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 12621080 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNLNEFKEWQ 609
Cdd:cd23437   1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 12621080 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 12621080 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNLNEFKEWQ 609
Cdd:cd23437   1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 12621080 610 YFKNLHRFTHIASGKCLDRSEVLHQVFISSCDNGKMTQKWEMNN 653
Cdd:cd23437  81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12621080   534 WGEIRGLETAYCIDSMG-KTNGGFVELGPCHRMGGNQLFRINEANQLMQY--DQCLTKG--PDGSKVMITHCNLNEFKE- 607
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGgSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVasDLCLDVGstADGAKVVLWPCHPGNGNQr 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 12621080   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 12621080 210 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLTEYIKLWNGlVKVFRNERREGLIQARSIGAQ 289
Cdd:COG0463   5 SVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGS-TDGTAEILRELAAKDPR-IRVIRLERNRGKGAARNAGLA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12621080 290 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRtictvpiIDVINGNTYeiipQGGGDEDGYARGAWDWSMLWKRVPLtp 369
Cdd:COG0463  80 AAR-GDYIAFLDADDQLDPEKLEELVAALEEGP-------ADLVYGSRL----IREGESDLRRLGSRLFNLVRLLTNL-- 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12621080 370 rekrlrktktepyrsPAMAGGLFAIERDFFFELGlYDPGLqiwgGENFEIsYKIWQCGGKLLFVP 434
Cdd:COG0463 146 ---------------PDSTSGFRLFRREVLEELG-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 12621080 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNLNEFKEWQ 609
Cdd:cd23437   1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 12621080 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 12621080   210 SVVIVFHNEgWSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLTEYIKLwNGLVKVFRNERREGLIQARSIGAQ 289
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKK-DPRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12621080   290 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRTICTVPIIDVINGNTYEIIPQgggdedgyargawdwSMLWKRVPLTP 369
Cdd:pfam00535  76 AAT-GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRA---------------SRITLSRLPFF 139

                         170       180
                  ....*....|....*....|....*...
gi 12621080   370 REKRLRKTKTePYRSPAMAGGLFAIERD 397
Cdd:pfam00535 140 LGLRLLGLNL-PFLIGGFALYRREALEE 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 12621080 535 GEIRGLETAYCIDSMGKTNGGF-VELGPCHRMGGNQLFRINEANQLMQYDQCLTkGPDGSKVMITHCNLNEFKE-WQYFK 612
Cdd:cd23460   3 GQIKHTESGLCLDWAGESNGDKtVALKPCHGGGGNQFWMYTGDGQIRQDHLCLT-ADEGNKVTLRECADQLPSQeWSYDE 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 12621080 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 12621080 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELG--PCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHC-NLNEFK 606
Cdd:cd23462   1 EALAYGEIRNLAGKLCLDAPGRKKELNKPVGlyPCHGQGGNQYWMLTKDGEIRRDDLCLDYAGGSGDVTLYPChGMKGNQ 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 12621080 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 12621080 534 WGEIRGLETAYCIDSMGKTNGGFVELG--PCHRMG-GNQLFRINEANQLMQYDQCLT-KGPDGSKVMITHC--NLNEFKE 607
Cdd:cd23459   7 YGQVRNPGTNLCLDTLQRDEDKGYNLGlyPCQGGLsSNQLFSLSKKGELRREESCADvQGTEESKVILITChgLEKFNQK 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 12621080 608 WQYFKNLHRFtHIASGKCLDRSEV--LHQVFISSCDnGKMTQKWEMNN 653
Cdd:cd23459  87 WKHTKGGQIV-HLASGKCLDAEGLksGDDVTLAKCD-GSLSQKWTFEH 132

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 12621080 535 GEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHC-NLNEFKEWQYFKN 613
Cdd:cd23466   7 GEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDDLCLDVSKLNGPVMMLKChHLKGNQLWEYDPV 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 12621080 614 LHRFTHIASGKCLDR-SEVLHQV-FISSCdNGKMTQKWEMNN 653
Cdd:cd23466  87 KLTLLHVNSNQCLDKaTEEDSQVpSIRDC-NGSRSQQWLLRN 127

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 12621080 535 GEIRGLETAYCIDSMG--KTNGGFVELGPCHRMGGNQLFRINEANQL---MQYDQCLTKGPDGSkVMITHCNL-----NE 604
Cdd:cd23435   5 GALRNKGSELCLDVNNpnGQGGKPVIMYGCHGLGGNQYFEYTSKGEIrhnIGKELCLHASGSDE-VILQHCTSkgkdvPP 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 12621080 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 12621080 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGP-DGSKVMITHCNLNEFKEW 608
Cdd:cd23467   2 RYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRlNGPVVMLKCHHMRGNQLW 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 12621080 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 12621080 534 WGEIRGLETAYCID--SMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNL-NEFKEWQY 610
Cdd:cd23442   5 SGQLYNTGTGYCADyiHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSLQLCLDVRQEQVVLQNCTKeKTSQKWDF 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 12621080 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 12621080 545 CIDSMGKTNGGFVELGPCHR----MGGNQLFRINEANQLMQY--DQCLTkgPDGSKVMITHCNLNEFKewQYFKNLHRFT 618
Cdd:cd23461  15 CLDILGRSHGGPPVLAKCSSnksmPGTFQNFSLTFHRQIKHGtsDDCLE--VRGNNVRLSRCHYQGGN--QYWKYDYETH 90

                        90       100       110
                ....*....|....*....|....*....|....*
gi 12621080 619 HIASG----KCLDRSEVLHQVFISSCDNGKMTQKW 649
Cdd:cd23461  91 QLINGgqnnKCLEADVESLKITLSICDSDNVEQKW 125

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 12621080 210 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEhLKEKLTEYIKLwNGLVKVFRNERReglIQ--ARSIG 287
Cdd:cd02525   3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTDG-TREIVQEYAAK-DPRIRLIDNPKR---IQsaGLNIG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12621080 288 AQKAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRTICTVPIIDVINGNTYEII-------PQGGGDedgyargawdwsm 360
Cdd:cd02525  77 IRNSR-GDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAiavaqssPLGSGG------------- 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12621080 361 lwkrvpltpreKRLRKTKTEPYRSPAMAGGLFaiERDFFFELGLYDPGLQIwgGENFEISYKIWQCGGKLLFVPCSRVGH 440
Cdd:cd02525 143 -----------SAYRGGAVKIGYVDTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYY 207

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 12621080 529 PRNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGN------QLFR------INEANQLMQYDQCLTKGPDGSKVM 596
Cdd:cd23477   2 PPPAAWGEIRNVAANLCVDSKHGATGTELRLDICVKDGSErtwsheQLFTfgwredIRPGEPLHTRKFCFDAISHNSPVT 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 12621080 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 12621080 535 GEIRglETAYCIDSMGKTNGGF--VELGPCHRMGG----NQLFRINEANQLMQYDQCL---TKGPdGSKVMITHCNLNEF 605
Cdd:cd23478  10 GVIR--QRQNCLESRRVEGQELpnLSLSPCIKSKGvpakSQEWAYTYNQQIRQQQLCLsvhTLFP-GSPVVLVPCKEGDG 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 12621080 606 KEwQYFKNLHRFTHIASGKCLDR------SEVLHQVFISSCDNGKMTQKWEM 651
Cdd:cd23478  87 KQ-RWTKVGSHIEHMASRFCLDTemfgdgTESSKEIVINPCESSAMSQRWDM 137

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12621080 211 VVIVFHNeGWSTLMRTVHSVIKRTPRKYlaEIVLIDDFSNK---EHLKEKLTEyiklwnglVKVFRNERREGLIQARSIG 287
Cdd:cd04186   1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVDNASTDgsvELLRELFPE--------VRLIRNGENLGFGAGNNQG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12621080 288 AQKAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRTIctvpiidvingntyeiipqgggdedgyarGAWdwsmlwkrvpl 367
Cdd:cd04186  70 IREAK-GDYVLLLNPDTVVEPGALLELLDAAEQDPDV-----------------------------GIV----------- 108

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12621080 368 tprekrlrktktepyrSPAMAGGLFAIERDFFFELGLYDPGLQIWGgENFEISYKIWQCGGKLLFVPCSRVGH 440
Cdd:cd04186 109 ----------------GPKVSGAFLLVRREVFEEVGGFDEDFFLYY-EDVDLCLRARLAGYRVLYVPQAVIYH 164

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 12621080 535 GEIRGLETAYCID--SMGKTNGGFVELGPCHRmGGNQLFRINEANQLMQYDQCLT-KGP---DGSKVMITHCNLNEFKEW 608
Cdd:cd23451   3 GPVRLANAGKCLDvpGSSTADGNPVQIYTCNG-TAAQKWTLGTDGTLRVLGKCLDvSGGgtaNGTLVQLWDCNGTGAQKW 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 12621080 609 QYFKNlHRFTHIASGKCLDRSEVLH----QVFISSCdNGKMTQKW 649
Cdd:cd23451  82 VPRAD-GTLYNPQSGKCLDAPGGSTtdgtQLQLYTC-NGTAAQQW 124

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12621080 211 VVIVFHNEGwSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEHLkEKLTEYIKLwNGLVKVFRNERREGLIQARSIGAQK 290
Cdd:cd04179   1 VVIPAYNEE-ENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTA-EIARELAAR-VPRVRVIRLSRNFGKGAAVRAGFKA 77

                        90
                ....*....|..
gi 12621080 291 AKlGQVLIYLDA 302
Cdd:cd04179  78 AR-GDIVVTMDA 88

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 12621080 567 GNQLFRINEANqlmqYDQCLTkgPDGSKVMITHC-NLNEFKEWQYFKNlHRFTHIASGKCL--DRSEVLHQVFISSCDNG 643
Cdd:cd23411   1 GNDIFTIQHEN----SGKCLK--VENSQISAVDCkQSSESLQWKWVSE-HRLFNLGSKQCLglDITKPSNTLKMFECDSK 73

                ....*.
gi 12621080 644 KMTQKW 649
Cdd:cd23411  74 SVMLWW 79