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 1622903375 235 RPRFSGKLHNTGLGLCADCQAEGNVLDCPMVLAPCSDSRQQQYLQHTSRKEIHFGrPQHLCFAVRQEQVILQNCTEEgla 314
Cdd:cd23442     1 APYFSGQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFG-SLQLCLDVRQEQVVLQNCTKE--- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622903375 315 IHQQRWDFQENGMIVHILSGKCMEAVVQESNKDLYLRPCDGKARQQWR 362
Cdd:cd23442    77 KTSQKWDFQETGRIVHILSGKCIEAVESENSKLLFLSPCNGQRNQMWK 124

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 1622903375 235 RPRFSGKLHNTGLGLCADCQAEGNVLDCPMVLAPCSDSRQQQYLQHTSRKEIHFGrPQHLCFAVRQEQVILQNCTEEgla 314
Cdd:cd23442     1 APYFSGQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFG-SLQLCLDVRQEQVVLQNCTKE--- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622903375 315 IHQQRWDFQENGMIVHILSGKCMEAVVQESNKDLYLRPCDGKARQQWR 362
Cdd:cd23442    77 KTSQKWDFQETGRIVHILSGKCIEAVESENSKLLFLSPCNGQRNQMWK 124

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 1622903375   1 MLGATRATGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVVSPVIDVIDWKTFQYYPSKDLQRGVLDWKLDFHWEPLPEH 80
Cdd:pfam00535  71 NAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLP 150

                  ..
gi 1622903375  81 VR 82
Cdd:pfam00535 151 FL 152

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

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1622903375   3 GATRATGDVLVFMDAHCECHPGWLEPLLSRIAGDR 37
Cdd:COG1215   106 GLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG 140

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 1622903375 235 RPRFSGKLHNTGLGLCADCQAEGNVLDCPMVLAPCSDSRQQQYLQHTSRKEIHFGrPQHLCFAVRQEQVILQNCTEEgla 314
Cdd:cd23442     1 APYFSGQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFG-SLQLCLDVRQEQVVLQNCTKE--- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622903375 315 IHQQRWDFQENGMIVHILSGKCMEAVVQESNKDLYLRPCDGKARQQWR 362
Cdd:cd23442    77 KTSQKWDFQETGRIVHILSGKCIEAVESENSKLLFLSPCNGQRNQMWK 124

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 1622903375 236 PRFSGKLHNTGLGLCADCQAEGNVLDCPMVLAPCSDSRQQQYLQHTSRKEIHFGRPQHLCFAVRQEQ-VILQNCTEEGLA 314
Cdd:cd23435     1 PGYYGALRNKGSELCLDVNNPNGQGGKPVIMYGCHGLGGNQYFEYTSKGEIRHNIGKELCLHASGSDeVILQHCTSKGKD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622903375 315 I-HQQRWDFQENGMIVHILSGKCMEAvvqeSNKDLYLRPCDGKAR-QQWRFD 364
Cdd:cd23435    81 VpPEQKWLFTQDGTIRNPASGLCLHA----SGYKVLLRTCNPSDDsQKWTFI 128

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 3 (Pgant3) and similar proteins; Pgant3, also called pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant3 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers EA2 as a substrate and has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Pgant3 plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. It may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Together with Pgant35A, Pgant3 regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903375 240 GKLHNTGLGLCADCQAEGNVLDCPmVLAPCSDSRQQQYLQHTSRKEIhfgRPQHLCFAVRQ-EQVILQNCTEEGLAihqQ 318
Cdd:cd23460     3 GQIKHTESGLCLDWAGESNGDKTV-ALKPCHGGGGNQFWMYTGDGQI---RQDHLCLTADEgNKVTLRECADQLPS---Q 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622903375 319 RWDFQENGM-IVHILSGKCMEAVVQESNkdLYLRPCDGKA-RQQWRF 363
Cdd:cd23460    76 EWSYDEKTGtIRHRSTGLCLTLDANNDV--VILKECDSNSlWQKWIF 120

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903375  246 GLGLCADCQAEGNvldcPMVLAPCSDSRQQQYLQHTSRKEIhfgRPQ--HLCFAVRQ---EQVILQNCTEEGLAihqQRW 320
Cdd:smart00458   5 NTGKCLDVNGNKN----PVGLFDCHGTGGNQLWKLTSDGAI---RIKdtDLCLTANGntgSTVTLYSCDGTNDN---QYW 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1622903375  321 DFQENGMIVHILSGKCMEAVVQESNKDLYLRPCDGKARQQWRF 363
Cdd:smart00458  75 EVNKDGTIRNPDSGKCLDVKDGNTGTKVILWTCSGNPNQKWIF 117

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 4 (GALNT4) and similar proteins; GALNT4 (EC 2.4.1.41), also called polypeptide GalNAc transferase 4, GalNAc-T4, pp-GaNTase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT4 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 1622903375 236 PRFSGKLHNTGL-GLCADCQA-EGNVLDCPMVLAPCSDSRQQQYLQHTSRKEIHFGRPQHLCFAVRQEQ--VILQNCTEE 311
Cdd:cd23469     1 PGWHGAVRSMGIsSECLDYNSpEHNPTGAHLSLFGCHGQGGNQFFEYTSNKEIRFNSVTELCAEVPDQKnyIGMKHCPKD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622903375 312 GLAIHQQ-RWDFQENGMIVHILSGKCMEAV-VQESNKDLYLRPCD-GKARQQWRFD 364
Cdd:cd23469    81 GSPVPANiIWHFKEDGTIYHPHSGMCISAYrTPEGRADVQMRTCDaGDKNQLWSFE 136

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 1622903375 234 PRPRFsGKLHNTGLGLCADcqAEGNVLDCPMVLAPCSDSR------QQQYLQHTSRKEIHFGRPQH---LCF-AVRQEQ- 302
Cdd:cd23476     3 PAAAW-GEIRNVGTGLCAD--TKHGALGSPLRLEGCVKGRgeaawnNGQVFTFGWREDIRPGDPQHtkkFCFdAISHNSp 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622903375 303 VILQNCteEGLAiHQQRWDFQENGMIVHILSGKCMEAvvQESNKDLYLRPCDGKA-RQQWRFDQVNA 368
Cdd:cd23476    80 VTLYDC--HGMK-GNQLWRYRKDKTLYHPVSNSCMDC--SESDHRIFMNTCNPSSpTQQWLFEHTNS 141

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 1622903375 235 RPRFSGKLHNTGLGLCADCQAEGNvlDCPMVLAPCSDSRQQQYLQHTSRKEIHFGrpqHLCFAVR--QEQVILQNCTEEG 312
Cdd:cd23437     1 KNLAWGEIRNLGTGLCLDTMGHQN--GGPVGLYPCHGMGGNQLFRLNEAGQLAVG---EQCLTASgsGGKVKLRKCNLGE 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622903375 313 laihQQRWDFQE-NGMIVHILSGKCMEavVQESNKDLYLRPCDG-KARQQWRF 363
Cdd:cd23437    76 ----TGKWEYDEaTGQIRHKGTGKCLD--LNEGTNKLILQPCDSsSPSQKWEF 122

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 1622903375 239 SGKLHNTGLGLCADCQ-AEGNVldcPMVLAPCSDSRQQ--QYLQHTSRKEIhfgRP--QHLCF----AVRQEQVILQNCt 309
Cdd:cd23439     2 SGEIRNVGSGLCIDTKhGGEND---EVRLSKCVKDGGGgeQQFELTWHEDI---RPkkRKVCFdvssHTPGAPVILYAC- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903375 310 eeglaiHQ----QRWDFQEN-GMIVHILSGKCMEAVvqESNKDLYLRPCD-GKARQQWRF 363
Cdd:cd23439    75 ------HGmkgnQLWKYRPNtKQLYHPVSGLCLDAD--PGSGKVFMNHCDeSSDTQKWTW 126

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903375 234 PRPRFSGKLHNTGLGLCADC---QAEGNVldcpmVLAPCSDSRQQQYLQHTSRKEIHFGrpqHLCFAVRQ--EQVILQNC 308
Cdd:cd23433     1 LDYYSLGEIRNVETNLCLDTmgrKAGEKV-----GLSSCHGQGGNQVFSYTAKGEIRSD---DLCLDASRkgGPVKLEKC 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622903375 309 TEEGLaihQQRWDF-QENGMIVHILSGKCMEAVVQESNKDLYLRPCDGKARQQWRF 363
Cdd:cd23433    73 HGMGG---NQEWEYdKETKQIRHVNSGLCLTAPNEDDPNEPVLRPCDGGPSQKWEL 125

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase-like 6 (GALNTL6) and similar proteins; GALNTL6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 17, GalNAc-T17, pp-GaNTase 17, protein-UDP acetylgalactosaminyltransferase 17, putative polypeptide N-acetylgalactosaminyltransferase 17, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17, 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. GALNTL6 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 1622903375 233 EPRPRFSGKLHNTGLGLCADCQ--AEGNVLDCPMVLAPCSDS--RQQQYLQHTSRKEIHFGRPQH---LCF-AVRQEQ-V 303
Cdd:cd23477     1 EPPPAAWGEIRNVAANLCVDSKhgATGTELRLDICVKDGSERtwSHEQLFTFGWREDIRPGEPLHtrkFCFdAISHNSpV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622903375 304 ILQNCteEGLAIHQQrWDFQENGMIVHILSGKCMEAvvQESNKDLYLRPCDGK-ARQQWRFDQVNA 368
Cdd:cd23477    81 TLYDC--HGMKGNQL-WSYRKDKTLFHPVSNSCMDC--NPADKKIFMNRCDPLsETQQWIFEHTNM 141

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a 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 may contain a potential sugar-binding pocket.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903375 239 SGKLHNTGLGLCADCQAEGNVLDCPMVLAPCSDSRQQQYLQHTSRKEIHFGRpqhLCFAV------RQEQVILQNCTEEG 312
Cdd:cd23418     5 GGQIRGYGSGRCLDVPGGSTTNGTRLILWDCHGGANQQFTFTSAGELRVGGD---KCLDAagggttNGTPVVIWPCNGGA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622903375 313 LaihqQRWDFQENGMIVHILSGKCMEAVVQES--NKDLYLRPCDGKARQQWRF 363
Cdd:cd23418    82 N----QKWRFNSDGTIRNVNSGLCLDVAGGGTanGTRLILWSCNGGSNQRWRR 130

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622903375 302 QVILQNCTEEGlaihQQRWDFQENG----MIVHILSGKCMEAV--VQESNKDLYLRPCDGKARQQWRFDQV 366
Cdd:cd00161    26 PVQQWTCNGGA----NQQWTLTPVGdgyyTIRNVASGKCLDVAggSTANGANVQQWTCNGGDNQQWRLEPV 92

second ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and similar proteins; This subfamily includes Sambucus ebulus ebulin I and Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf. Ebulin l is a type II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus. It is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. It is considered a nontoxic type II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type II RIP like ricin. Ebulin l binds an A-chain substrate analogue, pteroic acid. It binds bind galactose and lactose in subdomain 1alpha in a similar manner to that of ricin. In contrast, it binds only the monosaccharide galactose, and not the disaccharide lactose in subdomain 2gamma. SNAV is a non-toxic GalNAc-specific type II RIP which strongly inhibits mammalian protein synthesis but does not affect plant nor bacterial protein synthesis. SNAI is Neu5Ac(alpha2-6)Gal/GalNAc specific agglutinin. It also acts as a type II RIP that strongly inhibits mammalian but not plant ribosomes. SNAI' is another NeuAc(alpha2,6)Gal/GalNAc binding type II RIP from elderberry (Sambucus nigra) bark. It is a minor bark protein which closely resembles the major Neu5Ac(alpha2,6)Gal/GalNAc binding type II RIP, SNAI, with respect to its carbohydrate-binding specificity and ribosome-inactivating activity but has a different molecular structure due to a single cysteine residue present in the B chain of SNAI but absent from SNAI'. SNAIf is fruit specific SNAI. It functions as fetuin-binding fruit lectin. Like Ebulin l, SNAV, SNAI, SNAI' and SNAIf consist of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain. It may also be responsible for cell agglutination (lectin activity). The B chain contains 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 model corresponds to the second ricin B-type lectin domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903375 256 EGNVLDCPMVLAPCSDSRQQQYLQHTSRKEIHFGRPQHLCFA----VRQEQVILQNCteEGLAihQQRWDFQENGMIVHI 331
Cdd:cd23490    15 QANGENNGVWMEDCVVTSVQQQWALYGDGTIRVNSDRSLCVTsngyNSKDLIIILKC--QGLP--NQRWVFNTDGTIVNP 90

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622903375 332 LSGKCMEavVQESNKDL---YLRPCDGKARQQWRFD 364
Cdd:cd23490    91 NSKLVMD--VKQSDVSLreiILFPPTGNPNQQWITQ 124

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622903375 302 QVILQNCTEEGlaihQQRWDFQENGMIVHILSGKCMEAvvQESNK----DLYLRPCDGKARQQWR 362
Cdd:cd23451    67 LVQLWDCNGTG----AQKWVPRADGTLYNPQSGKCLDA--PGGSTtdgtQLQLYTCNGTAAQQWT 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
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622903375 318 QRWDF----QENGMIVHILSGKCMEAvvqESNKDLYLRPCDGKARQQWRF 363
Cdd:cd23415    33 QRWTWsgvgDGTVTLRNAATGRCLDS---NGNGGVYTLPCNGGSYQRWRV 79

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 17 (GALNT17) and similar proteins; GALNT17 (EC 2.4.1.41), also called polypeptide GalNAc transferase-like protein 3, GalNAc-T-like protein 3, pp-GaNTase-like protein 3, protein-UDP acetylgalactosaminyltransferase-like protein 3, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3, or Williams-Beuren syndrome chromosomal region 17 protein, may catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT17 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622903375 315 IHQQRWDFQENGMIVHILSGKCMEaVVQESNK--DLYLRPCDGkarQQW 361
Cdd:cd23474    91 ILHKRWNFIQNGAIMNLGTGRCLE-VENRGNFgiDLILRSCTG---QRW 135

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
                  ....*....|....*....|....*....|....*....|
gi 1622903375   2 LGATRATGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVV 41
Cdd:cd00761    71 AGLKAARGEYILFLDADDLLLPDWLERLVAELLADPEADA 110

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                          10        20        30
                  ....*....|....*....|....*....|
gi 1622903375   2 LGATRATGDVLVFMDAHCECHPGWLEPLLS 31
Cdd:COG1216    75 LGLRAAGGDYLLFLDDDTVVEPDWLERLLA 104

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts 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
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622903375 316 HQQRWDFQENG----MIVHILSGKCMEaVVQESNKD---LYLRPCDGKARQQWRF 363
Cdd:cd23458    36 SNQQWTLVEIDngyyRIKASHSGKCLD-VAGGSTANganIQQWDCVGGANQQWKL 89

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8)-like subfamily; The GALNT8-like subfamily includes GALNT8, GALNT9, GALNT17 and GALNT18. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT9 does not glycosylate apomucin or SDC3. Members of this family comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622903375 317 QQRWDFQENGMIVHILSGKCMEavVQESNKD----LYLRPCDGkarQQWRF 363
Cdd:cd23438    87 QKYWDFSQGGAIQNRATGRCLE--VEEDKLNfghrLVLQTCSG---QKWNI 132

Ricin-type beta-trefoil lectin domain-like;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622903375 318 QRWDFQENG-----MIVHILSGKCMEaVVQESNKD---LYLRPCDGKARQQWRFDQV 366
Cdd:pfam14200   3 QQWRFGGTVgdgyyTIVNVASGKYLD-VAGGSTANganVQQWTDNGNDNQQWRIVDA 58