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 564356515 126 SVIITFHNEARSTLLRTVKSVLNRTPAGLIQEIILVDDFSSDPEDCLLL-----TRIPKVKCLRNDKREGLIRSRVRGAD 200
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 201 VAGASVLTFLDSHCEVNVEWLQPMLQRVMEDHTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKmTR 280
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 281 TDPTKPIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFR-KRHPYNFPEGN 359
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564356515 360 AlTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMDCKSFRWYLENVY 420
Cdd:cd02510  240 G-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 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 564356515 126 SVIITFHNEARSTLLRTVKSVLNRTPAGLIQEIILVDDFSSDPEDCLLL-----TRIPKVKCLRNDKREGLIRSRVRGAD 200
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 201 VAGASVLTFLDSHCEVNVEWLQPMLQRVMEDHTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKmTR 280
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 281 TDPTKPIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFR-KRHPYNFPEGN 359
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564356515 360 AlTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMDCKSFRWYLENVY 420
Cdd:cd02510  240 G-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 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 564356515  126 SVIITFHNEArSTLLRTVKSVLNRTPAGLiqEIILVDDFSSD--PEDCL-LLTRIPKVKCLRNDKREGLIRSRVRGADVA 202
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGSTDgtVEIAEeYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515  203 GASVLTFLDSHCEVNVEWLQPMLQRVMEDHTRVVSPIIDVISLDNFAYlaasadlrggfdWSLHFKWEQIPLEQKMTRTD 282
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY------------RRASRITLSRLPFFLGLRLL 145

                         170       180
                  ....*....|....*....|....
gi 564356515  283 PTKpirTPVIAGGIFVIDKSWFNH 306
Cdd:pfam00535 146 GLN---LPFLIGGFALYRREALEE 166

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 126 SVIITFHNEARsTLLRTVKSVLNRTPAGLiqEIILVDDFSSDP-EDCL--LLTRIPKVKCLRNDKREGLIRSRVRGADVA 202
Cdd:COG0463    5 SVVIPTYNEEE-YLEEALESLLAQTYPDF--EIIVVDDGSTDGtAEILreLAAKDPRIRVIRLERNRGKGAARNAGLAAA 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564356515 203 GASVLTFLDSHCEVNVEWLQPMLQRVMEDHTRVV 236
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115

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 564356515 126 SVIITFHNEARSTLLRTVKSVLNRTPAGLIQEIILVDDFSSDPEDCLLL-----TRIPKVKCLRNDKREGLIRSRVRGAD 200
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 201 VAGASVLTFLDSHCEVNVEWLQPMLQRVMEDHTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKmTR 280
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 281 TDPTKPIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFR-KRHPYNFPEGN 359
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564356515 360 AlTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMDCKSFRWYLENVY 420
Cdd:cd02510  240 G-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. 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. 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. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 429 EVLPGVIKQGVNCLESQGQNTAGDLLLGMGICRGSAKSpppaQAWLFS-DHLIQQQGKCLAATSTlmsSPGSPVVLQSCN 507
Cdd:cd23441    2 ELAYGQIKQGNLCLDSDEQLFQGPALLILAPCSNSSDS----QEWSFTkDGQLQTQGLCLTVDSS---SKDLPVVLETCS 74

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 564356515 508 PkEGKQKWRRKGSFIQHSVSGLCLET-KPAQLVTNKC 543
Cdd:cd23441   75 D-DPKQKWTRTGRQLVHSESGLCLDSrKKKGLVVSPC 110

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 564356515 433 GVIKQGVNCLESQGQNTAGDLLLGMGICRGSAKSPPPAQAWLF-SDHLIQQQGKCLAATSTLmssPGSPVVLQSCNPKEG 511
Cdd:cd23478   10 GVIRQRQNCLESRRVEGQELPNLSLSPCIKSKGVPAKSQEWAYtYNQQIRQQQLCLSVHTLF---PGSPVVLVPCKEGDG 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564356515 512 KQKWRRKGSFIQHSVSGLCLETKPA--------QLVTNKC 543
Cdd:cd23478   87 KQRWTKVGSHIEHMASRFCLDTEMFgdgtesskEIVINPC 126

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 126 SVIITFHNEARsTLLRTVKSVLNRTPAGLiqEIILVDDFSSDP-EDCL--LLTRIPKVKCLRNDKREGLIRSRVRGADVA 202
Cdd:COG0463    5 SVVIPTYNEEE-YLEEALESLLAQTYPDF--EIIVVDDGSTDGtAEILreLAAKDPRIRVIRLERNRGKGAARNAGLAAA 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564356515 203 GASVLTFLDSHCEVNVEWLQPMLQRVMEDHTRVV 236
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115

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 564356515 127 VIITFHNEARsTLLRTVKSVLNRTPagLIQEIILVDDFSSD--PEDCL-LLTRIPKVKCLRNDKREGLIRSRVRGADVAG 203
Cdd:cd00761    1 VIIPAYNEEP-YLERCLESLLAQTY--PNFEVIVVDDGSTDgtLEILEeYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564356515 204 ASVLTFLDSHCEVNVEWLQPMLQRVMEDHTRVVspiidVISLDNFAYLAASADLRGGFDWSLHFKWE 270
Cdd:cd00761   78 GEYILFLDADDLLLPDWLERLVAELLADPEADA-----VGGPGNLLFRRELLEEIGGFDEALLSGEE 139

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 564356515 119 SSDLPATSVIITFHNEARsTLLRTVKSVLNRT-PAGLIqEIILVDDFSSDPEDCLLLT---RIPKVKCLRNDKREGLIRS 194
Cdd:COG1215   25 PADLPRVSVIIPAYNEEA-VIEETLRSLLAQDyPKEKL-EVIVVDDGSTDETAEIARElaaEYPRVRVIERPENGGKAAA 102

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564356515 195 RVRGADVAGASVLTFLDSHCEVNVEWLQPMLQR 227
Cdd:COG1215  103 LNAGLKAARGDIVVFLDADTVLDPDWLRRLVAA 135

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 441 CLESQGQNTAGDLllGMGICRGSAKspppAQAWLFSDHL-IQQQGKCLAAtstlmSSPGSPVVLQSCNPKEGKQKWR--R 517
Cdd:cd23433   17 CLDTMGRKAGEKV--GLSSCHGQGG----NQVFSYTAKGeIRSDDLCLDA-----SRKGGPVKLEKCHGMGGNQEWEydK 85

                         90       100       110
                 ....*....|....*....|....*....|
gi 564356515 518 KGSFIQHSVSGLCL----ETKPAQLVTNKC 543
Cdd:cd23433   86 ETKQIRHVNSGLCLtapnEDDPNEPVLRPC 115

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 564356515 433 GVIK-QGVN-CLESQGQnTAGDLLLGMGICRGSAKSpppaQAWLFS-DHLIQQQGKCLAATStlmsspGSPVVLQSCNPK 509
Cdd:cd23460    3 GQIKhTESGlCLDWAGE-SNGDKTVALKPCHGGGGN----QFWMYTgDGQIRQDHLCLTADE------GNKVTLRECADQ 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 564356515 510 EGKQKW--RRKGSFIQHSVSGLCLETKPA--QLVTNKC 543
Cdd:cd23460   72 LPSQEWsyDEKTGTIRHRSTGLCLTLDANndVVILKEC 109

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 441 CLESQGQNTAGDLLLGMGICRGSAKspppaQAWLFSDH--LIQQQGKCLAATSTlMSSPGSPVVLQSCNPKEGkQKWR-R 517
Cdd:cd23418   16 CLDVPGGSTTNGTRLILWDCHGGAN-----QQFTFTSAgeLRVGGDKCLDAAGG-GTTNGTPVVIWPCNGGAN-QKWRfN 88

                         90
                 ....*....|....*
gi 564356515 518 KGSFIQHSVSGLCLE 532
Cdd:cd23418   89 SDGTIRNVNSGLCLD 103

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 564356515 126 SVIITFHNEARsTLLRTVKSVLNRTPAGLIQEIILVDDFSSD-PEDCL--LLTRIPKVKCLRNDKReglIRS--RVRGAD 200
Cdd:cd02525    3 SIIIPVRNEEK-YIEELLESLLNQSYPKDLIEIIVVDGGSTDgTREIVqeYAAKDPRIRLIDNPKR---IQSagLNIGIR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 201 VAGASVLTFLDSHCEVNVEWLQPMLQRVMEDHTRVVSPIIDVISLDNF----AYLAASADLRGGfdwSLHfkweqipleq 276
Cdd:cd02525   79 NSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFqkaiAVAQSSPLGSGG---SAY---------- 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564356515 277 kmtRTDPTKPIRTPVIAGGIFviDKSWFNHLGKYDAQMDIwgGENFELSFRVWMCGGSLEIVPCSRVGHVFR 348
Cdd:cd02525  146 ---RGGAVKIGYVDTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPR 210

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 564356515 127 VIITFHNEARsTLLRTVKSVLNRT-PAGLIqEIILVDDFSSDpEDCLLLT-----RIPKVKCLRNDKREGlirSRVRGAD 200
Cdd:cd04192    1 VVIAARNEAE-NLPRLLQSLSALDyPKEKF-EVILVDDHSTD-GTVQILEfaaakPNFQLKILNNSRVSI---SGKKNAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 201 VAGASV-----LTFLDSHCEVNVEWLQPMLQ-RVMEDHTRVVSPII---------DVISLDnFAYLAASAdlRGGFDWSL 265
Cdd:cd04192   75 TTAIKAakgdwIVTTDADCVVPSNWLLTFVAfIQKEQIGLVAGPVIyfkgksllaKFQRLD-WLSLLGLI--AGSFGLGK 151

                 ..
gi 564356515 266 HF 267
Cdd:cd04192  152 PF 153

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 564356515 441 CLESQGQNTAGDLLLGMGICRGSAkspppAQAWLFSD-----HLIQQQ--GKCLAATSTLMSsPGSPVVLQSCNPKEGkQ 513
Cdd:cd00161   13 CLDVAGGSTANGAPVQQWTCNGGA-----NQQWTLTPvgdgyYTIRNVasGKCLDVAGGSTA-NGANVQQWTCNGGDN-Q 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 564356515 514 KWRRK----GSF-IQHSVSGLCLETK------PAQLVTNKC 543
Cdd:cd00161   86 QWRLEpvgdGYYrIVNKHSGKCLDVSggstanGANVQQWTC 126

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 564356515 127 VIITFHNEARsTLLRTVKSVLNRTPAGLiqEIILVDDFSSDPEDCLLLTRIPKVKCLRNDKREGLIRSRVRGADVAGASV 206
Cdd:cd04186    1 IIIVNYNSLE-YLKACLDSLLAQTYPDF--EVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 207 LTFLDSHCEVNVEWLQPMLqRVMEDHTRVVspiidvisldnfaylaasadlrggfdwslhfkweqipleqkmtrtdptkp 286
Cdd:cd04186   78 VLLLNPDTVVEPGALLELL-DAAEQDPDVG-------------------------------------------------- 106

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564356515 287 IRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWgGENFELSFRVWMCGGSLEIVPCSRVGH 345
Cdd:cd04186  107 IVGPKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYH 164

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 564356515 441 CLESQGQNTAGdlLLGMGICRGSAKSpppaQAW-LFSDHLIQQQGKCLAAtstlmSSPGSPVVLQSCNpKEGKQKWR--R 517
Cdd:cd23437   16 CLDTMGHQNGG--PVGLYPCHGMGGN----QLFrLNEAGQLAVGEQCLTA-----SGSGGKVKLRKCN-LGETGKWEydE 83

                         90       100
                 ....*....|....*....|....*...
gi 564356515 518 KGSFIQHSVSGLCLE--TKPAQLVTNKC 543
Cdd:cd23437   84 ATGQIRHKGTGKCLDlnEGTNKLILQPC 111

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 564356515 441 CLesqgQNTAGDLLLGMGICRGSAksppPAQAWL-FSDHLIQQQG--KCLAATStlmSSPGSPVVLQSCNPKEGKQKWRR 517
Cdd:cd23385   13 CL----AARSSSSKVSLSTCNPNS----PNQQWKwTSGHRLFNVGtgKCLGVSS---SSPSSPLRLFECDSEDELQKWKC 81

                         90
                 ....*....|
gi 564356515 518 KGSFIQHSVS 527
Cdd:cd23385   82 SKDGLLLLKG 91

first ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating proteins (RIPs); Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. They consist of a catalytic A-chain which has rRNA N-glycosidase activity and a lectin B-chain containing two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The lectin chain facilitates the internalization of the catalytic chain on binding to the cell surface. The two chains are connected by a disulfide bridge. This model corresponds to the first ricin B-type lectin domain. Members of this subfamily includes Ricinus communis ricin, bitter gourd (Momordica charantia) seed lectin (BGSL), snake gourd (Trichosanthes anguina) seed lectin (SGSL), Sambucus ebulus ebulin I, Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf, Abrus precatorius abrin (ABR) and agglutinin-I (AAG), and Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs).

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 471 QAWLF-SDHLIQQQGKCLAATStlmSSPGSPVVLQSCN-PKEGKQKWRRK--GSFIqHSVSGLCLETKPA 536
Cdd:cd23443   38 QLWTFkRDGTIRSNGKCLTTNG---YSPGSYVVIYDCStAVAEATKWEVSddGTII-NPASGLVLTADSG 103

ricin B-type lectin domain, beta-trefoil fold, found in alpha-galactosidase A (AglA) and similar proteins; AglA (EC 3.2.1.22), also called melibiase A, hydrolyzes a variety of simple alpha-D-galactosides as well as more complex molecules such as oligosaccharides and polysaccharides. It belongs to the glycosyl hydrolase 27 (GH27) family. AglA contains an N-terminal GH27 catalytic domain, an alpha galactosidase C-terminal beta sandwich domain in the middle region, and a carbohydrate-binding domain at the C-terminus. The carbohydrate-binding domain is also known as a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356515 440 NCLESQGQNtagdllLGMGICRGSAKspppaQAW-LFSDHLIQ---QQGKCLAATstlmsspGSPVVLQSCNPKEGkQKW 515
Cdd:cd23425   14 NCLTADAAE------VKFQTCDGSDS-----QIWqVRKSGILRnlsNTGQCLTAD-------GANVSLSPCDTSTS-QNW 74

                         90       100
                 ....*....|....*....|....*.
gi 564356515 516 R-RKGSFIQHSVSGLCLETKPAQLVT 540
Cdd:cd23425   75 SyEISGNLVNKKTGLCLTEGNDAQVT 100

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
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564356515 469 PAQAWLF--SDHLIQQQ--GKCLAATSTLmsspgSPVVLQSCNPKEGKQKWR 516
Cdd:cd23460   73 PSQEWSYdeKTGTIRHRstGLCLTLDANN-----DVVILKECDSNSLWQKWI 119

ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its 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 may harbor a sugar-binding pocket.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564356515 481 QQQGKCLAATSTLMSspGSPVVLQSCNPKEGkQKW-RRKGSFIQHSV-SGLCLE 532
Cdd:cd23456    8 QASGLCLDVSGGATN--GANVVVYDCNNSNS-QKWyYDATGRLHSKAnPGKCLD 58