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 1239961420 539 KNVEWGEIRGLETVYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKIMITHCNLNEFKEWQ 618
Cdd:cd23437     1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1239961420 619 YFKSLHRFTHIPSGKCLDRSDVLHQVFISNCDSSKMTQKWEMNN 662
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 1239961420 539 KNVEWGEIRGLETVYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKIMITHCNLNEFKEWQ 618
Cdd:cd23437     1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1239961420 619 YFKSLHRFTHIPSGKCLDRSDVLHQVFISNCDSSKMTQKWEMNN 662
Cdd:cd23437    81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239961420 543 WGEIRGLETVYCIDSMG-KTNGGFVELGPCHRMGGNQLFRINEANQLMQY--DQCLTKG--PDGSKIMITHCNLNEFKE- 616
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGgSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVasDLCLDVGstADGAKVVLWPCHPGNGNQr 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1239961420 617 WQYFKSLHRFTHIPSGKCLD---RSDVLHQVFISNCDSSKMTQKW 658
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 1239961420 219 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLDDYIKLWNGlVKVFRNERREGLIQARSIGAQ 298
Cdd:COG0463     5 SVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGS-TDGTAEILRELAAKDPR-IRVIRLERNRGKGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239961420 299 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRttctvplIDYIDGNDYSiepqQGGDEDGFARGAWDWSLLWKRIPLsy 378
Cdd:COG0463    80 AAR-GDYIAFLDADDQLDPEKLEELVAALEEGP-------ADLVYGSRLI----REGESDLRRLGSRLFNLVRLLTNL-- 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239961420 379 kekakrkhktepyrsPAMAGGLFAIERDFFFELGlYDPGLqiwgGENFEIsYKIWQCGGKLLFVP 443
Cdd:COG0463   146 ---------------PDSTSGFRLFRREVLEELG-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 1239961420 539 KNVEWGEIRGLETVYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKIMITHCNLNEFKEWQ 618
Cdd:cd23437     1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1239961420 619 YFKSLHRFTHIPSGKCLDRSDVLHQVFISNCDSSKMTQKWEMNN 662
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 1239961420 544 GEIRGLETVYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKIMITHCN-LNEFKEWQYFKS 622
Cdd:cd23433     7 GEIRNVETNLCLDTMGRKAGEKVGLSSCHGQGGNQVFSYTAKGEIRSDDLCLDASRKGGPVKLEKCHgMGGNQEWEYDKE 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1239961420 623 LHRFTHIPSGKCLD--RSDVLHQVFISNCDSSKmTQKWEMNN 662
Cdd:cd23433    87 TKQIRHVNSGLCLTapNEDDPNEPVLRPCDGGP-SQKWELEG 127

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239961420 543 WGEIRGLETVYCIDSMG-KTNGGFVELGPCHRMGGNQLFRINEANQLMQY--DQCLTKG--PDGSKIMITHCNLNEFKE- 616
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGgSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVasDLCLDVGstADGAKVVLWPCHPGNGNQr 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1239961420 617 WQYFKSLHRFTHIPSGKCLD---RSDVLHQVFISNCDSSKMTQKW 658
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 1239961420 539 KNVEWGEIRGLETVYCIDSMGKTNGGFVELG--PCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKIMITHC-NLNEFK 615
Cdd:cd23462     1 EALAYGEIRNLAGKLCLDAPGRKKELNKPVGlyPCHGQGGNQYWMLTKDGEIRRDDLCLDYAGGSGDVTLYPChGMKGNQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1239961420 616 EWQYFKSLHRFTHIPSGKCLDRSDVLHQVFISNCDSSKMTQKWE 659
Cdd:cd23462    81 FWIYDEETKQIVHGTSKKCLELSDDSSKLVMEPCNGSSPRQQWE 124

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 1 (Pgant1) and similar proteins; Pgant1, also called pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant1 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers the monoglycosylated Muc5AC-3 as a substrate. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239961420 543 WGEIRGLETVYCIDSMGKTNGGFVELG--PCHRMG-GNQLFRINEANQLMQYDQCLT-KGPDGSKIMITHC--NLNEFKE 616
Cdd:cd23459     7 YGQVRNPGTNLCLDTLQRDEDKGYNLGlyPCQGGLsSNQLFSLSKKGELRREESCADvQGTEESKVILITChgLEKFNQK 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1239961420 617 WQYFKSLHRFtHIPSGKCLDRSDV--LHQVFISNCDSSkMTQKWEMNN 662
Cdd:cd23459    87 WKHTKGGQIV-HLASGKCLDAEGLksGDDVTLAKCDGS-LSQKWTFEH 132

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. 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. 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. 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 1239961420 543 WGEIRGLETvyCIDSMGKTNGG--FVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPD--GSKIMITHCNLNEFKEWQ 618
Cdd:cd23441     5 YGQIKQGNL--CLDSDEQLFQGpaLLILAPCSNSSDSQEWSFTKDGQLQTQGLCLTVDSSskDLPVVLETCSDDPKQKWT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1239961420 619 YFKSlhRFTHIPSGKCLDrSDVLHQVFISNCDSSKMTQKWEM 660
Cdd:cd23441    83 RTGR--QLVHSESGLCLD-SRKKKGLVVSPCRSGAPSQKWDF 121

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 1239961420 544 GEIRGLETVYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGP-DGSKIMITHCNLNEFKEWQYFKS 622
Cdd:cd23467     7 GEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRlNGPVVMLKCHHMRGNQLWEYDAE 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1239961420 623 LHRFTHIPSGKCLDRSDVLHQVF--ISNCDSSKmTQKWEMNN 662
Cdd:cd23467    87 RLTLRHVNSNQCLDEPSEEDKMVptMKDCSGSR-SQQWLLRN 127

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 1239961420 544 GEIRGLETVYCIDSMG--KTNGGFVELGPCHRMGGNQLFRINEANQL---MQYDQCLTKGPDGSkIMITHCNL-----NE 613
Cdd:cd23435     5 GALRNKGSELCLDVNNpnGQGGKPVIMYGCHGLGGNQYFEYTSKGEIrhnIGKELCLHASGSDE-VILQHCTSkgkdvPP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1239961420 614 FKEWQYFKSLHRFtHIPSGKCLDRSDvlHQVFISNCDSSKMTQKW 658
Cdd:cd23435    84 EQKWLFTQDGTIR-NPASGLCLHASG--YKVLLRTCNPSDDSQKW 125

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 1239961420 219 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYLAEIVLIDDfSNKEHLKEKLDDYIKLWNGlVKVFRNERREGLIQARSIGAQ 298
Cdd:COG1215    32 SVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDD-GSTDETAEIARELAAEYPR-VRVIERPENGGKAAALNAGLK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239961420 299 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRTtctvplidyidgndysiepqqggdedgfargawdwsllwkriplsy 378
Cdd:COG1215   109 AAR-GDIVVFLDADTVLDPDWLRRLVAAFADPGV---------------------------------------------- 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239961420 379 kekakrkhktepyrspAMAGGLFAIERDFFFELGLYDPGLqiwGGENFEISYKIWQCGGKLLFVPCSRVGH 449
Cdd:COG1215   142 ----------------GASGANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYE 193

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 15 (GALNT15) and similar proteins; GALNT15 (EC 2.4.1.41), also called polypeptide GalNAc transferase 15, GalNAc-T15, polypeptide GalNAc transferase-like protein 2, GalNAc-T-like protein 2, pp-GaNTase-like protein 2, polypeptide N-acetylgalactosaminyltransferase-like protein 2, protein-UDP acetylgalactosaminyltransferase-like protein 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, GALNT15 can transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. It prefers Muc1a as its substrate. GALNT15 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239961420 543 WGEIRGLETVYCID--SMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKIMITHCNL-NEFKEWQY 619
Cdd:cd23442     5 SGQLYNTGTGYCADyiHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSLQLCLDVRQEQVVLQNCTKeKTSQKWDF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1239961420 620 FKSlHRFTHIPSGKCLDRSDVLHQ--VFISNCdSSKMTQKW 658
Cdd:cd23442    85 QET-GRIVHILSGKCIEAVESENSklLFLSPC-NGQRNQMW 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 1239961420 554 CIDSMGKTNGGF--VELGPCHRMGG----NQLFRINEANQLMQYDQCL---TKGPdGSKIMITHCNLNEFKEwQYFKSLH 624
Cdd:cd23478    18 CLESRRVEGQELpnLSLSPCIKSKGvpakSQEWAYTYNQQIRQQQLCLsvhTLFP-GSPVVLVPCKEGDGKQ-RWTKVGS 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1239961420 625 RFTHIPSGKCLDRSDVL------HQVFISNCDSSKMTQKWEM 660
Cdd:cd23478    96 HIEHMASRFCLDTEMFGdgtessKEIVINPCESSAMSQRWDM 137

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 1239961420 544 GEIRGLETVYCIDSMGK--TNGGFVELGPCHRMGGNQLFRINEANQLMQYDQ-CL-TKGPDGSKIMITHC-NLNEFKEWQ 618
Cdd:cd23440     6 GQLKHAGSGLCLVAEDEvsQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLlCLdSSETSSDFPRLMKChGSGGSQQWR 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1239961420 619 YFKSLHRFtHIPSGKCLDRSDVLH--QVFISNCDSSKmTQKWEM 660
Cdd:cd23440    86 FKKDNRLY-NPASGQCLAASKNGTsgYVTMDICSDSP-SQKWVF 127

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 16 (GALNT16) and similar proteins; GALNT16 (EC 2.4.1.41), also called polypeptide GalNAc transferase 16, GalNAc-T16, polypeptide GalNAc transferase-like protein 1, GalNAc-T-like protein 1, pp-GaNTase-like protein 1, polypeptide N-acetylgalactosaminyltransferase-like protein 1, protein-UDP acetylgalactosaminyltransferase-like protein 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. GALNT16 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 1239961420 537 PPKNVEWGEIRglETVYCIDSMGKTNGG--FVELGPCHRMGGNQLFR---INEANQLMQYDQCL--TKGPDGSKIMITHC 609
Cdd:cd23479     1 PEKEAIPGLIR--QGGNCLESQGQDTTGdtLLGLGECRGTASNLPASqewVLSDPLIRQQDKCLaiTSFSPGSKVILELC 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1239961420 610 NLNEFKEWQYFKSlHRFTHIPSGKCLD-RSDvlhQVFISNCDSSKMTQKWEM 660
Cdd:cd23479    79 NQKDGRQKWKLKG-SFIQHQVSGLCLDsQSG---RVVINQCQADLASQQWEL 126

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 1239961420 590 QYDQCLTKGPDGSKIMITHCNL-NEFKEWQYFkSLHRFTHIPSGKCLDRSDVLHQVFIS--NCDSSKMTQKWEMNN 662
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 1239961420 576 GNQLFRINEANqlmqYDQCLTkgPDGSKIMITHC-NLNEFKEWQYFkSLHRFTHIPSGKCL--DRSDVLHQVFISNCDSS 652
Cdd:cd23411     1 GNDIFTIQHEN----SGKCLK--VENSQISAVDCkQSSESLQWKWV-SEHRLFNLGSKQCLglDITKPSNTLKMFECDSK 73

                  ....*.
gi 1239961420 653 KMTQKW 658
Cdd:cd23411    74 SVMLWW 79

ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar proteins; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cytolysis by forming heptameric pores in target host membranes. After binding to target membranes, the protein assembles into a heptameric pre-pore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation. Hemolysin may be called "cytolysin" or "cytolytic toxin", according to a specific action for certain cells. For example, this subfamily includes Vibrio vulnificus cytolysin that attack blood cell membranes and cause cell rupture, thereby liberating hemoglobins. Members of this subfamily contain 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 may harbor a putative sugar-binding pocket.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239961420 592 DQCLTKGPDGsKIMITHCNLNEFKEWQYFKSLHRFTH-IPSGKCLDRSDVLhQVFISNCDSSkMTQKWE--MNNIHS 665
Cdd:cd23423    14 NRCLTVDNNG-RVTLESCDSGDRNQSWILDSEGRYRSrVAPDLCLDADDDG-LLTLEQCSLS-LTQKWEweGDRLKN 87

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 1239961420 543 WGEIRGLETVYCIDsMGKTNGGFVEL--GPCHRMGGNQLF--------RINEANQL--------MQYDQCLTKGPDgski 604
Cdd:cd23470     4 YGAIKNEGTNQCLD-VGENNRGGKPLimYSCHGMGGNQYFeytthkelRHNIAKQLclrvskgpVQLGECHYKGKN---- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1239961420 605 miTHCNLNEfkEWQyFKSLHRFTHIPSGKCLDRSDvlHQVFISNCDSSKMTQKW 658
Cdd:cd23470    79 --SQVPPDE--EWE-LTQDHLIRNSGSNMCLTARG--KHPAMAPCNPADPHQLW 125

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 1239961420 544 GEIRGLETVYCID--SMGKTNGGFVELGPCHRmGGNQLFRINEANQLMQYDQCLT-KGP---DGSKIMITHCNLNEFKEW 617
Cdd:cd23451     3 GPVRLANAGKCLDvpGSSTADGNPVQIYTCNG-TAAQKWTLGTDGTLRVLGKCLDvSGGgtaNGTLVQLWDCNGTGAQKW 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1239961420 618 QYFKSlHRFTHIPSGKCLDRSDVLH----QVFISNCDSSKmTQKW 658
Cdd:cd23451    82 VPRAD-GTLYNPQSGKCLDAPGGSTtdgtQLQLYTCNGTA-AQQW 124