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 564389016 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNLNEFKEWQ 609
Cdd:cd23437    1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 564389016 610 YFKNLHRFTHIASGKCLDRSEVLHQVFISSCDNGKMTQKWEMNN 653
Cdd:cd23437   81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124

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 564389016 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNLNEFKEWQ 609
Cdd:cd23437    1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 564389016 610 YFKNLHRFTHIASGKCLDRSEVLHQVFISSCDNGKMTQKWEMNN 653
Cdd:cd23437   81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389016  534 WGEIRGLETAYCIDSMG-KTNGGFVELGPCHRMGGNQLFRINEANQLMQY--DQCLTKG--PDGSKVMITHCNLNEFKE- 607
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGgSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVasDLCLDVGstADGAKVVLWPCHPGNGNQr 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 564389016  608 WQYFKNLHRFTHIASGKCLDRSEVLH---QVFISSCDNGKMTQKW 649
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 564389016 210 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLTEYIKLWNGlVKVFRNERREGLIQARSIGAQ 289
Cdd:COG0463    5 SVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGS-TDGTAEILRELAAKDPR-IRVIRLERNRGKGAARNAGLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389016 290 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRAtctvpliDYIDGNDYSiepqQGGDEDGFARGAWDWSMLWKRIPLSH 369
Cdd:COG0463   80 AAR-GDYIAFLDADDQLDPEKLEELVAALEEGPA-------DLVYGSRLI----REGESDLRRLGSRLFNLVRLLTNLPD 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564389016 370 kekakrkhktepyrspaMAGGLFAIERDFFFELGlYDPGLqiwgGENFEIsYKIWQCGGKLLFVP 434
Cdd:COG0463  148 -----------------STSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVP 189

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 564389016 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNLNEFKEWQ 609
Cdd:cd23437    1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 564389016 610 YFKNLHRFTHIASGKCLDRSEVLHQVFISSCDNGKMTQKWEMNN 653
Cdd:cd23437   81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124

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 564389016  210 SVVIVFHNEgWSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLTEYIKLwNGLVKVFRNERREGLIQARSIGAQ 289
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKK-DPRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389016  290 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRATCTVPLIDYIDGNDYSiepqqggdedgfargaWDWSMLWKRIPLSH 369
Cdd:pfam00535  76 AAT-GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGE----------------YRRASRITLSRLPF 138

                         170       180
                  ....*....|....*....|....*...
gi 564389016  370 KEKAKRKHKTEPYRSPAMAGGLFAIERD 397
Cdd:pfam00535 139 FLGLRLLGLNLPFLIGGFALYRREALEE 166

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 564389016 535 GEIRGLETAYCIDSMGKTNGGF-VELGPCHRMGGNQLFRINEANQLMQYDQCLTkGPDGSKVMITHCNLNEFKE-WQYFK 612
Cdd:cd23460    3 GQIKHTESGLCLDWAGESNGDKtVALKPCHGGGGNQFWMYTGDGQIRQDHLCLT-ADEGNKVTLRECADQLPSQeWSYDE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564389016 613 NLHRFTHIASGKCLDRSEVLHQVFISSCDNGKMTQKWEMN 652
Cdd:cd23460   82 KTGTIRHRSTGLCLTLDANNDVVILKECDSNSLWQKWIFQ 121

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 564389016 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELG--PCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHC-NLNEFK 606
Cdd:cd23462    1 EALAYGEIRNLAGKLCLDAPGRKKELNKPVGlyPCHGQGGNQYWMLTKDGEIRRDDLCLDYAGGSGDVTLYPChGMKGNQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 564389016 607 EWQYFKNLHRFTHIASGKCLDRSEVLHQVFISSCDNGKMTQKWE 650
Cdd:cd23462   81 FWIYDEETKQIVHGTSKKCLELSDDSSKLVMEPCNGSSPRQQWE 124

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 564389016 534 WGEIRGLETAYCIDSMGKTNGGFVELG--PCHRMG-GNQLFRINEANQLMQYDQCLT-KGPDGSKVMITHC--NLNEFKE 607
Cdd:cd23459    7 YGQVRNPGTNLCLDTLQRDEDKGYNLGlyPCQGGLsSNQLFSLSKKGELRREESCADvQGTEESKVILITChgLEKFNQK 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 564389016 608 WQYFKNLHRFtHIASGKCLDRSEV--LHQVFISSCDnGKMTQKWEMNN 653
Cdd:cd23459   87 WKHTKGGQIV-HLASGKCLDAEGLksGDDVTLAKCD-GSLSQKWTFEH 132

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10)-like subfamily; The GALNT10-like subfamily includes GALNT10 and GALNTL6. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389016 534 WGEIRGLETAYCIDSMGKTNGGFVELGPC--HRMGGNQLFRIN--EANQLMQYDQCL--TKGPDGSKVMITHC-----NL 602
Cdd:cd23439    2 SGEIRNVGSGLCIDTKHGGENDEVRLSKCvkDGGGGEQQFELTwhEDIRPKKRKVCFdvSSHTPGAPVILYAChgmkgNQ 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 564389016 603 NefkeWQYFKNLHRFTHIASGKCLDRSEVLHQVFISSCDNGKMTQKW 649
Cdd:cd23439   82 L----WKYRPNTKQLYHPVSGLCLDADPGSGKVFMNHCDESSDTQKW 124

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 564389016 535 GEIRGLETAYCIDSMG--KTNGGFVELGPCHRMGGNQLFRINEANQL---MQYDQCLTKGPDGSkVMITHCNL-----NE 604
Cdd:cd23435    5 GALRNKGSELCLDVNNpnGQGGKPVIMYGCHGLGGNQYFEYTSKGEIrhnIGKELCLHASGSDE-VILQHCTSkgkdvPP 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 564389016 605 FKEWQYFKNLHRFtHIASGKCLDRSEvlHQVFISSCDNGKMTQKW 649
Cdd:cd23435   84 EQKWLFTQDGTIR-NPASGLCLHASG--YKVLLRTCNPSDDSQKW 125

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 564389016 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGP-DGSKVMITHCNLNEFKEW 608
Cdd:cd23467    2 RYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRlNGPVVMLKCHHMRGNQLW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 564389016 609 QYFKNLHRFTHIASGKCLDRSEVLHQVF--ISSCdNGKMTQKWEMNN 653
Cdd:cd23467   82 EYDAERLTLRHVNSNQCLDEPSEEDKMVptMKDC-SGSRSQQWLLRN 127

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389016 534 WGEIRGLETAYCID--SMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNL-NEFKEWQY 610
Cdd:cd23442    5 SGQLYNTGTGYCADyiHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSLQLCLDVRQEQVVLQNCTKeKTSQKWDF 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 564389016 611 FKNlHRFTHIASGKCLD--RSEVLHQVFISSCdNGKMTQKW 649
Cdd:cd23442   85 QET-GRIVHILSGKCIEavESENSKLLFLSPC-NGQRNQMW 123

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). 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. Pgant8 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 both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. 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 564389016 545 CIDSMGKTNGGFVELGPCHR----MGGNQLFRINEANQLMQY--DQCLTkgPDGSKVMITHCNLNEFKewQYFKNLHRFT 618
Cdd:cd23461   15 CLDILGRSHGGPPVLAKCSSnksmPGTFQNFSLTFHRQIKHGtsDDCLE--VRGNNVRLSRCHYQGGN--QYWKYDYETH 90

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564389016 619 HIASG----KCLDRSEVLHQVFISSCDNGKMTQKW 649
Cdd:cd23461   91 QLINGgqnnKCLEADVESLKITLSICDSDNVEQKW 125

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 564389016 534 WGEIRGLETAYCIDSMG--KTNGGFVELGPCHRmGGNQLFRINEAN------QLMQYDQCLT----KGPDGSKVMITHCN 601
Cdd:cd00161    2 TYRIVNAASGKCLDVAGgsTANGAPVQQWTCNG-GANQQWTLTPVGdgyytiRNVASGKCLDvaggSTANGANVQQWTCN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564389016 602 LNEFKEWQYFKNL---HRFTHIASGKCLD----RSEVLHQVFISSCDNGKmTQKW 649
Cdd:cd00161   81 GGDNQQWRLEPVGdgyYRIVNKHSGKCLDvsggSTANGANVQQWTCNGGA-NQQW 134

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389016 529 PRNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGN------QLFR------INEANQLMQYDQCLTKGPDGSKVM 596
Cdd:cd23477    2 PPPAAWGEIRNVAANLCVDSKHGATGTELRLDICVKDGSErtwsheQLFTfgwredIRPGEPLHTRKFCFDAISHNSPVT 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389016 597 ITHCN-LNEFKEWQYFKNLHRFtHIASGKCLDRSEVLHQVFISSCDNGKMTQKWEMNNIH 655
Cdd:cd23477   82 LYDCHgMKGNQLWSYRKDKTLF-HPVSNSCMDCNPADKKIFMNRCDPLSETQQWIFEHTN 140

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14) and similar proteins; GALNT14 (EC 2.4.1.41), also called polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, protein-UDP acetylgalactosaminyltransferase 14, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. GALNT14 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389016 535 GEIRglETAYCIDSMGKTNGGF--VELGPCHRMGG----NQLFRINEANQLMQYDQCL---TKGPdGSKVMITHCNLNEF 605
Cdd:cd23478   10 GVIR--QRQNCLESRRVEGQELpnLSLSPCIKSKGvpakSQEWAYTYNQQIRQQQLCLsvhTLFP-GSPVVLVPCKEGDG 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564389016 606 KEwQYFKNLHRFTHIASGKCLDR------SEVLHQVFISSCDNGKMTQKWEM 651
Cdd:cd23478   87 KQ-RWTKVGSHIEHMASRFCLDTemfgdgTESSKEIVINPCESSAMSQRWDM 137

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564389016  381 PYRSPAMAGGLFAIERDFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLLFVPCsRVGHIYRLE 445
Cdd:pfam02709  13 KLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG-DIGRYYMLY 76

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 564389016 535 GEIRGLETAYCID--SMGKTNGGFVELGPCHRmGGNQLFRINEANQLMQYDQCLT-KGP---DGSKVMITHCNLNEFKEW 608
Cdd:cd23451    3 GPVRLANAGKCLDvpGSSTADGNPVQIYTCNG-TAAQKWTLGTDGTLRVLGKCLDvSGGgtaNGTLVQLWDCNGTGAQKW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 564389016 609 QYFKNlHRFTHIASGKCLDRSEVLH----QVFISSCdNGKMTQKW 649
Cdd:cd23451   82 VPRAD-GTLYNPQSGKCLDAPGGSTtdgtQLQLYTC-NGTAAQQW 124

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564389016 581 QYDQCLTKGPDGSkVMITHCNLNEFKEWQYFKNLH---RFTHIASGKCLDrSEVLHQVFISSCDNGKmTQKWE 650
Cdd:cd23415    9 ATGRCLDSNAGGN-VYTGPCNGGPYQRWTWSGVGDgtvTLRNAATGRCLD-SNGNGGVYTLPCNGGS-YQRWR 78

ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and similar proteins; Ly-75, also called C-type lectin domain family 13 member B, DEC-205, gp200-MR6, or CD205, 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. Ly-75 contains 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389016 567 GNQLFRINEANqlmqYDQCLTkgPDGSKVMITHC-NLNEFKEWQYFKNlHRFTHIASGKCL--DRSEVLHQVFISSCDNG 643
Cdd:cd23411    1 GNDIFTIQHEN----SGKCLK--VENSQISAVDCkQSSESLQWKWVSE-HRLFNLGSKQCLglDITKPSNTLKMFECDSK 73

                 ....*.
gi 564389016 644 KMTQKW 649
Cdd:cd23411   74 SVMLWW 79