHRLFN------------VGTGK-CLGVssSSPSSPLRLFE 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767932023 383 CHGMKGNQLWGYRKDrTLFHPVSNSCMDC-NPAEKKIFMarCDPLSETQQW 432
Cdd:cd23385   70 CDSEDELQKWKCSKD-GLLLLKGLGLLLLyDKSGKNVVV--SKGSGLSSRW 117

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 767932023 298 VEPPPAAWGEIRNVAANLCVDSKHGAT--GTELRLDICVKDGSERtWSHEQLFTFGWRedIRpgePLHTRKfCFDA---- 371
Cdd:cd00161   42 LTPVGDGYYTIRNVASGKCLDVAGGSTanGANVQQWTCNGGDNQQ-WRLEPVGDGYYR--IV---NKHSGK-CLDVsggs 114

                         90       100
                 ....*....|....*....|.
gi 767932023 372 ISHNSPVTLYDCHGmKGNQLW 392
Cdd:cd00161  115 TANGANVQQWTCNG-GANQQW 134

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 6 (GALNT6) and similar proteins; GALNT6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 6, GalNAc-T6, pp-GaNTase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6, 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. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT6 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 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
                 ....*....|....*....|....*....|....*....|....*....|
gi 767932023 368 CFDAISHN---SPVTLYDCHGMKGNQLWGYRKDRTLFHPVSNS-CMDCNP 413
Cdd:cd23470   15 CLDVGENNrggKPLIMYSCHGMGGNQYFEYTTHKELRHNIAKQlCLRVSK 64

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 6 (GALNT6) and similar proteins; GALNT6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 6, GalNAc-T6, pp-GaNTase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6, 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. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT6 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 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 767932023 302 PAAWGEIRNVAANLCVD---SKHGatGTELRLDICVKDGSErtwsheQLFTFGWREDIRpgeplHT--RKFCFDaiSHNS 376
Cdd:cd23470    1 PTFYGAIKNEGTNQCLDvgeNNRG--GKPLIMYSCHGMGGN------QYFEYTTHKELR-----HNiaKQLCLR--VSKG 65