ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 5 (GALNT5) and similar proteins; GALNT5 (EC 2.4.1.41), also called polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, protein-UDP acetylgalactosaminyltransferase 5, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, 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. GALNT5 has activity toward EA2 peptide substrate but has a weak activity toward Muc2 or Muc1b substrates. GALNT5 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 1034611243 806 PIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHK 885
Cdd:cd23436     1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034611243 886 STSVFhPELlsnsacgsfpallslqVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYY 954
Cdd:cd23436    81 SLIAF-PEL----------------MDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 5 (GALNT5) and similar proteins; GALNT5 (EC 2.4.1.41), also called polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, protein-UDP acetylgalactosaminyltransferase 5, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, 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. GALNT5 has activity toward EA2 peptide substrate but has a weak activity toward Muc2 or Muc1b substrates. GALNT5 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 1034611243 806 PIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHK 885
Cdd:cd23436     1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034611243 886 STSVFhPELlsnsacgsfpallslqVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYY 954
Cdd:cd23436    81 SLIAF-PEL----------------MDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034611243 496 PTTSVIMCFVDEvWSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYmsQFPKVRILRLKERHGLIRARLAG 575
Cdd:COG1216     3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGST-DGTAELLAAL--AFPRVRVIRNPENLGFAAARNLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034611243 576 AQNATGDVLTFLDSHVECNVGWLEPLLErvylsrkkVACpvievindkdmsymtvdnfqrgifvwpmnfgwrtippdvia 655
Cdd:COG1216    77 LRAAGGDYLLFLDDDTVVEPDWLERLLA--------AAC----------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034611243 656 knriketdtircpvmagglFSIDKSYFFELGTYDPGLDVWGGEnMELSFKVWMCGGEIEIIPCSRVGHIFRNDnpySFPK 735
Cdd:COG1216   108 -------------------LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGAS---SGPL 164

                         250
                  ....*....|....*....
gi 1034611243 736 DRMKTVERNLVRVAEVWLD 754
Cdd:COG1216   165 LRAYYLGRNRLLFLRKHGP 183

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034611243  815 INVALGKCISI--ENTTVILEDCDGSKELQQFNYTWLRLIKC--GEWCIAPIPDKGA-VRLHPCDNRNKGLKWLHKSTSv 889
Cdd:smart00458   2 ISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGStVTLYSCDGTNDNQYWEVNKDG- 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034611243  890 fhpeLLSNSACGsfpalLSLQVNhivfennqqllclEGNFSQKILkVAACDPvKPYQKWKFE 951
Cdd:smart00458  81 ----TIRNPDSG-----KCLDVK-------------DGNTGTKVI-LWTCSG-NPNQKWIFE 118

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 5 (GALNT5) and similar proteins; GALNT5 (EC 2.4.1.41), also called polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, protein-UDP acetylgalactosaminyltransferase 5, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, 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. GALNT5 has activity toward EA2 peptide substrate but has a weak activity toward Muc2 or Muc1b substrates. GALNT5 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 1034611243 806 PIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHK 885
Cdd:cd23436     1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034611243 886 STSVFhPELlsnsacgsfpallslqVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYY 954
Cdd:cd23436    81 SLIAF-PEL----------------MDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034611243 496 PTTSVIMCFVDEvWSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYmsQFPKVRILRLKERHGLIRARLAG 575
Cdd:COG1216     3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGST-DGTAELLAAL--AFPRVRVIRNPENLGFAAARNLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034611243 576 AQNATGDVLTFLDSHVECNVGWLEPLLErvylsrkkVACpvievindkdmsymtvdnfqrgifvwpmnfgwrtippdvia 655
Cdd:COG1216    77 LRAAGGDYLLFLDDDTVVEPDWLERLLA--------AAC----------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034611243 656 knriketdtircpvmagglFSIDKSYFFELGTYDPGLDVWGGEnMELSFKVWMCGGEIEIIPCSRVGHIFRNDnpySFPK 735
Cdd:COG1216   108 -------------------LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGAS---SGPL 164

                         250
                  ....*....|....*....
gi 1034611243 736 DRMKTVERNLVRVAEVWLD 754
Cdd:COG1216   165 LRAYYLGRNRLLFLRKHGP 183

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034611243 496 PTTSVIMCFVDEvWSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAG 575
Cdd:COG0463     2 PLVSVVIPTYNE-EEYLEEALESLLAQTYPDF--EIIVVDDGST-DGTAEILRELAAKDPRIRVIRLERNRGKGAARNAG 77

                          90       100
                  ....*....|....*....|....*....
gi 1034611243 576 AQNATGDVLTFLDSHVECNVGWLEPLLER 604
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAA 106

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 1034611243 500 VIMCFVDEVwSTLLRSVHSVINRSPPHLikEILLVDDFSTKDYLKDnLDKYMSQFPKVRILRLKERHGLIRARLAGAQNA 579
Cdd:cd00761     1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTLEI-LEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034611243 580 TGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVAC 614
Cdd:cd00761    77 RGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111

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 1034611243 808 VRASGVLINVALGKCI----SIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGlKWL 883
Cdd:cd23437     2 NLAWGEIRNLGTGLCLdtmgHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETG-KWE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034611243 884 HKSTSvfhpELLSNSACGsfpallslqvnhivfennqqlLCLEGNFSQKILKVAACDPVKPYQKWKF 950
Cdd:cd23437    81 YDEAT----GQIRHKGTG---------------------KCLDLNEGTNKLILQPCDSSSPSQKWEF 122

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 1034611243 810 ASGVLINVALGKCIS------IENTTVILEDCDGSKELQQFNYTWLRLIKCGEWC--IAPIPDKgaVRLHPCDNRNKGLK 881
Cdd:cd23462     4 AYGEIRNLAGKLCLDapgrkkELNKPVGLYPCHGQGGNQYWMLTKDGEIRRDDLCldYAGGSGD--VTLYPCHGMKGNQF 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034611243 882 WLHKSTSvfhpellsnsacgsfpallslqvNHIVFENNQqlLCLEGNFSQKILKVAACDPVKPYQKWKFE 951
Cdd:cd23462    82 WIYDEET-----------------------KQIVHGTSK--KCLELSDDSSKLVMEPCNGSSPRQQWEFE 126

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 1034611243 512 LLRSVHSVINRSPPHlikEILLVDDFSTkdylkDN----LDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFL 587
Cdd:cd04179    15 LVERLLAVLEEGYDY---EIIVVDDGST-----DGtaeiARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARGDIVVTM 86

                  ..
gi 1034611243 588 DS 589
Cdd:cd04179    87 DA 88

putative glycosyl transferase; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034611243 530 EILLVDDFSTkDYLKDNLDKYMSQFPKVRILRlKERHGLIRARLAGAQNATGDVLTFLD 588
Cdd:PRK10073   37 EIIIVNDGST-DNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAVATGKYVAFPD 93

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 1034611243 812 GVLINVALGKCISI---ENT--TVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKgAVRLHPCDNRNKGLKWLHKS 886
Cdd:cd23460     3 GQIKHTESGLCLDWageSNGdkTVALKPCHGGGGNQFWMYTGDGQIRQDHLCLTADEGN-KVTLRECADQLPSQEWSYDE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034611243 887 tsvfhpellsnsacgsfpallslQVNHIVfeNNQQLLCLEGNFSQKILKVAACDPVKPYQKWKF 950
Cdd:cd23460    82 -----------------------KTGTIR--HRSTGLCLTLDANNDVVILKECDSNSLWQKWIF 120

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 1034611243 806 PIVRASGVLINVALGKCISIEN----TTVILEDC--DGSKEL----QQFNYTWLRLIKCGE------WCIAPIPDKGAVR 869
Cdd:cd23477     2 PPPAAWGEIRNVAANLCVDSKHgatgTELRLDICvkDGSERTwsheQLFTFGWREDIRPGEplhtrkFCFDAISHNSPVT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034611243 870 LHPCDNRNKGLKWLH-KSTSVFHPelLSNSacgsfpallslqvnhivfennqqllCLEGNFSQKILKVAACDPVKPYQKW 948
Cdd:cd23477    82 LYDCHGMKGNQLWSYrKDKTLFHP--VSNS-------------------------CMDCNPADKKIFMNRCDPLSETQQW 134

                  ....
gi 1034611243 949 KFEK 952
Cdd:cd23477   135 IFEH 138

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 1034611243 814 LINVALGKCISIENTT--VILEDCDGSKELQQFNYTW---LRLIKCGEwCIA--PIPDKGAVRLHPCDNRNKGLKW 882
Cdd:cd23385     5 IYNEDLGKCLAARSSSskVSLSTCNPNSPNQQWKWTSghrLFNVGTGK-CLGvsSSSPSSPLRLFECDSEDELQKW 79

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 1034611243 509 WSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKymsQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD 588
Cdd:cd04186     9 LEYLKACLDSLLAQTYPDF--EVIVVDNAST-DGSVELLRE---LFPEVRLIRNGENLGFGAGNNQGIREAKGDYVLLLN 82

                          90       100
                  ....*....|....*....|....*.
gi 1034611243 589 SHVECNVGWLEPLLERvYLSRKKVAC 614
Cdd:cd04186    83 PDTVVEPGALLELLDA-AEQDPDVGI 107

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 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. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034611243 824 SIENTTVILEDCDGSKELQQFNYT----WLRLIKCGeWCIAPIPDK-GAVRLHPCDNRNKGLKW 882
Cdd:cd23434    57 RAPGSLVTLQPCREDDSNQKWEQIennsKLRHVGSN-LCLDSRNAKsGGLTVETCDPSSGSQQW 119