pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 499 SVIMCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTKDYLKDNLD-KYMSQFPKVRILRLKERHGLIRARLAGAQ 577
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEeYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 578 NATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDViaKN 657
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 658 RIKETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND-NPYSFPKD 736
Cdd:cd02510 159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFPGG 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32698686 737 rMKTVERNLVRVAEVWLDEYKELFYGHGDHLidQGLDVGNLTQQRELRKKLKCKSFKWYLENVF 800
Cdd:cd02510 239 -SGTVLRNYKRVAEVWMDEYKEYFYKARPEL--RNIDYGDLSERKALRERLKCKSFKWYLENVY 299

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 499 SVIMCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTKDYLKDNLD-KYMSQFPKVRILRLKERHGLIRARLAGAQ 577
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEeYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 578 NATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDViaKN 657
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 658 RIKETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND-NPYSFPKD 736
Cdd:cd02510 159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFPGG 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32698686 737 rMKTVERNLVRVAEVWLDEYKELFYGHGDHLidQGLDVGNLTQQRELRKKLKCKSFKWYLENVF 800
Cdd:cd02510 239 -SGTVLRNYKRVAEVWMDEYKEYFYKARPEL--RNIDYGDLSERKALRERLKCKSFKWYLENVY 299

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 32698686   499 SVIMCFVDEvWSTLLRSVHSVINRspPHLIKEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQN 578
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQ--TYPNFEIIVVDDGST-DGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686   579 ATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYmtvdnfqrgifvWPMNFGWRTIPPDVIAKNR 658
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY------------RRASRITLSRLPFFLGLRL 144

                         170       180
                  ....*....|....*....|.
gi 32698686   659 IKETDTIRCPVMAGGLFSIDK 679
Cdd:pfam00535 145 LGLNLPFLIGGFALYRREALE 165

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 496 PTTSVIMCFVDEvWSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYmsQFPKVRILRLKERHGLIRARLAG 575
Cdd:COG1216   3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGST-DGTAELLAAL--AFPRVRVIRNPENLGFAAARNLG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 576 AQNATGDVLTFLDSHVECNVGWLEPLLErvylsrkkVACpvievindkdmsymtvdnfqrgifvwpmnfgwrtippdvia 655
Cdd:COG1216  77 LRAAGGDYLLFLDDDTVVEPDWLERLLA--------AAC----------------------------------------- 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 656 knriketdtircpvmagglFSIDKSYFFELGTYDPGLDVWGGEnMELSFKVWMCGGEIEIIPCSRVGHIFRNDnpySFPK 735
Cdd:COG1216 108 -------------------LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGAS---SGPL 164

                       250
                ....*....|....*....
gi 32698686 736 DRMKTVERNLVRVAEVWLD 754
Cdd:COG1216 165 LRAYYLGRNRLLFLRKHGP 183

putative glycosyl transferase; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32698686  530 EILLVDDFSTkDYLKDNLDKYMSQFPKVRILRlKERHGLIRARLAGAQNATGDVLTFLD 588
Cdd:PRK10073  37 EIIIVNDGST-DNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAVATGKYVAFPD 93

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 499 SVIMCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTKDYLKDNLD-KYMSQFPKVRILRLKERHGLIRARLAGAQ 577
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEeYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 578 NATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDViaKN 657
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 658 RIKETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND-NPYSFPKD 736
Cdd:cd02510 159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFPGG 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32698686 737 rMKTVERNLVRVAEVWLDEYKELFYGHGDHLidQGLDVGNLTQQRELRKKLKCKSFKWYLENVF 800
Cdd:cd02510 239 -SGTVLRNYKRVAEVWMDEYKEYFYKARPEL--RNIDYGDLSERKALRERLKCKSFKWYLENVY 299

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 32698686   499 SVIMCFVDEvWSTLLRSVHSVINRspPHLIKEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQN 578
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQ--TYPNFEIIVVDDGST-DGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686   579 ATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYmtvdnfqrgifvWPMNFGWRTIPPDVIAKNR 658
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY------------RRASRITLSRLPFFLGLRL 144

                         170       180
                  ....*....|....*....|.
gi 32698686   659 IKETDTIRCPVMAGGLFSIDK 679
Cdd:pfam00535 145 LGLNLPFLIGGFALYRREALE 165

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 496 PTTSVIMCFVDEvWSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYmsQFPKVRILRLKERHGLIRARLAG 575
Cdd:COG1216   3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGST-DGTAELLAAL--AFPRVRVIRNPENLGFAAARNLG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 576 AQNATGDVLTFLDSHVECNVGWLEPLLErvylsrkkVACpvievindkdmsymtvdnfqrgifvwpmnfgwrtippdvia 655
Cdd:COG1216  77 LRAAGGDYLLFLDDDTVVEPDWLERLLA--------AAC----------------------------------------- 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 656 knriketdtircpvmagglFSIDKSYFFELGTYDPGLDVWGGEnMELSFKVWMCGGEIEIIPCSRVGHIFRNDnpySFPK 735
Cdd:COG1216 108 -------------------LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGAS---SGPL 164

                       250
                ....*....|....*....
gi 32698686 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 32698686 496 PTTSVIMCFVDEvWSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAG 575
Cdd:COG0463   2 PLVSVVIPTYNE-EEYLEEALESLLAQTYPDF--EIIVVDDGST-DGTAEILRELAAKDPRIRVIRLERNRGKGAARNAG 77

                        90       100
                ....*....|....*....|....*....
gi 32698686 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 32698686 500 VIMCFVDEVwSTLLRSVHSVINRSPPHLikEILLVDDFSTKDYLKDnLDKYMSQFPKVRILRLKERHGLIRARLAGAQNA 579
Cdd:cd00761   1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTLEI-LEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 32698686 580 TGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVAC 614
Cdd:cd00761  77 RGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111

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 32698686 810 ASGVLINVALGKCIS------IENTTVILEDCDGSKELQQFNYTWLRLIKCGEWC--IAPIPDKgaVRLHPCDNRNKGLK 881
Cdd:cd23462   4 AYGEIRNLAGKLCLDapgrkkELNKPVGLYPCHGQGGNQYWMLTKDGEIRRDDLCldYAGGSGD--VTLYPCHGMKGNQF 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 32698686 882 WLHKSTSvfhpelvNHIVFENNQqlLCLEGNFSQKILKVAACDPVKPYQKWKFE 935
Cdd:cd23462  82 WIYDEET-------KQIVHGTSK--KCLELSDDSSKLVMEPCNGSSPRQQWEFE 126

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 32698686 496 PTTSVIM--CFVDEVWstLLRSVHSVINRSPPHLikEILLVDDFSTKDYLKDNLDKYMSQFPKVRILRLKERHGLIRARL 573
Cdd:cd04184   1 PLISIVMpvYNTPEKY--LREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATN 76

                        90
                ....*....|....*.
gi 32698686 574 AGAQNATGDVLTFLDS 589
Cdd:cd04184  77 SALELATGEFVALLDH 92

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        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 820 GKCI----SIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPI-PDKGA-VRLHPCDNRNKGLKWLHkstsvfhpe 893
Cdd:cd23434   9 NLCLdtlgHKAGGTVGLYPCHGTGGNQEWSFTKDGQIKHDDLCLTVVdRAPGSlVTLQPCREDDSNQKWEQ--------- 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32698686 894 lvnhivFENNQQL------LCLEG-NFSQKILKVAACDPVKPYQKWKF 934
Cdd:cd23434  80 ------IENNSKLrhvgsnLCLDSrNAKSGGLTVETCDPSSGSQQWKF 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 32698686 512 LLRSVHSVINRSPPHlikEILLVDDFSTkdylkDN----LDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFL 587
Cdd:cd04179  15 LVERLLAVLEEGYDY---EIIVVDDGST-----DGtaeiARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARGDIVVTM 86

                ..
gi 32698686 588 DS 589
Cdd:cd04179  87 DA 88

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 32698686 806 PIVRASGVLINVALGKCISIEN----TTVILEDC--DGSKEL----QQFNYTWLRLIKCGE------WCIAPIPDKGAVR 869
Cdd:cd23477   2 PPPAAWGEIRNVAANLCVDSKHgatgTELRLDICvkDGSERTwsheQLFTFGWREDIRPGEplhtrkFCFDAISHNSPVT 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32698686 870 LHPCDNRNKGLKWLH-KSTSVFHPelvnhivFENNqqllCLEGNFSQKILKVAACDPVKPYQKWKFEK 936
Cdd:cd23477  82 LYDCHGMKGNQLWSYrKDKTLFHP-------VSNS----CMDCNPADKKIFMNRCDPLSETQQWIFEH 138

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 32698686 518 SVINRSPPHLIKEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHgLIRARLAGAQNATGDVLTFLDSHVECNVGW 597
Cdd:cd02525  21 SLLNQSYPKDLIEIIVVDGGST-DGTREIVQEYAAKDPRIRLIDNPKRI-QSAGLNIGIRNSRGDIIIRVDAHAVYPKDY 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 598 LEPLLErvYLSRKKVACpVIEVINDKDMSymtvdNFQRGIfVWPMNFGWRTIppdvIAKNRIKETDTIRCPVMAGGLFSi 677
Cdd:cd02525  99 ILELVE--ALKRTGADN-VGGPMETIGES-----KFQKAI-AVAQSSPLGSG----GSAYRGGAVKIGYVDTVHHGAYR- 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 32698686 678 dKSYFFELGTYDPGLDVwgGENMELSFKVWMCGGEIEIIPCSRVGH 723
Cdd:cd02525 165 -REVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYY 207

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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 814 LINVALGKCISIENTT--VILEDCDGSKELQQFNYTW---LRLIKCGEwCIA--PIPDKGAVRLHPCDNRNKGLKWlhks 886
Cdd:cd23385   5 IYNEDLGKCLAARSSSskVSLSTCNPNSPNQQWKWTSghrLFNVGTGK-CLGvsSSSPSSPLRLFECDSEDELQKW---- 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32698686 887 tsvfhpELVNHIVFENNQQLLCLEGNFSQKILKVaaCDPVKPYQKWK 933
Cdd:cd23385  80 ------KCSKDGLLLLKGLGLLLLYDKSGKNVVV--SKGSGLSSRWK 118

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 32698686 830 VILEDCDGSKELQQFNYTW---LRLIKCGEWCIAPIPDkGAVRLHPCDNRNKGL----KWLHK-STSVFHPelvnhivfe 901
Cdd:cd23435  29 VIMYGCHGLGGNQYFEYTSkgeIRHNIGKELCLHASGS-DEVILQHCTSKGKDVppeqKWLFTqDGTIRNP--------- 98

                        90       100       110
                ....*....|....*....|....*....|....
gi 32698686 902 nnQQLLCLEGnfSQKILKVAACDPVKPYQKWKFE 935
Cdd:cd23435  99 --ASGLCLHA--SGYKVLLRTCNPSDDSQKWTFI 128

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 32698686 500 VIMCFVDEVwSTLLRSVHSVINRSPPHLIKEILLVDDFS---TKDYLKDNLDKymsQFPKVRILRLKERH--GLIRARLA 574
Cdd:cd04192   1 VVIAARNEA-ENLPRLLQSLSALDYPKEKFEVILVDDHStdgTVQILEFAAAK---PNFQLKILNNSRVSisGKKNALTT 76

                        90       100
                ....*....|....*....|....*..
gi 32698686 575 GAQNATGDVLTFLDShvECNV--GWLE 599
Cdd:cd04192  77 AIKAAKGDWIVTTDA--DCVVpsNWLL 101

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 32698686 509 WSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKymsQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD 588
Cdd:cd04186   9 LEYLKACLDSLLAQTYPDF--EVIVVDNAST-DGSVELLRE---LFPEVRLIRNGENLGFGAGNNQGIREAKGDYVLLLN 82

                        90       100
                ....*....|....*....|....*.
gi 32698686 589 SHVECNVGWLEPLLERvYLSRKKVAC 614
Cdd:cd04186  83 PDTVVEPGALLELLDA-AEQDPDVGI 107