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 74195843 419 AFGALQQGTNCLDTLGHFADGVVGIYECHNAGGNQEWALTKEKSVKHMDLCLTVVDRSPGSLIRLQGCRENDSRQKWEQI 498
Cdd:cd23434   1 KFGSLKQGNLCLDTLGHKAGGTVGLYPCHGTGGNQEWSFTKDGQIKHDDLCLTVVDRAPGSLVTLQPCREDDSNQKWEQI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 74195843 499 EGNSKLRHVGSNLCLDSRTAKSGGLSVEVCGPA-LSQQWKF 538
Cdd:cd23434  81 ENNSKLRHVGSNLCLDSRNAKSGGLTVETCDPSsGSQQWKF 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 74195843 419 AFGALQQGTNCLDTLGHFADGVVGIYECHNAGGNQEWALTKEKSVKHMDLCLTVVDRSPGSLIRLQGCRENDSRQKWEQI 498
Cdd:cd23434   1 KFGSLKQGNLCLDTLGHKAGGTVGLYPCHGTGGNQEWSFTKDGQIKHDDLCLTVVDRAPGSLVTLQPCREDDSNQKWEQI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 74195843 499 EGNSKLRHVGSNLCLDSRTAKSGGLSVEVCGPA-LSQQWKF 538
Cdd:cd23434  81 ENNSKLRHVGSNLCLDSRNAKSGGLTVETCDPSsGSQQWKF 121

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74195843   419 AFGALQQGTN--CLDTLGHFADG-VVGIYECHNAGGNQEWALTKEKSVKHM--DLCLTVVDRSPGSLIRLQGCRENDSRQ 493
Cdd:pfam00652   1 ATGRIRNRASgkCLDVPGGSSAGgPVGLYPCHGSNGNQLWTLTGDGTIRSVasDLCLDVGSTADGAKVVLWPCHPGNGNQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 74195843   494 KWEQIEGNSKLRHVGSNLCLDSRTAKSGGLSVEV--CGP-ALSQQW 536
Cdd:pfam00652  81 RWRYDEDGTQIRNPQSGKCLDVSGAGTSNGKVILwtCDSgNPNQQW 126

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74195843 112 SVVITFHNEARSaLLRTVVSVLKRSPPHLikEIILVDDYSNDpedG------ALLGKIEKVRVLRNDRREGLMRSRVRGA 185
Cdd:COG0463   5 SVVIPTYNEEEY-LEEALESLLAQTYPDF--EIIVVDDGSTD---GtaeilrELAAKDPRIRVIRLERNRGKGAARNAGL 78

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 74195843 186 DAAQAKVLTFLDSHCECNERWLEPLLERVAEDRTRVV 222
Cdd:COG0463  79 AAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115

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 74195843 419 AFGALQQGTNCLDTLGHFADGVVGIYECHNAGGNQEWALTKEKSVKHMDLCLTVVDRSPGSLIRLQGCRENDSRQKWEQI 498
Cdd:cd23434   1 KFGSLKQGNLCLDTLGHKAGGTVGLYPCHGTGGNQEWSFTKDGQIKHDDLCLTVVDRAPGSLVTLQPCREDDSNQKWEQI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 74195843 499 EGNSKLRHVGSNLCLDSRTAKSGGLSVEVCGPA-LSQQWKF 538
Cdd:cd23434  81 ENNSKLRHVGSNLCLDSRNAKSGGLTVETCDPSsGSQQWKF 121

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 74195843   112 SVVITFHNEArSALLRTVVSVLKRspPHLIKEIILVDDYSNDPEDG---ALLGKIEKVRVLRNDRREGLMRSRVRGADAA 188
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQ--TYPNFEIIVVDDGSTDGTVEiaeEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74195843   189 QAKVLTFLDSHCECNERWLEPLLERVAEDRTRVVSPIIDVINMDNFQYVGASadlkggfdwnlvFKWDYMTPEQRRSRQG 268
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRAS------------RITLSRLPFFLGLRLL 145

                         170       180
                  ....*....|....*....|
gi 74195843   269 NPVAPIKTPMIAGGLFVMDK 288
Cdd:pfam00535 146 GLNLPFLIGGFALYRREALE 165

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74195843    429 CLDTLGHfaDGVVGIYECHNAGGNQEWALTKEKSVKHM--DLCLTvVDRSPGSLIRLQGCRENDSRQKWeQIEGNSKLRH 506
Cdd:smart00458   9 CLDVNGN--KNPVGLFDCHGTGGNQLWKLTSDGAIRIKdtDLCLT-ANGNTGSTVTLYSCDGTNDNQYW-EVNKDGTIRN 84

                           90       100       110
                   ....*....|....*....|....*....|...
gi 74195843    507 VGSNLCLDSRTAKSGG-LSVEVCGPALSQQWKF 538
Cdd:smart00458  85 PDSGKCLDVKDGNTGTkVILWTCSGNPNQKWIF 117

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 74195843 429 CLDTLGHFADGVVGIYECHNAGGNQEWALTKEKSVKHMDLCLTVvdRSPGSLIRLQGCRENDSrQKWEQIEGNSKLRHVG 508
Cdd:cd23437  16 CLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTA--SGSGGKVKLRKCNLGET-GKWEYDEATGQIRHKG 92

                        90       100       110
                ....*....|....*....|....*....|..
gi 74195843 509 SNLCLDsRTAKSGGLSVEVCGPAL-SQQWKFS 539
Cdd:cd23437  93 TGKCLD-LNEGTNKLILQPCDSSSpSQKWEFN 123

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 74195843 418 IAFGALQ-QGTN-CLDTLG--HFADGVVGIYECHNAGGNQEWALTKEKSVKHMDLCLTVvdRSPGSLIRLQGCRENDSRQ 493
Cdd:cd23462   3 LAYGEIRnLAGKlCLDAPGrkKELNKPVGLYPCHGQGGNQYWMLTKDGEIRRDDLCLDY--AGGSGDVTLYPCHGMKGNQ 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 74195843 494 KWEQIEGNSKLRHVGSNLCLDSRtAKSGGLSVEVC-GPALSQQWKFS 539
Cdd:cd23462  81 FWIYDEETKQIVHGTSKKCLELS-DDSSKLVMEPCnGSSPRQQWEFE 126

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 13 (GALNT13) and similar proteins; GALNT13 (EC 2.4.1.41), also called polypeptide GalNAc transferase 13, GalNAc-T13, pp-GaNTase 13, protein-UDP acetylgalactosaminyltransferase 13, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. GALNT13 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). The model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74195843 429 CLDTLGHFADGVVGIYECHNAGGNQEWALTKEKSVKHMDLCLTvVDRSPGSLIRLQgCRENDSRQKWEQIEGNSKLRHVG 508
Cdd:cd23467  17 CLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLD-VSRLNGPVVMLK-CHHMRGNQLWEYDAERLTLRHVN 94

                        90       100
                ....*....|....*....|....*....
gi 74195843 509 SNLCLDSRTAKSGGL-SVEVCGPALSQQW 536
Cdd:cd23467  95 SNQCLDEPSEEDKMVpTMKDCSGSRSQQW 123

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74195843 412 VPDHQDIAFGALQQGTNCLDTlgHFADG----VVGIYECHNAGG----NQEWALTKEKSVKHMDLCLTVVDRSPGSLIRL 483
Cdd:cd23478   1 IPDESDIQSGVIRQRQNCLES--RRVEGqelpNLSLSPCIKSKGvpakSQEWAYTYNQQIRQQQLCLSVHTLFPGSPVVL 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74195843 484 QGCRENDSRQKWEQIegNSKLRHVGSNLCLDSRTAKSGGLSVE--VCGP----ALSQQWKFSL 540
Cdd:cd23478  79 VPCKEGDGKQRWTKV--GSHIEHMASRFCLDTEMFGDGTESSKeiVINPcessAMSQRWDMVL 139

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 74195843 419 AFGALQ-QGTN-CLDTLG-HFADGVVGIYECHNAGGNQEWALTKEKSVKHMDLCLTVVDrspGSLIRLQGCRENDSRQKW 495
Cdd:cd23460   1 GLGQIKhTESGlCLDWAGeSNGDKTVALKPCHGGGGNQFWMYTGDGQIRQDHLCLTADE---GNKVTLRECADQLPSQEW 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 74195843 496 EQIEGNSKLRHVGSNLCLDSRtAKSGGLSVEVCGPA-LSQQWKF 538
Cdd:cd23460  78 SYDEKTGTIRHRSTGLCLTLD-ANNDVVILKECDSNsLWQKWIF 120

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74195843 109 PATSVVITFHNEArSALLRTVVSVLKRSPPHLikEIILVDDYSNDPEDGAL-LGKIEKVRVLRNDRREGLMRSRVRGADA 187
Cdd:COG1216   3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTAELLaALAFPRVRVIRNPENLGFAAARNLGLRA 79

                        90       100
                ....*....|....*....|....*
gi 74195843 188 AQAKVLTFLDSHCECNERWLEPLLE 212
Cdd:COG1216  80 AGGDYLLFLDDDTVVEPDWLERLLA 104

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 74195843 418 IAFGALQ-QGTN-CLDTLG--HFADGVVGIYECHNAGGNQEWALTKEKSVKH---MDLCLTVVDRSPgslIRLQGCRE-- 488
Cdd:cd23435   2 GYYGALRnKGSElCLDVNNpnGQGGKPVIMYGCHGLGGNQYFEYTSKGEIRHnigKELCLHASGSDE---VILQHCTSkg 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 74195843 489 --NDSRQKWEQIEGNSkLRHVGSNLCLdsrTAKSGGLSVEVCGPA-LSQQWKF 538
Cdd:cd23435  79 kdVPPEQKWLFTQDGT-IRNPASGLCL---HASGYKVLLRTCNPSdDSQKWTF 127

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant8 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74195843 429 CLDTLGHFADGVVGIYECHN----AGGNQEWALTKEKSVKH--MDLCLTVVDRSpgslIRLQGCRENDSRQKWE-QIEGN 501
Cdd:cd23461  15 CLDILGRSHGGPPVLAKCSSnksmPGTFQNFSLTFHRQIKHgtSDDCLEVRGNN----VRLSRCHYQGGNQYWKyDYETH 90

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 74195843 502 SKLRHVGSNLCLDSrTAKSGGLSVEVCGPA-LSQQWKFS 539
Cdd:cd23461  91 QLINGGQNNKCLEA-DVESLKITLSICDSDnVEQKWKWG 128

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 74195843 445 ECHNAGGNQEWALTKEKSVKHMD-LCLTVvDRSPGSLIRLQGCRENDSRQKWeQIEGNSKLRHVGSNLCLD-SRTAKSGG 522
Cdd:cd23440  34 PCSRNDKKQLWYYTEDGELRLANlLCLDS-SETSSDFPRLMKCHGSGGSQQW-RFKKDNRLYNPASGQCLAaSKNGTSGY 111

                        90
                ....*....|....*.
gi 74195843 523 LSVEVCGPALSQQWKF 538
Cdd:cd23440 112 VTMDICSDSPSQKWVF 127

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74195843    424 QQGTNCLDTLGHfADGVVGIYECHNAGGNQEWALTKEKSVKHMD--LCLTVVDRSPGSLIRLQGCrENDSRQKWEQI 498
Cdd:smart00458  44 KDTDLCLTANGN-TGSTVTLYSCDGTNDNQYWEVNKDGTIRNPDsgKCLDVKDGNTGTKVILWTC-SGNPNQKWIFE 118

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 74195843 429 CLDTLGHF-ADGV-VGIYEChNAGGNQEWALTKEKSVKHMDLCLTVVDRSP--GSLIRLQGCreNDSR-QKWEQIEGNSk 503
Cdd:cd23451  13 CLDVPGSStADGNpVQIYTC-NGTAAQKWTLGTDGTLRVLGKCLDVSGGGTanGTLVQLWDC--NGTGaQKWVPRADGT- 88

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 74195843 504 LRHVGSNLCLD---SRTAKSGGLSVEVCGPALSQQWK 537
Cdd:cd23451  89 LYNPQSGKCLDapgGSTTDGTQLQLYTCNGTAAQQWT 125

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

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74195843 467 DLCLTVvdrSPGSLIRLQGCRENDsRQKWE---QIEGNSKLRHVGSNLCLDSRTAksGGLSVEVCGPALSQQWKFS 539
Cdd:cd23415  11 GRCLDS---NAGGNVYTGPCNGGP-YQRWTwsgVGDGTVTLRNAATGRCLDSNGN--GGVYTLPCNGGSYQRWRVT 80

first ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating proteins (RIPs); Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. They consist of a catalytic A-chain which has rRNA N-glycosidase activity and a lectin B-chain containing two ricin B-type lectin domains 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 lectin chain facilitates the internalization of the catalytic chain on binding to the cell surface. The two chains are connected by a disulfide bridge. This model corresponds to the first ricin B-type lectin domain. Members of this subfamily includes Ricinus communis ricin, bitter gourd (Momordica charantia) seed lectin (BGSL), snake gourd (Trichosanthes anguina) seed lectin (SGSL), Sambucus ebulus ebulin I, Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf, Abrus precatorius abrin (ABR) and agglutinin-I (AAG), and Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74195843 429 CLDT-LGHFADGVVGI-YECHNAGGNQEWALTKEKSVKHMDLCLTVVDRSPGSLIRLQGCRE-NDSRQKWEqIEGNSKLR 505
Cdd:cd23443  12 CVDVkDGYYSDGNPVIlWPCKSQDANQLWTFKRDGTIRSNGKCLTTNGYSPGSYVVIYDCSTaVAEATKWE-VSDDGTII 90

                        90       100       110
                ....*....|....*....|....*....|..
gi 74195843 506 HVGSNLCLDSRTAKSG-GLSVEVCGPALSQQW 536
Cdd:cd23443  91 NPASGLVLTADSGTSGtTLTVETNIYASSQGW 122

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 6 (GALNT6) and similar proteins; GALNT6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 6, GalNAc-T6, pp-GaNTase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6, 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. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT6 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 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 74195843 420 FGALQ-QGTN-CLDTLGHFADGVVGI-YECHNAGGNQEWALTKEKSVKH---MDLCLTVvdrSPGSLiRLQGC--RENDS 491
Cdd:cd23470   4 YGAIKnEGTNqCLDVGENNRGGKPLImYSCHGMGGNQYFEYTTHKELRHniaKQLCLRV---SKGPV-QLGEChyKGKNS 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 74195843 492 R----QKWEqIEGNSKLRHVGSNLCLDSRTAKSgglSVEVCGPA-LSQQWKFS 539
Cdd:cd23470  80 QvppdEEWE-LTQDHLIRNSGSNMCLTARGKHP---AMAPCNPAdPHQLWSFS 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 74195843 113 VVITFHNEARS--ALLRTVVSVLKRSPPHlikEIILVDDYSNdpeDG------ALLGKIEKVRVLRNDRREGLMRSRVRG 184
Cdd:cd04179   1 VVIPAYNEEENipELVERLLAVLEEGYDY---EIIVVDDGST---DGtaeiarELAARVPRVRVIRLSRNFGKGAAVRAG 74

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 74195843 185 ADAAQAKVLTFLDSHCECNERWLEPLLERVAEDRTRVV 222
Cdd:cd04179  75 FKAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVV 112

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 74195843 112 SVVITFHNEARS--ALLRtvvSVLKRSPPHLIKEIILVDDYSndpEDG------ALLGKIEKVRVLRNDRR---EGlmrs 180
Cdd:cd02525   3 SIIIPVRNEEKYieELLE---SLLNQSYPKDLIEIIVVDGGS---TDGtreivqEYAAKDPRIRLIDNPKRiqsAG---- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74195843 181 RVRGADAAQAKVLTFLDSHCECNERWLEPLLERVAEDRTRVVSPIIDVINMDNFQ----YVGASADLKGGfdwnlvfkwd 256
Cdd:cd02525  73 LNIGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQkaiaVAQSSPLGSGG---------- 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74195843 257 ymtpeqRRSRQGnPVAPIKTPMIAGGLFVMDklYFEELGKYDMMMDVwgGENLEISFRVWQCGGSLEIIPCSRVGHVFR 335
Cdd:cd02525 143 ------SAYRGG-AVKIGYVDTVHHGAYRRE--VFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPR 210