ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 18 (GALNT18) and similar proteins; GALNT18 (EC 2.4.1.41), also called polypeptide GalNAc transferase 18, GalNAc-T18, polypeptide GalNAc transferase-like protein 4, GalNAc-T-like protein 4, pp-GaNTase-like protein 4, polypeptide N-acetylgalactosaminyltransferase-like protein 4, protein-UDP acetylgalactosaminyltransferase-like protein 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT18 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 1390249233 399 MRMYSDIIAYGVLQNSLKTDLCLDQGPDTENVPIMYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRCLVDVNSRPRL 478
Cdd:cd23475     1 MRMYTDTIAYGVLQNSLKTDLCLDQGPDTDNIPIMYICHGMTPQNVYYTSNQQLHVGILSPTIDDDDNRCLVDVNSRPRL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249233 479 IECSYAKAKRMKLHWQFSQGGPIQNRKSKRCLELQENSDLEFGFQLVLQKCSGQHWSITNVL 540
Cdd:cd23475    81 IECSYAKAKRMKLYWLFTQGGSIQNKKSKRCLELQENADNEFGYQLVLQKCSGQRWTITNVL 142

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 18 (GALNT18) and similar proteins; GALNT18 (EC 2.4.1.41), also called polypeptide GalNAc transferase 18, GalNAc-T18, polypeptide GalNAc transferase-like protein 4, GalNAc-T-like protein 4, pp-GaNTase-like protein 4, polypeptide N-acetylgalactosaminyltransferase-like protein 4, protein-UDP acetylgalactosaminyltransferase-like protein 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT18 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 1390249233 399 MRMYSDIIAYGVLQNSLKTDLCLDQGPDTENVPIMYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRCLVDVNSRPRL 478
Cdd:cd23475     1 MRMYTDTIAYGVLQNSLKTDLCLDQGPDTDNIPIMYICHGMTPQNVYYTSNQQLHVGILSPTIDDDDNRCLVDVNSRPRL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249233 479 IECSYAKAKRMKLHWQFSQGGPIQNRKSKRCLELQENSDLEFGFQLVLQKCSGQHWSITNVL 540
Cdd:cd23475    81 IECSYAKAKRMKLYWLFTQGGSIQNKKSKRCLELQENADNEFGYQLVLQKCSGQRWTITNVL 142

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 1390249233 157 SIVFIFVNEAlSVLLRSIHSAMERTPPHLlkEIILVDDNSSnEELKEKLTEYVdkvnsQKPGFIKVVRHSKQEGLIRSRV 236
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGST-DGTVEIAEEYA-----KKDPRVRVIRLPENRGKAGARN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249233 237 SGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFeieEYPLAAQGFDWELWCRYLNppkaww 316
Cdd:pfam00535  72 AGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETG---EYRRASRITLSRLPFFLGL------ 142

                         170       180
                  ....*....|....*....|....*..
gi 1390249233 317 KLENSTAPIRSPaliGCFIVDRQYFQE 343
Cdd:pfam00535 143 RLLGLNLPFLIG---GFALYRREALEE 166

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249233 154 PEVSIVFIFVNEAlSVLLRSIHSAMERTPPHLlkEIILVDDNSSNEELkEKLTEYvdkvnSQKPGFIKVVRHSKQEGLIR 233
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTA-EILREL-----AAKDPRIRVIRLERNRGKGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249233 234 SRVSGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFdniKYDNFEIEEYPLAAQGFDWELWCRYLNPPK 313
Cdd:COG0463    73 ARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSR---LIREGESDLRRLGSRLFNLVRLLTNLPDST 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1390249233 314 AWWKLenstapIRSPALIGcFIVDRQYFQEIGLL 347
Cdd:COG0463   150 SGFRL------FRREVLEE-LGFDEGFLEDTELL 176

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 18 (GALNT18) and similar proteins; GALNT18 (EC 2.4.1.41), also called polypeptide GalNAc transferase 18, GalNAc-T18, polypeptide GalNAc transferase-like protein 4, GalNAc-T-like protein 4, pp-GaNTase-like protein 4, polypeptide N-acetylgalactosaminyltransferase-like protein 4, protein-UDP acetylgalactosaminyltransferase-like protein 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT18 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 1390249233 399 MRMYSDIIAYGVLQNSLKTDLCLDQGPDTENVPIMYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRCLVDVNSRPRL 478
Cdd:cd23475     1 MRMYTDTIAYGVLQNSLKTDLCLDQGPDTDNIPIMYICHGMTPQNVYYTSNQQLHVGILSPTIDDDDNRCLVDVNSRPRL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249233 479 IECSYAKAKRMKLHWQFSQGGPIQNRKSKRCLELQENSDLEFGFQLVLQKCSGQHWSITNVL 540
Cdd:cd23475    81 IECSYAKAKRMKLYWLFTQGGSIQNKKSKRCLELQENADNEFGYQLVLQKCSGQRWTITNVL 142

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8)-like subfamily; The GALNT8-like subfamily includes GALNT8, GALNT9, GALNT17 and GALNT18. 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. GALNT9 does not glycosylate apomucin or SDC3. 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 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 1390249233 404 DIIAYGVLQNSLKTDLCLDQGPDTENVPIMYICHGMTPQNVYYTSSQQIHVGILSPTVdDDDNRCLVDVNS--RPRLIEC 481
Cdd:cd23438     1 NTVAYGEMRNSLVTDLCLDQGPKENHTAILYPCHGWSPQLVRYTKDGQLYLGQLGSTA-SPDTRCLVDDGKsdKPQLLDC 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249233 482 SYAKaKRMKLHWQFSQGGPIQNRKSKRCLELQENSDlEFGFQLVLQKCSGQHWSITN 538
Cdd:cd23438    80 SKVK-NRLQKYWDFSQGGAIQNRATGRCLEVEEDKL-NFGHRLVLQTCSGQKWNIKN 134

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 17 (GALNT17) and similar proteins; GALNT17 (EC 2.4.1.41), also called polypeptide GalNAc transferase-like protein 3, GalNAc-T-like protein 3, pp-GaNTase-like protein 3, protein-UDP acetylgalactosaminyltransferase-like protein 3, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3, or Williams-Beuren syndrome chromosomal region 17 protein, may 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. GALNT17 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 1390249233 399 MRMYSDIIAYGVLQNSLKTDLCLDQGPDTENVPIMYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRCLVDvNSR--- 475
Cdd:cd23474     1 MRRYNNTVAYGELRNNKAKDVCLDQGPPENHTAILYPCHGWGPQLARYTKEGYLHLGALGTTTLLPDTRCLVD-NKKsrf 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249233 476 PRLIECSYAKAKRMKlHWQFSQGGPIQNRKSKRCLELQENSDleFGFQLVLQKCSGQHWSITNVLR 541
Cdd:cd23474    80 PQLLDCDKVKSILHK-RWNFIQNGAIMNLGTGRCLEVENRGN--FGIDLILRSCTGQRWTIKNFIK 142

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 1390249233 157 SIVFIFVNEAlSVLLRSIHSAMERTPPHLlkEIILVDDNSSnEELKEKLTEYVdkvnsQKPGFIKVVRHSKQEGLIRSRV 236
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGST-DGTVEIAEEYA-----KKDPRVRVIRLPENRGKAGARN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249233 237 SGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFeieEYPLAAQGFDWELWCRYLNppkaww 316
Cdd:pfam00535  72 AGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETG---EYRRASRITLSRLPFFLGL------ 142

                         170       180
                  ....*....|....*....|....*..
gi 1390249233 317 KLENSTAPIRSPaliGCFIVDRQYFQE 343
Cdd:pfam00535 143 RLLGLNLPFLIG---GFALYRREALEE 166

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249233 154 PEVSIVFIFVNEAlSVLLRSIHSAMERTPPHLlkEIILVDDNSSNEELkEKLTEYvdkvnSQKPGFIKVVRHSKQEGLIR 233
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTA-EILREL-----AAKDPRIRVIRLERNRGKGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249233 234 SRVSGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFdniKYDNFEIEEYPLAAQGFDWELWCRYLNPPK 313
Cdd:COG0463    73 ARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSR---LIREGESDLRRLGSRLFNLVRLLTNLPDST 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1390249233 314 AWWKLenstapIRSPALIGcFIVDRQYFQEIGLL 347
Cdd:COG0463   150 SGFRL------FRREVLEE-LGFDEGFLEDTELL 176

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 1390249233 406 IAYGVLQNSLkTDLCLDQGPDTEN---VPIMYICHGMtPQNVY--YTSSQQIHVGILSPTvddddnrCLVDVNSRPRLI- 479
Cdd:cd23435     2 GYYGALRNKG-SELCLDVNNPNGQggkPVIMYGCHGL-GGNQYfeYTSKGEIRHNIGKEL-------CLHASGSDEVILq 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249233 480 ECSYAK---AKRMKlhWQFSQGGPIQNRKSKRCLELQensdlefGFQLVLQKCSG----QHWSIT 537
Cdd:cd23435    73 HCTSKGkdvPPEQK--WLFTQDGTIRNPASGLCLHAS-------GYKVLLRTCNPsddsQKWTFI 128

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 1390249233 407 AYGVLQNsLKTDLCLD--QGPDTENVPIMYICHGMTPQNV-YYTSSQQI-HvgilsptvdddDNRCL-VDVNSRPRLIEC 481
Cdd:cd23460     1 GLGQIKH-TESGLCLDwaGESNGDKTVALKPCHGGGGNQFwMYTGDGQIrQ-----------DHLCLtADEGNKVTLREC 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249233 482 SYAKAKRMklhWQFS-QGGPIQNRKSKRCLELQENSDlefgfQLVLQKCSG----QHWSIT 537
Cdd:cd23460    69 ADQLPSQE---WSYDeKTGTIRHRSTGLCLTLDANND-----VVILKECDSnslwQKWIFQ 121

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249233 154 PEVSIVFIFVNEAlSVLLRSIHSAMERTPPHLlkEIILVDDNSSNEElkeklteyVDKVNSQKPGFIKVVRHSKQEGLIR 233
Cdd:COG1216     3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGT--------AELLAALAFPRVRVIRNPENLGFAA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249233 234 SRVSGWRAATAPVVALFDAHVEFNVGWAEPVLTRikenrkriispsfdnikydnfeieeyplaaqgfdwelwcrylnppk 313
Cdd:COG1216    72 ARNLGLRAAGGDYLLFLDDDTVVEPDWLERLLAA---------------------------------------------- 105

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1390249233 314 awwklenstapirspaliGCFIVDRQYFQEIGLLDEGMEVYGGEnVELGIR 364
Cdd:COG1216   106 ------------------ACLLIRREVFEEVGGFDERFFLYGED-VDLCLR 137

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 1390249233 158 IVFIFVNEAlSVLLRSIHSAMERTPPHLlkEIILVDDNSSnEELKEKLTEYVDKVNSqkpgfIKVVRHSKQEGLIRSRVS 237
Cdd:cd00761     1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGST-DGTLEILEEYAKKDPR-----VIRVINEENQGLAAARNA 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249233 238 GWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPS-----FDNIKYDNFEIEEYPLAAQGFDWELWCRYLN 310
Cdd:cd00761    72 GLKAARGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGpgnllFRRELLEEIGGFDEALLSGEEDDDFLLRLLR 149

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 1390249233 164 NEA--LSVLLRSIHSAMERTPPHllkEIILVDDNSSNEELkEKLTEYVDKVNSqkpgfIKVVRHSKQEGLIRSRVSGWRA 241
Cdd:cd04179     7 NEEenIPELVERLLAVLEEGYDY---EIIVVDDGSTDGTA-EIARELAARVPR-----VRVIRLSRNFGKGAAVRAGFKA 77

                          90
                  ....*....|.
gi 1390249233 242 ATAPVVALFDA 252
Cdd:cd04179    78 ARGDIVVTMDA 88

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 1390249233 409 GVLQNSlKTDLCLD--QGPDTENVPI-MYICHGMTPQNVY-YTSSQQIHVGilsptvddDDNRCLvDVNS-RPRLIECSY 483
Cdd:cd23442     6 GQLYNT-GTGYCADyiHGWRLAGGPVeLSPCSGQNGNQLFeYTSDKEIRFG--------SLQLCL-DVRQeQVVLQNCTK 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1390249233 484 AKAKRmklHWQFSQGGPIQNRKSKRCLELQENSDLEFGFqlvLQKCSGQ 532
Cdd:cd23442    76 EKTSQ---KWDFQETGRIVHILSGKCIEAVESENSKLLF---LSPCNGQ 118

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249233 154 PEVSIVFIFVNEALSVLLRSIHSAMERTPPHLlkEIILVDDNSSNEELKEKLTEYvdkvnSQKPGFIKVVRHSKQEGLIR 233
Cdd:cd04184     1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKY-----AAQDPRIKVVFREENGGISA 73

                          90
                  ....*....|....*...
gi 1390249233 234 SRVSGWRAATAPVVALFD 251
Cdd:cd04184    74 ATNSALELATGEFVALLD 91

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 1390249233 407 AYGVLQNSLkTDLCLD-QGPDTEN--VPIMYICHGMTPQNVYYTSSQQIHVGILSptvdDDDNRCLvDV-------NSRP 476
Cdd:cd00161     1 GTYRIVNAA-SGKCLDvAGGSTANgaPVQQWTCNGGANQQWTLTPVGDGYYTIRN----VASGKCL-DVaggstanGANV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249233 477 RLIECSYAKAKRMKLHWQFSQGGPIQNRKSKRCLELQENSdLEFGFQLVLQKCSG---QHW 534
Cdd:cd00161    75 QQWTCNGGDNQQWRLEPVGDGYYRIVNKHSGKCLDVSGGS-TANGANVQQWTCNGganQQW 134

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 12 (GALNT12) and similar proteins; GALNT12 (EC 2.4.1.41), also called polypeptide GalNAc transferase 12, GalNAc-T12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12, 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. 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. GALNT12 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
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1390249233 408 YGVLQNSLKTDLCLDQGPDTEN-----VPIMYICHGMTpQNVY--YTSSQQI 452
Cdd:cd23471     4 FGMLKNKGMTNYCFDYNPPDEHqiaghQVILYQCHGMG-QNQFfeYTSQNEI 54

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) and similar proteins; GALNT3 (EC 2.4.1.41), also called polypeptide GalNAc transferase 3, GalNAc-T3, pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT3 has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. It probably glycosylates fibronectin in vivo as well as FGF23. It plays a central role in phosphate homeostasis. GALNT3 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249233 408 YGVLQNsLKTDLCLDQGPDTENVP--IMYICHGMTpQNVY--YTSSQQIHVGIlsptvddDDNRCLVDVNSRPRLIECSY 483
Cdd:cd23468     5 FGAIKN-VGKELCLDVGENNHGGKplIMYNCHGLG-GNQYfeYSTHHEIRHNI-------QKELCLHGSQGSVQLKECTY 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 1390249233 484 AKAKRMKL---HWQFSQGGPIQNRKSKRCL 510
Cdd:cd23468    76 KGRNTAVLpeeKWELQKDQLLYNPALNMCL 105