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 1823817603 529 KNVDWGEIRGFETVYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKIMITHCNLNEFKEWQ 608
Cdd:cd23437     1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1823817603 609 YFKSLHRFTHIPSGKCLDRSEVLHQVFLSHCDSSKMTQKWEMNN 652
Cdd:cd23437    81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 529 KNVDWGEIRGFETVYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKIMITHCNLNEFKEWQ 608
Cdd:cd23437     1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1823817603 609 YFKSLHRFTHIPSGKCLDRSEVLHQVFLSHCDSSKMTQKWEMNN 652
Cdd:cd23437    81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 533 WGEIRGFETVYCIDSMG-KTNGGFVELGPCHRMGGNQLFRINEANQLMQY--DQCLTKG--PDGSKIMITHCNLNEFKE- 606
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGgSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVasDLCLDVGstADGAKVVLWPCHPGNGNQr 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1823817603 607 WQYFKSLHRFTHIPSGKCLDRSEVLH---QVFLSHCDSSKMTQKW 648
Cdd:pfam00652  82 WRYDEDGTQIRNPQSGKCLDVSGAGTsngKVILWTCDSGNPNQQW 126

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 209 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLDDYIKLWNGlVKVFRNERREGLIQARSIGAQ 288
Cdd:COG0463     5 SVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGS-TDGTAEILRELAAKDPR-IRVIRLERNRGKGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 289 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRttctvplIDYIDGNDYSiepqQGGDEDGFARGAWDWSLLWKRIPLSH 368
Cdd:COG0463    80 AAR-GDYIAFLDADDQLDPEKLEELVAALEEGP-------ADLVYGSRLI----REGESDLRRLGSRLFNLVRLLTNLPD 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1823817603 369 kekakrkhktepyrspaMAGGLFAIEREFFFELGlYDPGLqiwgGENFEIsYKIWQCGGKLLFVP 433
Cdd:COG0463   148 -----------------STSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVP 189

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 529 KNVDWGEIRGFETVYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKIMITHCNLNEFKEWQ 608
Cdd:cd23437     1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1823817603 609 YFKSLHRFTHIPSGKCLDRSEVLHQVFLSHCDSSKMTQKWEMNN 652
Cdd:cd23437    81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 534 GEIRGFETVYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKIMITHCN-LNEFKEWQYFKS 612
Cdd:cd23433     7 GEIRNVETNLCLDTMGRKAGEKVGLSSCHGQGGNQVFSYTAKGEIRSDDLCLDASRKGGPVKLEKCHgMGGNQEWEYDKE 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1823817603 613 LHRFTHIPSGKCLDRSEVLH--QVFLSHCDSSKmTQKWEMNN 652
Cdd:cd23433    87 TKQIRHVNSGLCLTAPNEDDpnEPVLRPCDGGP-SQKWELEG 127

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 533 WGEIRGFETVYCIDSMG-KTNGGFVELGPCHRMGGNQLFRINEANQLMQY--DQCLTKG--PDGSKIMITHCNLNEFKE- 606
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGgSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVasDLCLDVGstADGAKVVLWPCHPGNGNQr 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1823817603 607 WQYFKSLHRFTHIPSGKCLDRSEVLH---QVFLSHCDSSKMTQKW 648
Cdd:pfam00652  82 WRYDEDGTQIRNPQSGKCLDVSGAGTsngKVILWTCDSGNPNQQW 126

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 529 KNVDWGEIRGFETVYCIDSMGKTNGGFVELG--PCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKIMITHC-NLNEFK 605
Cdd:cd23462     1 EALAYGEIRNLAGKLCLDAPGRKKELNKPVGlyPCHGQGGNQYWMLTKDGEIRRDDLCLDYAGGSGDVTLYPChGMKGNQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1823817603 606 EWQYFKSLHRFTHIPSGKCLDRSEVLHQVFLSHCDSSKMTQKWE 649
Cdd:cd23462    81 FWIYDEETKQIVHGTSKKCLELSDDSSKLVMEPCNGSSPRQQWE 124

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 533 WGEIRGFETVYCIDSMGKTNGGFVELGPC--HRMGGNQLFRIN--EANQLMQYDQCL--TKGPDGSKIMITHC-----NL 601
Cdd:cd23439     2 SGEIRNVGSGLCIDTKHGGENDEVRLSKCvkDGGGGEQQFELTwhEDIRPKKRKVCFdvSSHTPGAPVILYAChgmkgNQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1823817603 602 NefkeWQYFKSLHRFTHIPSGKCLDRSEVLHQVFLSHCDSSKMTQKW 648
Cdd:cd23439    82 L----WKYRPNTKQLYHPVSGLCLDADPGSGKVFMNHCDESSDTQKW 124

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1) and similar proteins; GALNT1 (EC 2.4.1.41), also called polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT1 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 534 GEIRGFETVYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKIMITHC-NLNEFKEWQYFKS 612
Cdd:cd23466     7 GEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDDLCLDVSKLNGPVMMLKChHLKGNQLWEYDPV 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1823817603 613 LHRFTHIPSGKCLDR-SEVLHQV-FLSHCDSSKmTQKWEMNN 652
Cdd:cd23466    87 KLTLLHVNSNQCLDKaTEEDSQVpSIRDCNGSR-SQQWLLRN 127

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 209 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLDDYIKLWNGlVKVFRNERREGLIQARSIGAQ 288
Cdd:COG0463     5 SVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGS-TDGTAEILRELAAKDPR-IRVIRLERNRGKGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 289 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRttctvplIDYIDGNDYSiepqQGGDEDGFARGAWDWSLLWKRIPLSH 368
Cdd:COG0463    80 AAR-GDYIAFLDADDQLDPEKLEELVAALEEGP-------ADLVYGSRLI----REGESDLRRLGSRLFNLVRLLTNLPD 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1823817603 369 kekakrkhktepyrspaMAGGLFAIEREFFFELGlYDPGLqiwgGENFEIsYKIWQCGGKLLFVP 433
Cdd:COG0463   148 -----------------STSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVP 189

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 1823817603 210 VVIVFHNEGwSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLDDYIKlWNGLVKVFRNERREGLIQARSIGAQK 289
Cdd:cd00761     1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGS-TDGTLEILEEYAK-KDPRVIRVINEENQGLAAARNAGLKA 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1823817603 290 AKlGQVLIYLDAHCEVAVNWYAPLVAPISKDR 321
Cdd:cd00761    76 AR-GEYILFLDADDLLLPDWLERLVAELLADP 106

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 1823817603 534 GEIRGFETVYCIDSMG--KTNGGFVELGPCHRMGGNQLFRINEANQL---MQYDQCLTKGPDGSkIMITHCNL-----NE 603
Cdd:cd23435     5 GALRNKGSELCLDVNNpnGQGGKPVIMYGCHGLGGNQYFEYTSKGEIrhnIGKELCLHASGSDE-VILQHCTSkgkdvPP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1823817603 604 FKEWQYFKSLHRFtHIPSGKCLDRSEvlHQVFLSHCDSSKMTQKW 648
Cdd:cd23435    84 EQKWLFTQDGTIR-NPASGLCLHASG--YKVLLRTCNPSDDSQKW 125

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 1823817603 544 CIDSMGKTNGGFVELGPCHR----MGGNQLFRINEANQLMQY--DQCLTkgPDGSKIMITHCNLNEFKewQYFKSLHRFT 617
Cdd:cd23461    15 CLDILGRSHGGPPVLAKCSSnksmPGTFQNFSLTFHRQIKHGtsDDCLE--VRGNNVRLSRCHYQGGN--QYWKYDYETH 90

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1823817603 618 HIPSG----KCLDRSEVLHQVFLSHCDSSKMTQKW 648
Cdd:cd23461    91 QLINGgqnnKCLEADVESLKITLSICDSDNVEQKW 125

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 209 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEhLKEKLDDYIKLwNGLVKVFRNERReglIQ--ARSIG 286
Cdd:cd02525     3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTDG-TREIVQEYAAK-DPRIRLIDNPKR---IQsaGLNIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 287 AQKAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRTTCTVplidyidGNDYSIepqqggDEDGFARG-AWDWSLLWKRIP 365
Cdd:cd02525    77 IRNSR-GDIIIRVDAHAVYPKDYILELVEALKRTGADNVG-------GPMETI------GESKFQKAiAVAQSSPLGSGG 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1823817603 366 LSHKEKAKRKHKTEPYRSPAMagglfaiEREFFFELGLYDPGLQIwgGENFEISYKIWQCGGKLLFVPCSRVGH 439
Cdd:cd02525   143 SAYRGGAVKIGYVDTVHHGAY-------RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYY 207

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 1823817603 544 CIDSMGKTNGGF--VELGPCHRMGG----NQLFRINEANQLMQYDQCL---TKGPdGSKIMITHCNLNEFKEwQYFKSLH 614
Cdd:cd23478    18 CLESRRVEGQELpnLSLSPCIKSKGvpakSQEWAYTYNQQIRQQQLCLsvhTLFP-GSPVVLVPCKEGDGKQ-RWTKVGS 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1823817603 615 RFTHIPSGKCLDR------SEVLHQVFLSHCDSSKMTQKWEM 650
Cdd:cd23478    96 HIEHMASRFCLDTemfgdgTESSKEIVINPCESSAMSQRWDM 137

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10) and similar proteins; GALNT10 (EC 2.4.1.41), also called polypeptide GalNAc transferase 10, GalNAc-T10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, 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. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. GALNT10 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 1823817603 533 WGEIRGFETVYCIDSMGKTNGGFVELGPCHRMGGN------QLFR------INEANQLMQYDQCLTKGPDGSKIMITHCN 600
Cdd:cd23476     7 WGEIRNVGTGLCADTKHGALGSPLRLEGCVKGRGEaawnngQVFTfgwredIRPGDPQHTKKFCFDAISHNSPVTLYDCH 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1823817603 601 -LNEFKEWQYFKSlHRFTHIPSGKCLDRSEVLHQVFLSHCDSSKMTQKW 648
Cdd:cd23476    87 gMKGNQLWRYRKD-KTLYHPVSNSCMDCSESDHRIFMNTCNPSSPTQQW 134

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823817603 580 QYDQCLTKGPDGSKIMITHCNL-NEFKEWQYFkSLHRFTHIPSGKCLDRSEVLHQ--VFLSHCDSSKMTQKWEMNN 652
Cdd:cd23385     9 DLGKCLAARSSSSKVSLSTCNPnSPNQQWKWT-SGHRLFNVGTGKCLGVSSSSPSspLRLFECDSEDELQKWKCSK 83

ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and similar proteins; Ly-75, also called C-type lectin domain family 13 member B, DEC-205, gp200-MR6, or CD205, acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. Ly-75 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823817603 566 GNQLFRINEANqlmqYDQCLTkgPDGSKIMITHCN-LNEFKEWQYFkSLHRFTHIPSGKCL--DRSEVLHQVFLSHCDSS 642
Cdd:cd23411     1 GNDIFTIQHEN----SGKCLK--VENSQISAVDCKqSSESLQWKWV-SEHRLFNLGSKQCLglDITKPSNTLKMFECDSK 73

                  ....*.
gi 1823817603 643 KMTQKW 648
Cdd:cd23411    74 SVMLWW 79

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 1823817603 210 VVIVFHNEGwSTLMRTVHSVIKRTPRKYLAEIVLIDDFSN---KEHLKEKLDDYiklwnGLVKVFRNERREGLIQARSIG 286
Cdd:cd04179     1 VVIPAYNEE-ENIPELVERLLAVLEEGYDYEIIVVDDGSTdgtAEIARELAARV-----PRVRVIRLSRNFGKGAAVRAG 74

                          90
                  ....*....|....*
gi 1823817603 287 AQKAKlGQVLIYLDA 301
Cdd:cd04179    75 FKAAR-GDIVVTMDA 88

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 1823817603 533 WGEIRGFETVYCIDsMGKTNGGFVEL--GPCHRMGGNQLF--------RINEANQL--------MQYDQCLTKGPDgski 594
Cdd:cd23470     4 YGAIKNEGTNQCLD-VGENNRGGKPLimYSCHGMGGNQYFeytthkelRHNIAKQLclrvskgpVQLGECHYKGKN---- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1823817603 595 miTHCNLNEfkEWQyFKSLHRFTHIPSGKCLD-RSEvlhQVFLSHCDSSKMTQKW 648
Cdd:cd23470    79 --SQVPPDE--EWE-LTQDHLIRNSGSNMCLTaRGK---HPAMAPCNPADPHQLW 125