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 1229177745 583 LGAIKNLGVNMCLDGIasrkdGRRDVDIDAALELCQGSGPGQVFAYNSRNQLQHDRQCLTAVEGTKaAQLRFCIGDearN 662
Cdd:cd23460     2 LGQIKHTESGLCLDWA-----GESNGDKTVALKPCHGGGGNQFWMYTGDGQIRQDHLCLTADEGNK-VTLRECADQ---L 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1229177745 663 ANQRWVYNSKGMTIVNVSTKNCLDVKPSeadddIFLATMNECDGA-LSQQWTMH 715
Cdd:cd23460    73 PSQEWSYDEKTGTIRHRSTGLCLTLDAN-----NDVVILKECDSNsLWQKWIFQ 121

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 1229177745 583 LGAIKNLGVNMCLDGIasrkdGRRDVDIDAALELCQGSGPGQVFAYNSRNQLQHDRQCLTAVEGTKaAQLRFCIGDearN 662
Cdd:cd23460     2 LGQIKHTESGLCLDWA-----GESNGDKTVALKPCHGGGGNQFWMYTGDGQIRQDHLCLTADEGNK-VTLRECADQ---L 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1229177745 663 ANQRWVYNSKGMTIVNVSTKNCLDVKPSeadddIFLATMNECDGA-LSQQWTMH 715
Cdd:cd23460    73 PSQEWSYDEKTGTIRHRSTGLCLTLDAN-----NDVVILKECDSNsLWQKWIFQ 121

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229177745 584 GAIKNLGVNMCLDGIASRKDGRRdvdidAALELCQGSGPGQVFAYNSRNQLQH--DRQCLTAVEGTKAA--QLRFCigdE 659
Cdd:pfam00652   3 GRIRNRASGKCLDVPGGSSAGGP-----VGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDVGSTADGAkvVLWPC---H 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1229177745 660 ARNANQRWVYNSKGMTIVNVSTKNCLDVKPSE-ADDDIFLATMneCDGALSQQW 712
Cdd:pfam00652  75 PGNGNQRWRYDEDGTQIRNPQSGKCLDVSGAGtSNGKVILWTC--DSGNPNQQW 126

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229177745  586 IKNLGVNMCLDGIASrkdgrrdvDIDAALELCQGSGPGQVFAYNSRNQLQH--DRQCLTAVEGT-KAAQLRFCIGDearN 662
Cdd:smart00458   1 IISGNTGKCLDVNGN--------KNPVGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTgSTVTLYSCDGT---N 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1229177745  663 ANQRWVYNSKGmTIVNVSTKNCLDVKPSEADDDIflaTMNECDGALSQQWT 713
Cdd:smart00458  70 DNQYWEVNKDG-TIRNPDSGKCLDVKDGNTGTKV---ILWTCSGNPNQKWI 116

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 1229177745 583 LGAIKNLGVNMCLDGIasrkdGRRDVDIDAALELCQGSGPGQVFAYNSRNQLQHDRQCLTAVEGTKaAQLRFCIGDearN 662
Cdd:cd23460     2 LGQIKHTESGLCLDWA-----GESNGDKTVALKPCHGGGGNQFWMYTGDGQIRQDHLCLTADEGNK-VTLRECADQ---L 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1229177745 663 ANQRWVYNSKGMTIVNVSTKNCLDVKPSeadddIFLATMNECDGA-LSQQWTMH 715
Cdd:cd23460    73 PSQEWSYDEKTGTIRHRSTGLCLTLDAN-----NDVVILKECDSNsLWQKWIFQ 121

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 1229177745 580 FSVLGAIKNLGVNMCLDGIaSRKDGRrdvdiDAALELCQGSGPGQVFAYNSRNQLQHDRQCLTAVEGTKAAQLRFCIGDe 659
Cdd:cd23433     3 YYSLGEIRNVETNLCLDTM-GRKAGE-----KVGLSSCHGQGGNQVFSYTAKGEIRSDDLCLDASRKGGPVKLEKCHGM- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1229177745 660 arNANQRWVYNSKGMTIVNVSTKNCLDvKPSEADDDifLATMNECDGALSQQWTM 714
Cdd:cd23433    76 --GGNQEWEYDKETKQIRHVNSGLCLT-APNEDDPN--EPVLRPCDGGPSQKWEL 125

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229177745 584 GAIKNLGVNMCLDGIASRKDGRRdvdidAALELCQGSGPGQVFAYNSRNQLQH--DRQCLTAVEGTKAA--QLRFCigdE 659
Cdd:pfam00652   3 GRIRNRASGKCLDVPGGSSAGGP-----VGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDVGSTADGAkvVLWPC---H 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1229177745 660 ARNANQRWVYNSKGMTIVNVSTKNCLDVKPSE-ADDDIFLATMneCDGALSQQW 712
Cdd:pfam00652  75 PGNGNQRWRYDEDGTQIRNPQSGKCLDVSGAGtSNGKVILWTC--DSGNPNQQW 126

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 13 (GALNT13) and similar proteins; GALNT13 (EC 2.4.1.41), also called polypeptide GalNAc transferase 13, GalNAc-T13, pp-GaNTase 13, protein-UDP acetylgalactosaminyltransferase 13, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, 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. It 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. GALNT13 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). The 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 1229177745 579 KFSVLGAIKNLGVNMCLDGIAsRKDGRRdvdidAALELCQGSGPGQVFAYNSRNQLQHDRQCLTAVEGTKAAQLRFCigd 658
Cdd:cd23467     2 RYYSLGEIRNVETNQCLDNMG-RKENEK-----VGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKC--- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1229177745 659 EARNANQRWVYNSKGMTIVNVSTKNCLDvKPSEadDDIFLATMNECDGALSQQWTMHN 716
Cdd:cd23467    73 HHMRGNQLWEYDAERLTLRHVNSNQCLD-EPSE--EDKMVPTMKDCSGSRSQQWLLRN 127

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 1229177745 583 LGAIKNLGVNMCLDGIASRKDGRRDVDIDAalelCQGSGPGQVFAYNSRNQLQHDRQCLTAVEGTKAAQLRFCIGdeaRN 662
Cdd:cd23462     5 YGEIRNLAGKLCLDAPGRKKELNKPVGLYP----CHGQGGNQYWMLTKDGEIRRDDLCLDYAGGSGDVTLYPCHG---MK 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1229177745 663 ANQRWVYNSKGMTIVNVSTKNCLDVkpseaDDDIFLATMNECDGALS-QQWT 713
Cdd:cd23462    78 GNQFWIYDEETKQIVHGTSKKCLEL-----SDDSSKLVMEPCNGSSPrQQWE 124

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229177745 264 PTTSVIIVFHNEaWSTLLRTVTSVINRSSRELvkEIVLVDDASEpkfDWLQKPLEKYVAGlpvSVKVERLKSRQGIVAAR 343
Cdd:COG1216     3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGST---DGTAELLAALAFP---RVRVIRNPENLGFAAAR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229177745 344 HLGVSVSKGEVLTFLDSHCECTKGWLEPLLEriardrtrvtspvidsisdttfeysaapglpliggfswlpeftwtgvpl 423
Cdd:COG1216    74 NLGLRAAGGDYLLFLDDDTVVEPDWLERLLA------------------------------------------------- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229177745 424 reqrrvnydihlplrtptmAGGLFaIHRDFFRRLGGYDTGMRIWGGENLqLSFKVWQCGGSLEIVPCSHVGHVFRSTTpy 503
Cdd:COG1216   105 -------------------AACLL-IRREVFEEVGGFDERFFLYGEDVD-LCLRLRKAGYRIVYVPDAVVYHLGGASS-- 161

                         250       260
                  ....*....|....*....|...
gi 1229177745 504 dFPEGAETTVLRNNRRFLEVWAD 526
Cdd:COG1216   162 -GPLLRAYYLGRNRLLFLRKHGP 183

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229177745 264 PTTSVIIVFHNEAwSTLLRTVTSVINRSSRELvkEIVLVDDASEPKFDWLqkpLEKYVAGLPvSVKVERLKSRQGIVAAR 343
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTAEI---LRELAAKDP-RIRVIRLERNRGKGAAR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229177745 344 HLGVSVSKGEVLTFLDSHCECTKGWLEPLLERIARDRTRVtspvidsisdttfeysaapglplIGGFSWLPEFTWTGVPL 423
Cdd:COG0463    75 NAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADL-----------------------VYGSRLIREGESDLRRL 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1229177745 424 ReqRRVNYDIHLPLRTPTMAGGLFAIHRDFFRRLgGYDTGMRI 466
Cdd:COG0463   132 G--SRLFNLVRLLTNLPDSTSGFRLFRREVLEEL-GFDEGFLE 171

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 1229177745 268 VIIVFHNEAwSTLLRTVTSVINRSSRELvkEIVLVDDASEPkfDWLQKpLEKYVAgLPVSVKVERLKSRQGIVAARHLGV 347
Cdd:cd00761     1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTD--GTLEI-LEEYAK-KDPRVIRVINEENQGLAAARNAGL 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1229177745 348 SVSKGEVLTFLDSHCECTKGWLEPLLERIARDR 380
Cdd:cd00761    74 KAARGEYILFLDADDLLLPDWLERLVAELLADP 106

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 1229177745 580 FSVLGAIKNLgvNMCLDGiasrkdGRRDVDIDAALEL--CQGSGPGQVFAYNSRNQLQHDRQCLTAVEGTKAAQ--LRFC 655
Cdd:cd23441     2 ELAYGQIKQG--NLCLDS------DEQLFQGPALLILapCSNSSDSQEWSFTKDGQLQTQGLCLTVDSSSKDLPvvLETC 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229177745 656 IGDearnANQRWVYnsKGMTIVNVSTKNCLDVKPSeadddiFLATMNEC-DGALSQQWTMH 715
Cdd:cd23441    74 SDD----PKQKWTR--TGRQLVHSESGLCLDSRKK------KGLVVSPCrSGAPSQKWDFT 122

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 15 (GALNT15) and similar proteins; GALNT15 (EC 2.4.1.41), also called polypeptide GalNAc transferase 15, GalNAc-T15, polypeptide GalNAc transferase-like protein 2, GalNAc-T-like protein 2, pp-GaNTase-like protein 2, polypeptide N-acetylgalactosaminyltransferase-like protein 2, protein-UDP acetylgalactosaminyltransferase-like protein 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, GALNT15 can transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. It prefers Muc1a as its substrate. GALNT15 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 1229177745 583 LGAIKNLGVNMCLDGIAsrkdGRRDVDIDAALELCQGSGPGQVFAYNSRNQLQHDRQ--CLTAVEgtKAAQLRFCigdEA 660
Cdd:cd23442     5 SGQLYNTGTGYCADYIH----GWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSLqlCLDVRQ--EQVVLQNC---TK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1229177745 661 RNANQRWVYNSKGMtIVNVSTKNCLDVKPSEADDDIFLatmNECDGALSQQWT 713
Cdd:cd23442    76 EKTSQKWDFQETGR-IVHILSGKCIEAVESENSKLLFL---SPCNGQRNQMWK 124

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229177745 268 VIIVFHNEAwSTLLRTVTSVinRSSRELVKEIVLVDDASEPKFDWLqkpLEKYVAGLPVSVKVERLKSRQGIVAARHLGV 347
Cdd:cd06423     1 IIVPAYNEE-AVIERTIESL--LALDYPKLEVIVVDDGSTDDTLEI---LEELAALYIRRVLVVRDKENGGKAGALNAGL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229177745 348 SVSKGEVLTFLDSHCECTKGWLEPLLERIARDrtrvtSPVIdsisdttfeysAAPGLPLI--GGFSWLPEF------TWT 419
Cdd:cd06423    75 RHAKGDIVVVLDADTILEPDALKRLVVPFFAD-----PKVG-----------AVQGRVRVrnGSENLLTRLqaieylSIF 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1229177745 420 GVPLREQRRVNydihlplRTPTMAGGLFAIHRDFFRRLGGYDTGM 464
Cdd:cd06423   139 RLGRRAQSALG-------GVLVLSGAFGAFRREALREVGGWDEDT 176

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 1229177745 267 SVIIVFHNEAwSTLLRTVTSVINrSSRELVK-EIVLVDDASEpkfDWLQKPLEKYVAGLPVSVKVERLKSRQGivAARHL 345
Cdd:cd02525     3 SIIIPVRNEE-KYIEELLESLLN-QSYPKDLiEIIVVDGGST---DGTREIVQEYAAKDPRIRLIDNPKRIQS--AGLNI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229177745 346 GVSVSKGEVLTFLDSHCECTKGWLEPLLERIARDRTRVTSPVIDSISDTTFEYSAApglpliggfswLPEFTWTGVPLRE 425
Cdd:cd02525    76 GIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIA-----------VAQSSPLGSGGSA 144

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1229177745 426 QRRVNYDIHlplRTPTMAGGLFaiHRDFFRRLGGYD 461
Cdd:cd02525   145 YRGGAVKIG---YVDTVHHGAY--RREVFEKVGGFD 175

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10) and similar proteins; GALNT10 (EC 2.4.1.41), also called polypeptide GalNAc transferase 10, GalNAc-T10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, 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. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. GALNT10 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 1229177745 580 FSVLGAIKNLGVNMCLDGiasrKDGRRDVDIdaALELCQ-GSG-----PGQVFAYNSRNQL-----QHDRQ-CLTAVEGT 647
Cdd:cd23476     4 AAAWGEIRNVGTGLCADT----KHGALGSPL--RLEGCVkGRGeaawnNGQVFTFGWREDIrpgdpQHTKKfCFDAISHN 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229177745 648 KAAQLRFCIGdeaRNANQRWVYNsKGMTIVNVSTKNCLDVkpSEADDDIFlatMNECD-GALSQQW 712
Cdd:cd23476    78 SPVTLYDCHG---MKGNQLWRYR-KDKTLYHPVSNSCMDC--SESDHRIF---MNTCNpSSPTQQW 134

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 1229177745 635 QHDRQCLTAVEGTKAAQLRFCIGDEARNANQRWVYNSKGM---TIVNVSTKNCLDVKPSEADDDIFLaTMNECDGALSQQ 711
Cdd:cd00161     8 AASGKCLDVAGGSTANGAPVQQWTCNGGANQQWTLTPVGDgyyTIRNVASGKCLDVAGGSTANGANV-QQWTCNGGDNQQ 86

                          90
                  ....*....|..
gi 1229177745 712 WTMHNITIRGFS 723
Cdd:cd00161    87 WRLEPVGDGYYR 98

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) and similar proteins; GALNT3 (EC 2.4.1.41), also called polypeptide GalNAc transferase 3, GalNAc-T3, pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, 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. 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. GALNT3 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 1229177745 577 PLKFsvlGAIKNLGVNMCLDGIASRKDGRRDVdidaaLELCQGSGPGQVFAYNSRNQLQHDRQ---CLTAVEGTkaAQLR 653
Cdd:cd23468     2 PLIF---GAIKNVGKELCLDVGENNHGGKPLI-----MYNCHGLGGNQYFEYSTHHEIRHNIQkelCLHGSQGS--VQLK 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229177745 654 FCI---GDEARNANQRWVYNsKGMTIVNVSTKNCLDVKPSEADddifLATMNECDgaLSQQW 712
Cdd:cd23468    72 ECTykgRNTAVLPEEKWELQ-KDQLLYNPALNMCLSANGENPS----LVPCNPSD--PFQQW 126

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8)-like subfamily; The GALNT8-like subfamily includes GALNT8, GALNT9, GALNT17 and GALNT18. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT9 does not glycosylate apomucin or SDC3. Members of this family comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229177745 584 GAIKNLGV-NMCLD-GIasrKDGRRdvdidAALELCQGSGPgQVFAYNSRNQLQ---------HDRQCLTAVEGTKAAQL 652
Cdd:cd23438     6 GEMRNSLVtDLCLDqGP---KENHT-----AILYPCHGWSP-QLVRYTKDGQLYlgqlgstasPDTRCLVDDGKSDKPQL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229177745 653 RFCigDEARNANQR-WVYnSKGMTIVNVSTKNCLDVKPSeADDDIFLATMNECDGalsQQWTMHN 716
Cdd:cd23438    77 LDC--SKVKNRLQKyWDF-SQGGAIQNRATGRCLEVEED-KLNFGHRLVLQTCSG---QKWNIKN 134