ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 461 KSFQMKIGNLCLDSMARKESEAPGLFGCHGTGGNQEWVFDQLtKTFKNaiSQLCLDFSSNTENKTVTMVKCENL-RPDTM 539
Cdd:cd23434   1 KFGSLKQGNLCLDTLGHKAGGTVGLYPCHGTGGNQEWSFTKD-GQIKH--DDLCLTVVDRAPGSLVTLQPCREDdSNQKW 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 72000997 540 VVEKNG-WLTQG--GKCLTVNQGSggDWLIYGAHCELNNGAQRWIF 582
Cdd:cd23434  78 EQIENNsKLRHVgsNLCLDSRNAK--SGGLTVETCDPSSGSQQWKF 121

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 461 KSFQMKIGNLCLDSMARKESEAPGLFGCHGTGGNQEWVFDQLtKTFKNaiSQLCLDFSSNTENKTVTMVKCENL-RPDTM 539
Cdd:cd23434   1 KFGSLKQGNLCLDTLGHKAGGTVGLYPCHGTGGNQEWSFTKD-GQIKH--DDLCLTVVDRAPGSLVTLQPCREDdSNQKW 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 72000997 540 VVEKNG-WLTQG--GKCLTVNQGSggDWLIYGAHCELNNGAQRWIF 582
Cdd:cd23434  78 EQIENNsKLRHVgsNLCLDSRNAK--SGGLTVETCDPSSGSQQWKF 121

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997   469 NLCLDSMARKESEAP-GLFGCHGTGGNQEWVFDQlTKTFKNAISQLCLDFSSNTENKTVTMVKCENLRPDTM-VVEKNG- 545
Cdd:pfam00652  11 GKCLDVPGGSSAGGPvGLYPCHGSNGNQLWTLTG-DGTIRSVASDLCLDVGSTADGAKVVLWPCHPGNGNQRwRYDEDGt 89

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 72000997   546 WLTQG--GKCLTVNQGSGGDWLIYGAHCELNNGAQRW 580
Cdd:pfam00652  90 QIRNPqsGKCLDVSGAGTSNGKVILWTCDSGNPNQQW 126

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 154 TVIITYHNEARSsLLRTVFSVFNQSPEELllEIVLVDDNSQD--VEIGKELAQIQ-RITVLRNNQREGLIRSRVKGAQVA 230
Cdd:COG0463   5 SVVIPTYNEEEY-LEEALESLLAQTYPDF--EIIVVDDGSTDgtAEILRELAAKDpRIRVIRLERNRGKGAARNAGLAAA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 231 RAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVapiidvinvdnfnyVGASADLRGGFDWTLVFRWEFMNEQLRkerha 310
Cdd:COG0463  82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLV--------------YGSRLIREGESDLRRLGSRLFNLVRLL----- 142

                       170       180
                ....*....|....*....|....*..
gi 72000997 311 hptapIRSPTMAGGLFAISKEWFNELG 337
Cdd:COG0463 143 -----TNLPDSTSGFRLFRREVLEELG 164

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 461 KSFQMKIGNLCLDSMARKESEAPGLFGCHGTGGNQEWVFDQLtKTFKNaiSQLCLDFSSNTENKTVTMVKCENL-RPDTM 539
Cdd:cd23434   1 KFGSLKQGNLCLDTLGHKAGGTVGLYPCHGTGGNQEWSFTKD-GQIKH--DDLCLTVVDRAPGSLVTLQPCREDdSNQKW 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 72000997 540 VVEKNG-WLTQG--GKCLTVNQGSggDWLIYGAHCELNNGAQRWIF 582
Cdd:cd23434  78 EQIENNsKLRHVgsNLCLDSRNAK--SGGLTVETCDPSSGSQQWKF 121

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997   469 NLCLDSMARKESEAP-GLFGCHGTGGNQEWVFDQlTKTFKNAISQLCLDFSSNTENKTVTMVKCENLRPDTM-VVEKNG- 545
Cdd:pfam00652  11 GKCLDVPGGSSAGGPvGLYPCHGSNGNQLWTLTG-DGTIRSVASDLCLDVGSTADGAKVVLWPCHPGNGNQRwRYDEDGt 89

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 72000997   546 WLTQG--GKCLTVNQGSGGDWLIYGAHCELNNGAQRW 580
Cdd:pfam00652  90 QIRNPqsGKCLDVSGAGTSNGKVILWTCDSGNPNQQW 126

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 72000997 469 NLCLDSMARKESEAPGLFGCHGTGGNQEWVFdqltkTFKNAISQ--LCLDFSSNteNKTVTMVKCENLRP------Dtmv 540
Cdd:cd23433  15 NLCLDTMGRKAGEKVGLSSCHGQGGNQVFSY-----TAKGEIRSddLCLDASRK--GGPVKLEKCHGMGGnqeweyD--- 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 72000997 541 vEKNGWL--TQGGKCLTVNQGSGGDWLIYGAhCELNNGaQRWIFE 583
Cdd:cd23433  85 -KETKQIrhVNSGLCLTAPNEDDPNEPVLRP-CDGGPS-QKWELE 126

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 468 GNLCLDSMARKESEAPGLFGCHGTGGNQEWVFD---QLtktfknAISQLCLDFSSNTEnkTVTMVKCeNLRPDTMVV--E 542
Cdd:cd23437  13 TGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNeagQL------AVGEQCLTASGSGG--KVKLRKC-NLGETGKWEydE 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 72000997 543 KNGWLTQG--GKCLTVNQGSGGdwLIYgAHCELNNGAQRWIF 582
Cdd:cd23437  84 ATGQIRHKgtGKCLDLNEGTNK--LIL-QPCDSSSPSQKWEF 122

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 154 TVIITYHNEARSsLLRTVFSVFNQSPEELLLEIVLVDDNSQD--VEIGKELA-QIQRITVLRNNQREGLIRSRVKGAQVA 230
Cdd:COG1215  32 SVIIPAYNEEAV-IEETLRSLLAQDYPKEKLEVIVVDDGSTDetAEIARELAaEYPRVRVIERPENGGKAAALNAGLKAA 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 231 RAPVLTFLDSHIECNQKWLEPLLARIaENPKavvapiidvinvdnfnyVGASadlrggfdwtlvfrwefmneqlrkerha 310
Cdd:COG1215 111 RGDIVVFLDADTVLDPDWLRRLVAAF-ADPG-----------------VGAS---------------------------- 144

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 72000997 311 hptapirsptmaGGLFAISKEWFNELGTYDLDMevwGGENLEMSFRVWQCGGSLEIMPCSRVGHVFR 377
Cdd:COG1215 145 ------------GANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYEEAP 196

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 72000997 461 KSFQMKIGNLCLDsmARKESEAPGLFGCHGTGGNQEWVFDQLTKTFKNAISQLCLDFSSNTenKTVTMVKCEN 533
Cdd:cd23462  48 KDGEIRRDDLCLD--YAGGSGDVTLYPCHGMKGNQFWIYDEETKQIVHGTSKKCLELSDDS--SKLVMEPCNG 116

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 72000997 469 NLCLDSMARKESEAPGLFGCHGTGGNQewVFdQLTKTFKNAISQLCLDFSSntENKTVTMVKCENLR 535
Cdd:cd23466  15 NQCLDNMARKENEKVGIFNCHGMGGNQ--VF-SYTANKEIRTDDLCLDVSK--LNGPVMMLKCHHLK 76

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

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 72000997 466 KIGNLCLDSMARKESEAPGLFGCHGTGGNQEWVFDQLTKTFKNAISQLCLDfsSNTENKTVTMVKC 531
Cdd:cd23439  52 KKRKVCFDVSSHTPGAPVILYACHGMKGNQLWKYRPNTKQLYHPVSGLCLD--ADPGSGKVFMNHC 115

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 72000997 155 VIITYHNEARSsLLRTVFSVFNQSPEelLLEIVLVDDNSQDVEIGKELAQIQRITVLRNNQREGLIRSRVKGAQVARAPV 234
Cdd:cd04186   1 IIIVNYNSLEY-LKACLDSLLAQTYP--DFEVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 235 LTFLDSHIECNQKWLEPLLARIAENPKAVVApiidvinvdnfnyvgasadlrggfdwtlvfrwefmneqlrkerhahpta 314
Cdd:cd04186  78 VLLLNPDTVVEPGALLELLDAAEQDPDVGIV------------------------------------------------- 108

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 315 pirSPTMAGGLFAISKEWFNELGTYDLDMEVWgGENLEMSFRVWQCGGSLEIMPCSRVGH 374
Cdd:cd04186 109 ---GPKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYH 164

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 72000997 469 NLCLDSmarKESEAPG-----LFGCHGTGGNQewvFDQLTKTFK---NAISQLCLdfsSNTENKTVTMVKCEnlRPDTMV 540
Cdd:cd23435  13 ELCLDV---NNPNGQGgkpviMYGCHGLGGNQ---YFEYTSKGEirhNIGKELCL---HASGSDEVILQHCT--SKGKDV 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 72000997 541 VEKNGWL-TQGG--------KCLTVNQGSggdwlIYGAHCELNNGAQRWIFE 583
Cdd:cd23435  82 PPEQKWLfTQDGtirnpasgLCLHASGYK-----VLLRTCNPSDDSQKWTFI 128

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 72000997 155 VIITYHNEARS--SLLRTVFSVFNQSPEellLEIVLVDDNSQD--VEIGKELAQI-QRITVLRNNQREGLIRSRVKGAQV 229
Cdd:cd04179   1 VVIPAYNEEENipELVERLLAVLEEGYD---YEIIVVDDGSTDgtAEIARELAARvPRVRVIRLSRNFGKGAAVRAGFKA 77

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 72000997 230 ARAPVLTFLDS----HIECnqkwLEPLLARIAENPKAVV 264
Cdd:cd04179  78 ARGDIVVTMDAdlqhPPED----IPKLLEKLLEGGADVV 112

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 72000997 155 VIITYHNEARSsLLRTVFSVFNQS-PEELLlEIVLVDDNSQD--VEIGKELAQIQ--RITVLRNNQREGlirSRVK---- 225
Cdd:cd04192   1 VVIAARNEAEN-LPRLLQSLSALDyPKEKF-EVILVDDHSTDgtVQILEFAAAKPnfQLKILNNSRVSI---SGKKnalt 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 226 -GAQVARAPVLTFLDSHIECNQKWLEPLLARIA-ENPKAVVAPII---------DVINVDNFNYVGASAdlrGGFDWTLv 294
Cdd:cd04192  76 tAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQkEQIGLVAGPVIyfkgksllaKFQRLDWLSLLGLIA---GSFGLGK- 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 72000997 295 frwefmneqlrkerhahptapirsPTMAGGL-FAISKEWFNELGTYDLDMEVWGGE 349
Cdd:cd04192 152 ------------------------PFMCNGAnMAYRKEAFFEVGGFEGNDHIASGD 183

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 72000997 154 TVIITYHNEARSsLLRTVFSVFNQSPEELLLEIVLVDDNSQD--VEIGKELAQIQ-RITVLRNNQReglIRS--RVKGAQ 228
Cdd:cd02525   3 SIIIPVRNEEKY-IEELLESLLNQSYPKDLIEIIVVDGGSTDgtREIVQEYAAKDpRIRLIDNPKR---IQSagLNIGIR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 229 VARAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVAPIIDVINVDNFN----YVGASADLRGGfdwtLVFRwefmneQL 304
Cdd:cd02525  79 NSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQkaiaVAQSSPLGSGG----SAYR------GG 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 305 RKERHAHPTAPirsptmaGGLFaiSKEWFNELGTYDLDMEVwgGENLEMSFRVWQCGGSL 364
Cdd:cd02525 149 AVKIGYVDTVH-------HGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKI 197

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 72000997 469 NLCLDsmARKESEAPG----LFGCHGtGGNQEWVFDQLTK---TFKNAISQLCLDFS--SNTENKTVTMVKCENLRPDTM 539
Cdd:cd00161  11 GKCLD--VAGGSTANGapvqQWTCNG-GANQQWTLTPVGDgyyTIRNVASGKCLDVAggSTANGANVQQWTCNGGDNQQW 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 72000997 540 VVEKNGWLT------QGGKCLTVNQGSGGDwliyGAHCEL----NNGAQRW 580
Cdd:cd00161  88 RLEPVGDGYyrivnkHSGKCLDVSGGSTAN----GANVQQwtcnGGANQQW 134

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 72000997   315 PIRSPTMAGGLFAISKEWFNELGTYDLDMEVWGGENLEMSFRVWQCGGSLEImPCSRVGHVFRKKHP 381
Cdd:pfam02709  13 KLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIER-PPGDIGRYYMLYHK 78

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 11 (GALNT11) and similar proteins; GALNT11 (EC 2.4.1.41), also called polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes its activation, modulating the balance between motile and immotile (sensory) cilia at the left-right organizer (LRO). GALNT11 displays the same enzyme activity toward MUC1, MUC4, and EA2 as GALNT1. It is not involved in glycosylation of erythropoietin (EPO). GALNT11 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 72000997 464 QMKIGN-LCLDsMARKESEAPGLFGCHGTGGNQEWVFDQLTKTFkNAISQLCLDFSSNTENKTVTMVKC 531
Cdd:cd23440  51 ELRLANlLCLD-SSETSSDFPRLMKCHGSGGSQQWRFKKDNRLY-NPASGQCLAASKNGTSGYVTMDIC 117

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 72000997 461 KSFQMKIGNLCLDSmarkESEAPGLFGCHGTGGNQEWVFDQLTKTFKN-AISQLCLDFssNTENKTVTMVKC 531
Cdd:cd23461  51 RQIKHGTSDDCLEV----RGNNVRLSRCHYQGGNQYWKYDYETHQLINgGQNNKCLEA--DVESLKITLSIC 116

DPG_synthase is involved in protein N-linked glycosylation; 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 155 VIITYHNEARSsLLRTVFSVFNQSPEELLL--EIVLVDDNSQD--VEIGKELA--QIQRITVLRNNQREGlirsrvKGAQ 228
Cdd:cd04188   1 VVIPAYNEEKR-LPPTLEEAVEYLEERPSFsyEIIVVDDGSKDgtAEVARKLArkNPALIRVLTLPKNRG------KGGA 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 72000997 229 V------ARAPVLTFLD----SHIECnqkwLEPLL-ARIAENPKAVVA 265
Cdd:cd04188  74 VragmlaARGDYILFADadlaTPFEE----LEKLEeALKTSGYDIAIG 117

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000997 151 QPT-TVIITYHNEARSsLLRTVFSVFNQSPEELLLEIVLVDDNSQD--VEIGKELAQiQRITVLRNNQREGLIRSRVKGA 227
Cdd:cd06439  28 LPTvTIIIPAYNEEAV-IEAKLENLLALDYPRDRLEIIVVSDGSTDgtAEIAREYAD-KGVKLLRFPERRGKAAALNRAL 105

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 72000997 228 QVARAPVLTFLDShiecNQKWlEP----LLARIAENPK 261
Cdd:cd06439 106 ALATGEIVVFTDA----NALL-DPdalrLLVRHFADPS 138