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 2462597541 489 KNVDWGEIRGFETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHCNLNEFKEWQ 568
Cdd:cd23437     1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462597541 569 YFKNLHRFTHIPSGKCLDRSEVLHQVFISNCDSSKTTQKWEMNN 612
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 2462597541 489 KNVDWGEIRGFETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHCNLNEFKEWQ 568
Cdd:cd23437     1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462597541 569 YFKNLHRFTHIPSGKCLDRSEVLHQVFISNCDSSKTTQKWEMNN 612
Cdd:cd23437    81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597541 493 WGEIRGFETAYCIDSMG-KTNGGFVELGPCHRMGGNQLFRINEANQLMQY--DQCLTKG--ADGSKVMITHCNLNEFKE- 566
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGgSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVasDLCLDVGstADGAKVVLWPCHPGNGNQr 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462597541 567 WQYFKNLHRFTHIPSGKCLDRSEVLH---QVFISNCDSSKTTQKW 608
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 2462597541 169 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLDEYIKLWNGlVKVFRNERREGLIQARSIGAQ 248
Cdd:COG0463     5 SVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGS-TDGTAEILRELAAKDPR-IRVIRLERNRGKGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597541 249 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRttctvplIDYIDGNDYSiepqQGGDEDGFARGAWDWSLLWKRIPLSH 328
Cdd:COG0463    80 AAR-GDYIAFLDADDQLDPEKLEELVAALEEGP-------ADLVYGSRLI----REGESDLRRLGSRLFNLVRLLTNLPD 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462597541 329 kekakrkhktepyrspaMAGGLFAIEREFFFELGlYDPGLqiwgGENFEIsYKIWQCGGKLLFVP 393
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 2462597541 489 KNVDWGEIRGFETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHCNLNEFKEWQ 568
Cdd:cd23437     1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462597541 569 YFKNLHRFTHIPSGKCLDRSEVLHQVFISNCDSSKTTQKWEMNN 612
Cdd:cd23437    81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1)-like subfamily; The GALNT1-like subfamily includes GALNT1 and GALNT13. They catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT1 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT13 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597541 494 GEIRGFETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHCN-LNEFKEWQYFKN 572
Cdd:cd23433     7 GEIRNVETNLCLDTMGRKAGEKVGLSSCHGQGGNQVFSYTAKGEIRSDDLCLDASRKGGPVKLEKCHgMGGNQEWEYDKE 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462597541 573 LHRFTHIPSGKCLDRSEVLH--QVFISNCDSSKtTQKWEMNN 612
Cdd:cd23433    87 TKQIRHVNSGLCLTAPNEDDpnEPVLRPCDGGP-SQKWELEG 127

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597541 493 WGEIRGFETAYCIDSMG-KTNGGFVELGPCHRMGGNQLFRINEANQLMQY--DQCLTKG--ADGSKVMITHCNLNEFKE- 566
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGgSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVasDLCLDVGstADGAKVVLWPCHPGNGNQr 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462597541 567 WQYFKNLHRFTHIPSGKCLDRSEVLH---QVFISNCDSSKTTQKW 608
Cdd:pfam00652  82 WRYDEDGTQIRNPQSGKCLDVSGAGTsngKVILWTCDSGNPNQQW 126

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597541 489 KNVDWGEIRGFETAYCIDSMGKTNGGFVELG--PCHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHC-NLNEFK 565
Cdd:cd23462     1 EALAYGEIRNLAGKLCLDAPGRKKELNKPVGlyPCHGQGGNQYWMLTKDGEIRRDDLCLDYAGGSGDVTLYPChGMKGNQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462597541 566 EWQYFKNLHRFTHIPSGKCLDRSEVLHQVFISNCDSSKTTQKWE 609
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 2462597541 488 PKNV-DWGEIRGFETAYCIDSMGKTNGGFVELG--PCHRMG-GNQLFRINEANQLMQYDQCLT-KGADGSKVMITHC--N 560
Cdd:cd23459     1 DEDVlAYGQVRNPGTNLCLDTLQRDEDKGYNLGlyPCQGGLsSNQLFSLSKKGELRREESCADvQGTEESKVILITChgL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462597541 561 LNEFKEWQYFKNLHRFtHIPSGKCLDRSEV--LHQVFISNCDSSKtTQKWEMNN 612
Cdd:cd23459    81 EKFNQKWKHTKGGQIV-HLASGKCLDAEGLksGDDVTLAKCDGSL-SQKWTFEH 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 2462597541 494 GEIRGFETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHC-NLNEFKEWQYFKN 572
Cdd:cd23466     7 GEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDDLCLDVSKLNGPVMMLKChHLKGNQLWEYDPV 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462597541 573 LHRFTHIPSGKCLDR-SEVLHQV-FISNCDSSKtTQKWEMNN 612
Cdd:cd23466    87 KLTLLHVNSNQCLDKaTEEDSQVpSIRDCNGSR-SQQWLLRN 127

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597541 169 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLDEYIKLWNGlVKVFRNERREGLIQARSIGAQ 248
Cdd:COG0463     5 SVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGS-TDGTAEILRELAAKDPR-IRVIRLERNRGKGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597541 249 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRttctvplIDYIDGNDYSiepqQGGDEDGFARGAWDWSLLWKRIPLSH 328
Cdd:COG0463    80 AAR-GDYIAFLDADDQLDPEKLEELVAALEEGP-------ADLVYGSRLI----REGESDLRRLGSRLFNLVRLLTNLPD 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462597541 329 kekakrkhktepyrspaMAGGLFAIEREFFFELGlYDPGLqiwgGENFEIsYKIWQCGGKLLFVP 393
Cdd:COG0463   148 -----------------STSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVP 189

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 2462597541 494 GEIRGFETAYCIDSMG--KTNGGFVELGPCHRMGGNQLFRINEANQL---MQYDQCLTKGADGSkVMITHCNL-----NE 563
Cdd:cd23435     5 GALRNKGSELCLDVNNpnGQGGKPVIMYGCHGLGGNQYFEYTSKGEIrhnIGKELCLHASGSDE-VILQHCTSkgkdvPP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462597541 564 FKEWQYFKNLHRFtHIPSGKCLDRSEvlHQVFISNCDSSKTTQKW 608
Cdd:cd23435    84 EQKWLFTQDGTIR-NPASGLCLHASG--YKVLLRTCNPSDDSQKW 125

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597541 170 VVIVFHNEGwSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLDEYIKlWNGLVKVFRNERREGLIQARSIGAQK 249
Cdd:cd00761     1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGS-TDGTLEILEEYAK-KDPRVIRVINEENQGLAAARNAGLKA 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462597541 250 AKlGQVLIYLDAHCEVAVNWYAPLVAPISKDR 281
Cdd:cd00761    76 AR-GEYILFLDADDLLLPDWLERLVAELLADP 106

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 2462597541 493 WGEIRGFETAYCID--SMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHCNL-NEFKEWQY 569
Cdd:cd23442     5 SGQLYNTGTGYCADyiHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSLQLCLDVRQEQVVLQNCTKeKTSQKWDF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462597541 570 FKNlHRFTHIPSGKCLD--RSEVLHQVFISNCdSSKTTQKW 608
Cdd:cd23442    85 QET-GRIVHILSGKCIEavESENSKLLFLSPC-NGQRNQMW 123

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 2462597541 489 KNVDWGEIRGFETAYCIDSMGK--TNGGFVELGPCHRMGGNQLFRINEANQLMQYDQ-CL---TKGADGSKVMITHcNLN 562
Cdd:cd23440     1 KVIRKGQLKHAGSGLCLVAEDEvsQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLlCLdssETSSDFPRLMKCH-GSG 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462597541 563 EFKEWQYFKNLHRFtHIPSGKCLDRSEVLH--QVFISNCDSSKtTQKWEM 610
Cdd:cd23440    80 GSQQWRFKKDNRLY-NPASGQCLAASKNGTsgYVTMDICSDSP-SQKWVF 127

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 2462597541 169 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEhLKEKLDEYIKLwNGLVKVFRNERReglIQ--ARSIG 246
Cdd:cd02525     3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTDG-TREIVQEYAAK-DPRIRLIDNPKR---IQsaGLNIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597541 247 AQKAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRTTCTVplidyidGNDYSIepqqggDEDGFARG-AWDWSLLWKRIP 325
Cdd:cd02525    77 IRNSR-GDIIIRVDAHAVYPKDYILELVEALKRTGADNVG-------GPMETI------GESKFQKAiAVAQSSPLGSGG 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462597541 326 LSHKEKAKRKHKTEPYRSPAMagglfaiEREFFFELGLYDPGLQIwgGENFEISYKIWQCGGKLLFVPCSRVGH 399
Cdd:cd02525   143 SAYRGGAVKIGYVDTVHHGAY-------RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYY 207

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462597541 540 QYDQCLTKGADGSKVMITHCNL-NEFKEWQYFKNlHRFTHIPSGKCLDRSEVLHQVFIS--NCDSSKTTQKWEMNN 612
Cdd:cd23385     9 DLGKCLAARSSSSKVSLSTCNPnSPNQQWKWTSG-HRLFNVGTGKCLGVSSSSPSSPLRlfECDSEDELQKWKCSK 83

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 2462597541 340 PYRSPAMAGGLFAIEREFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLLFVPCsRVGHIYRLE 404
Cdd:pfam02709  13 KLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG-DIGRYYMLY 76

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 2462597541 170 VVIVFHNeGWSTLMRTVHSVIKRTPRKYlaEIVLIDDFSNK---EHLKEKLDEyiklwnglVKVFRNERREGLIQARSIG 246
Cdd:cd04186     1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVDNASTDgsvELLRELFPE--------VRLIRNGENLGFGAGNNQG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597541 247 AQKAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRTTctvplidyidgndysiepqqggdedgfarGAWdwsllwkripl 326
Cdd:cd04186    70 IREAK-GDYVLLLNPDTVVEPGALLELLDAAEQDPDV-----------------------------GIV----------- 108

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462597541 327 shkekakrkhktepyrSPAMAGGLFAIEREFFFELGLYDPGLQIWGgENFEISYKIWQCGGKLLFVPCSRVGH 399
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 2462597541 494 GEIRGFETAYCID--SMGKTNGGFVELGPCHRmGGNQLFRINEANQLMQYDQCLT-KG---ADGSKVMITHCNLNEFKEW 567
Cdd:cd23451     3 GPVRLANAGKCLDvpGSSTADGNPVQIYTCNG-TAAQKWTLGTDGTLRVLGKCLDvSGggtANGTLVQLWDCNGTGAQKW 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462597541 568 QYFKNlHRFTHIPSGKCLDRSEVLH----QVFISNCDSSkTTQKW 608
Cdd:cd23451    82 VPRAD-GTLYNPQSGKCLDAPGGSTtdgtQLQLYTCNGT-AAQQW 124

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 2462597541 526 GNQLFRINEANqlmqYDQCLTkgADGSKVMITHCN-LNEFKEWQYFKNlHRFTHIPSGKCL--DRSEVLHQVFISNCDSS 602
Cdd:cd23411     1 GNDIFTIQHEN----SGKCLK--VENSQISAVDCKqSSESLQWKWVSE-HRLFNLGSKQCLglDITKPSNTLKMFECDSK 73

                  ....*.
gi 2462597541 603 KTTQKW 608
Cdd:cd23411    74 SVMLWW 79