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
                 ....*....|....*....|....*....|....*....|....
gi 767948450 457 MRRYNNTVAYGELRNNKAKDVCLDQGPLENHTAILYPCHGWGPQ 500
Cdd:cd23474    1 MRRYNNTVAYGELRNNKAKDVCLDQGPPENHTAILYPCHGWGPQ 44

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 767948450 457 MRRYNNTVAYGELRNNKAKDVCLDQGPLENHTAILYPCHGWGPQ 500
Cdd:cd23474    1 MRRYNNTVAYGELRNNKAKDVCLDQGPPENHTAILYPCHGWGPQ 44

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948450 152 PQISIIFIFVNEAlSVILRSVHSAVNHTPTHLlkEIILVDDNSDEEELkvpleEYVHKRYPGLVKVVRNQKREGLIRARI 231
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTA-----ELLAALAFPRVRVIRNPENLGFAAARN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948450 232 EGWKVATGQVTGFFDAHVEFTAGWAEPVLsriqenrkrvilpsidnikqdnfevqryensahgyswELWCMYISppkdww 311
Cdd:COG1216   75 LGLRAAGGDYLLFLDDDTVVEPDWLERLL-------------------------------------AAACLLIR------ 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948450 312 dagdpslpirtpamigcsfvvnRKFFGEIGLLDPGMDVYGGEnIELGIKVWLCGGSMEVLPCSRVAHIERKKKPYNSNIg 391
Cdd:COG1216  112 ----------------------REVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRA- 167

                        250
                 ....*....|....*.
gi 767948450 392 FYTKRNALRVAEVWMD 407
Cdd:COG1216  168 YYLGRNRLLFLRKHGP 183

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 767948450 457 MRRYNNTVAYGELRNNKAKDVCLDQGPLENHTAILYPCHGWGPQ 500
Cdd:cd23474    1 MRRYNNTVAYGELRNNKAKDVCLDQGPPENHTAILYPCHGWGPQ 44

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
                 ....*....|....*....|....*....|....*....
gi 767948450 462 NTVAYGELRNNKAKDVCLDQGPLENHTAILYPCHGWGPQ 500
Cdd:cd23438    1 NTVAYGEMRNSLVTDLCLDQGPKENHTAILYPCHGWSPQ 39

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948450 152 PQISIIFIFVNEAlSVILRSVHSAVNHTPTHLlkEIILVDDNSDEEELkvpleEYVHKRYPGLVKVVRNQKREGLIRARI 231
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTA-----ELLAALAFPRVRVIRNPENLGFAAARN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948450 232 EGWKVATGQVTGFFDAHVEFTAGWAEPVLsriqenrkrvilpsidnikqdnfevqryensahgyswELWCMYISppkdww 311
Cdd:COG1216   75 LGLRAAGGDYLLFLDDDTVVEPDWLERLL-------------------------------------AAACLLIR------ 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948450 312 dagdpslpirtpamigcsfvvnRKFFGEIGLLDPGMDVYGGEnIELGIKVWLCGGSMEVLPCSRVAHIERKKKPYNSNIg 391
Cdd:COG1216  112 ----------------------REVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRA- 167

                        250
                 ....*....|....*.
gi 767948450 392 FYTKRNALRVAEVWMD 407
Cdd:COG1216  168 YYLGRNRLLFLRKHGP 183

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 767948450 156 IIFIFVNEAlSVILRSVHSAVNHTPTHLlkEIILVDDNSDEEELKVpLEEYVHKRYPglVKVVRNQKREGLIRARIEGWK 235
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTLEI-LEEYAKKDPR--VIRVINEENQGLAAARNAGLK 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767948450 236 VATGQVTGFFDAHVEFTAGWAEPVLSRIQENRKRVI 271
Cdd:cd00761   75 AARGEYILFLDADDLLLPDWLERLVAELLADPEADA 110

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 18 (GALNT18) and similar proteins; GALNT18 (EC 2.4.1.41), also called polypeptide GalNAc transferase 18, GalNAc-T18, polypeptide GalNAc transferase-like protein 4, GalNAc-T-like protein 4, pp-GaNTase-like protein 4, polypeptide N-acetylgalactosaminyltransferase-like protein 4, protein-UDP acetylgalactosaminyltransferase-like protein 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. GALNT18 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 767948450 457 MRRYNNTVAYGELRNNKAKDVCLDQGPLENHTAILYPCHGWGPQ 500
Cdd:cd23475    1 MRMYTDTIAYGVLQNSLKTDLCLDQGPDTDNIPIMYICHGMTPQ 44

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 767948450 162 NEA--LSVILRSVHSAVNHTPTHllkEIILVDDNSDEEELKVpLEEYvHKRYPGlVKVVRNQKREGLIRARIEGWKVATG 239
Cdd:cd04179    7 NEEenIPELVERLLAVLEEGYDY---EIIVVDDGSTDGTAEI-AREL-AARVPR-VRVIRLSRNFGKGAAVRAGFKAARG 80

                 ....*...
gi 767948450 240 QVTGFFDA 247
Cdd:cd04179   81 DIVVTMDA 88

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948450 159 IFVN-EALSVILRSVHSAVNHTPTHLlkEIILVDDNSDEEELkvpleEYVHKRYPGlVKVVRNQKREGLIRARIEGWKVA 237
Cdd:cd04186    2 IIVNyNSLEYLKACLDSLLAQTYPDF--EVIVVDNASTDGSV-----ELLRELFPE-VRLIRNGENLGFGAGNNQGIREA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948450 238 TGQVTGFFDAHVEFTAGWAEPVLSRIQENRkrvilpsidnikqdnfevqryensahgyswelwcmyisppkdwwDAGdps 317
Cdd:cd04186   74 KGDYVLLLNPDTVVEPGALLELLDAAEQDP--------------------------------------------DVG--- 106

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948450 318 lpIRTPAMIGCSFVVNRKFFGEIGLLDPGMDVYgGENIELGIKVWLCGGSMEVLPCSRVAHIE 380
Cdd:cd04186  107 --IVGPKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYHHG 166

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948450 162 NEAlSVILRSVHSAVNHTptHLLKEIILVDDNSDEEELKVPLEEYVhkRYPGLVKVVRNQKREGLIRARIEGWKVATGQV 241
Cdd:cd06423    7 NEE-AVIERTIESLLALD--YPKLEVIVVDDGSTDDTLEILEELAA--LYIRRVLVVRDKENGGKAGALNAGLRHAKGDI 81

                 ....*.
gi 767948450 242 TGFFDA 247
Cdd:cd06423   82 VVVLDA 87

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948450 152 PQISIIFIFVNEALSVILRSVHSAVNHTPTHLlkEIILVDDNSDEEELKVPLEEYV--HKRypglVKVVRNQKREGLIRA 229
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYAaqDPR----IKVVFREENGGISAA 74

                         90
                 ....*....|....*..
gi 767948450 230 RIEGWKVATGQVTGFFD 246
Cdd:cd04184   75 TNSALELATGEFVALLD 91

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
                 ....*....|....*....|....*....|....*...
gi 767948450 464 VAYGELRNnKAKDVCLDQGPLENHTA---ILYPCHGWG 498
Cdd:cd23435    2 GYYGALRN-KGSELCLDVNNPNGQGGkpvIMYGCHGLG 38