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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971399571 434 PEKDLIPGIIRQGGNCLESWAQDTTGNTLAGIGNCKGTVNNPPVT----------------------------------- 478
Cdd:cd23479    1 PEKEAIPGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASqewvlsdplirqqdkclaitsfspgskvilelcnq 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 971399571 479 ----QKWKMKGSFIQHFVSGLCLENQTGKVVTNPCQADVPGQQWELLQA 523
Cdd:cd23479   81 kdgrQKWKLKGSFIQHQVSGLCLDSQSGRVVINQCQADLASQQWELLQV 129

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 971399571 434 PEKDLIPGIIRQGGNCLESWAQDTTGNTLAGIGNCKGTVNNPPVT----------------------------------- 478
Cdd:cd23479    1 PEKEAIPGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASqewvlsdplirqqdkclaitsfspgskvilelcnq 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 971399571 479 ----QKWKMKGSFIQHFVSGLCLENQTGKVVTNPCQADVPGQQWELLQA 523
Cdd:cd23479   81 kdgrQKWKLKGSFIQHQVSGLCLDSQSGRVVINQCQADLASQQWELLQV 129

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971399571 134 SLIITFHNEARSaLLRTVKSVLNRTPPNLiqEIILVDDFSSD--PEDCQ-LLTRIPKVKCLRNIRREGLIRSRVRGAEAA 210
Cdd:COG0463    5 SVVIPTYNEEEY-LEEALESLLAQTYPDF--EIIVVDDGSTDgtAEILReLAAKDPRIRVIRLERNRGKGAARNAGLAAA 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 971399571 211 TADILTFLDSHCEVNSEWLQPMLQRVKEDYTRVV 244
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115

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 971399571 434 PEKDLIPGIIRQGGNCLESWAQDTTGNTLAGIGNCKGTVNNPPVT----------------------------------- 478
Cdd:cd23479    1 PEKEAIPGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASqewvlsdplirqqdkclaitsfspgskvilelcnq 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 971399571 479 ----QKWKMKGSFIQHFVSGLCLENQTGKVVTNPCQADVPGQQWELLQA 523
Cdd:cd23479   81 kdgrQKWKLKGSFIQHQVSGLCLDSQSGRVVINQCQADLASQQWELLQV 129

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971399571 134 SLIITFHNEARSaLLRTVKSVLNRTPPNLiqEIILVDDFSSD--PEDCQ-LLTRIPKVKCLRNIRREGLIRSRVRGAEAA 210
Cdd:COG0463    5 SVVIPTYNEEEY-LEEALESLLAQTYPDF--EIIVVDDGSTDgtAEILReLAAKDPRIRVIRLERNRGKGAARNAGLAAA 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 971399571 211 TADILTFLDSHCEVNSEWLQPMLQRVKEDYTRVV 244
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971399571 131 PATSLIITFHNEArSALLRTVKSVLNRTPPNLiqEIILVDDFSSDPEDCQLLT-RIPKVKCLRNIRREGLIRSRVRGAEA 209
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTAELLAAlAFPRVRVIRNPENLGFAAARNLGLRA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971399571 210 ATADILTFLDSHCEVNSEWLQPMlqrvkedytrvvspiidvisldnfayLAASAdlrggfdwslhfkweqipieqkmsrt 289
Cdd:COG1216   80 AGGDYLLFLDDDTVVEPDWLERL--------------------------LAAAC-------------------------- 107

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971399571 290 dptqsirtpviaggiFVINKSWFNHLGKYDTQMDIWGGEnFELSFRVWMCGGSLEIVPCSRVGHVFRKRH 359
Cdd:COG1216  108 ---------------LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASS 161

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 971399571 125 RYDTDLPATSLIITFHNEARSaLLRTVKSVLNRTPPNLIQEIILVDDFSSDP--EDC-QLLTRIPKVKCLRNIRREGLIR 201
Cdd:COG1215   23 RAPADLPRVSVIIPAYNEEAV-IEETLRSLLAQDYPKEKLEVIVVDDGSTDEtaEIArELAAEYPRVRVIERPENGGKAA 101

                         90       100       110
                 ....*....|....*....|....*....|....
gi 971399571 202 SRVRGAEAATADILTFLDSHCEVNSEWLQPMLQR 235
Cdd:COG1215  102 ALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAA 135

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971399571 134 SLIITFHNEARSaLLRTVKSVLNRTPPNLIQEIILVDDFSSD--PEDCQLLT-RIPKVKCLRNIRReglIRS--RVRGAE 208
Cdd:cd02525    3 SIIIPVRNEEKY-IEELLESLLNQSYPKDLIEIIVVDGGSTDgtREIVQEYAaKDPRIRLIDNPKR---IQSagLNIGIR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971399571 209 AATADILTFLDSHCEVNSEWLQPMLQRVKEDYTRVVSPIIDVISLDNF----AYLAASADLRGGfdwSLHfkweqipieq 284
Cdd:cd02525   79 NSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFqkaiAVAQSSPLGSGG---SAY---------- 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971399571 285 kmsRTDPTQSIRTPVIAGGIFviNKSWFNHLGKYDTQMDIwgGENFELSFRVWMCGGSLEIVPCSRVGHVFR 356
Cdd:cd02525  146 ---RGGAVKIGYVDTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPR 210

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971399571  441 GIIRQGGN--CLEswAQDTTGNTLAGIGNCKGTVNNppvtQKW--KMKGSFIQHFVSGLCLE-----NQTGKVVTNPCQA 511
Cdd:pfam00652  46 GTIRSVASdlCLD--VGSTADGAKVVLWPCHPGNGN----QRWryDEDGTQIRNPQSGKCLDvsgagTSNGKVILWTCDS 119

                  ....*..
gi 971399571  512 DVPGQQW 518
Cdd:pfam00652 120 GNPNQQW 126

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 971399571 441 GIIRQGGNCLESWaqdTTGNTLaGIGNCKGTVnnppvTQKWK--MKGSFIQHFVSGLCLE--NQTGKVVTNPCQADVPGQ 516
Cdd:cd23437   48 GQLAVGEQCLTAS---GSGGKV-KLRKCNLGE-----TGKWEydEATGQIRHKGTGKCLDlnEGTNKLILQPCDSSSPSQ 118

                 ...
gi 971399571 517 QWE 519
Cdd:cd23437  119 KWE 121

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 971399571 135 LIITFHNEARSaLLRTVKSVLNRTPPNLIQEIILVDDFSSD--PEDCQLLT-RIPKVKCLRNIRREGLIRSRVRGAEAAT 211
Cdd:cd04179    1 VVIPAYNEEEN-IPELVERLLAVLEEGYDYEIIVVDDGSTDgtAEIARELAaRVPRVRVIRLSRNFGKGAAVRAGFKAAR 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 971399571 212 ADILTFLDSHCEVNSEWLQPMLQRVKEDYTRVV 244
Cdd:cd04179   80 GDIVVTMDADLQHPPEDIPKLLEKLLEGGADVV 112

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971399571 449 CLEswaqdTTGNTLAGIGNCKGTVNNPPVTQKWKMK-GSFIQHFVSGLCLENQTGKVVTNPCQADVPGQQW 518
Cdd:cd23435   60 CLH-----ASGSDEVILQHCTSKGKDVPPEQKWLFTqDGTIRNPASGLCLHASGYKVLLRTCNPSDDSQKW 125

N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971399571  300 IAGGIFVINKSWFNHLGKYDTQMDIWGGENFELSFRVWMCGGSLEIVPCsRVGHVFRKRHP 360
Cdd:pfam02709  19 YFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG-DIGRYYMLYHK 78

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 971399571 433 VPEKDLI-PGIIRQGGNCLESWAQDTTGNTLAGIGNCKGTVNNP------------------------------PVT--- 478
Cdd:cd23478    1 IPDESDIqSGVIRQRQNCLESRRVEGQELPNLSLSPCIKSKGVPaksqewaytynqqirqqqlclsvhtlfpgsPVVlvp 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 971399571 479 -------QKWKMKGSFIQHFVSGLCLE-------NQTGK-VVTNPCQADVPGQQWEL 520
Cdd:cd23478   81 ckegdgkQRWTKVGSHIEHMASRFCLDtemfgdgTESSKeIVINPCESSAMSQRWDM 137

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. 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 of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971399571 127 DTDLPATSLIITFHNEARsALLRTVKSVLNRTPPNLIQEIILVDDFSSDPEDcQLLTRIP--KVKCLRNIRREGLIRSRV 204
Cdd:cd06439   25 PAYLPTVTIIIPAYNEEA-VIEAKLENLLALDYPRDRLEIIVVSDGSTDGTA-EIAREYAdkGVKLLRFPERRGKAAALN 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 971399571 205 RGAEAATADILTFLDshceVNSEWLQPMLQRVKEDYTrvvSPIIDVIS 252
Cdd:cd06439  103 RALALATGEIVVFTD----ANALLDPDALRLLVRHFA---DPSVGAVS 143

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
                 ....*....|....*....|....*....|....*....|....*..
gi 971399571 478 TQKWK--MKGSFIQHFVSGLCLE--NQTGKVVTNPCQADVPGQQWEL 520
Cdd:cd23462   79 NQFWIydEETKQIVHGTSKKCLElsDDSSKLVMEPCNGSSPRQQWEF 125

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 971399571 131 PATSLIITFHNEARSALLRTVKSVLNRTPPNLiqEIILVDDFSSDPEDCQLLTRI----PKVKCLRNIRREGLIRSRVRG 206
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYaaqdPRIKVVFREENGGISAATNSA 78

                         90
                 ....*....|....
gi 971399571 207 AEAATADILTFLDS 220
Cdd:cd04184   79 LELATGEFVALLDH 92

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; 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. This protein family belongs to Glycosyltransferase 2 superfamily.

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gi 971399571 165 EIILVDDFSSD--PEDCQLLTRI-PKVKCLRNIRREGLIRSRVRGAEAATADILTFLD---SH 221
Cdd:cd06442   29 EIIVVDDNSPDgtAEIVRELAKEyPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDadlSH 91