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 2462569737 244 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQL 323
Cdd:cd23467     1 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNQL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462569737 324 WEYDAETHTLLHIITQSCLSVNKVADgSQHPTVETCNDSTLQKWLLRN 371
Cdd:cd23467    81 WEYDAERLTLRHVNSNQCLDEPSEED-KMVPTMKDCSGSRSQQWLLRN 127

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 2462569737 244 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQL 323
Cdd:cd23467     1 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNQL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462569737 324 WEYDAETHTLLHIITQSCLSVNKVADgSQHPTVETCNDSTLQKWLLRN 371
Cdd:cd23467    81 WEYDAERLTLRHVNSNQCLDEPSEED-KMVPTMKDCSGSRSQQWLLRN 127

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569737  252 IRNVETNQCLDNMGRKENekVGIFNCHGMGGNQVFSYTADKEIRT--DDLCLDVSRLNG-PVIMLKCHHMRGNQLWEYDa 328
Cdd:smart00458   1 IISGNTGKCLDVNGNKNP--VGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGsTVTLYSCDGTNDNQYWEVN- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462569737  329 ETHTLLHIITQSCLSVNKvADGSQHPTVETCNDSTLQKWLLR 370
Cdd:smart00458  78 KDGTIRNPDSGKCLDVKD-GNTGTKVILWTCSGNPNQKWIFE 118

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569737 237 YPDSQIPRR-YYSLGEIRnVETNQCLDNMGR-KENEKVGIFNCHGmGGNQVFSYTADKEIRTDDLCLDVSRLN----GPV 310
Cdd:NF035930  106 YPDYPGQGGgGWGGREIR-GKGGLCLDVSGGlRPGNGLIVYNCNG-GENQRFTWGRGGELRVGDLCLDVADGNtrdgARV 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462569737 311 IMLKCHHMRgNQLWEYD-AETHTLLhiiTQSCLSV-NKVADGSQHPTVETCNDSTLQKW 367
Cdd:NF035930  184 IAWSCSGGP-NQRWRWRgGQIRSRL---SGKCLDIeGGRARPGQPVIVWSCNGGPNQRW 238

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 2462569737 244 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQL 323
Cdd:cd23467     1 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNQL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462569737 324 WEYDAETHTLLHIITQSCLSVNKVADgSQHPTVETCNDSTLQKWLLRN 371
Cdd:cd23467    81 WEYDAERLTLRHVNSNQCLDEPSEED-KMVPTMKDCSGSRSQQWLLRN 127

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 2462569737 244 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQL 323
Cdd:cd23433     1 LDYYSLGEIRNVETNLCLDTMGRKAGEKVGLSSCHGQGGNQVFSYTAKGEIRSDDLCLDASRKGGPVKLEKCHGMGGNQE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462569737 324 WEYDAETHTLLHIITQSCLSVNKvADGSQHPTVETCNDSTLQKWLLRN 371
Cdd:cd23433    81 WEYDKETKQIRHVNSGLCLTAPN-EDDPNEPVLRPCDGGPSQKWELEG 127

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 2462569737 250 GEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKChHMRGNQLWEYDAE 329
Cdd:cd23437     6 GEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKC-NLGETGKWEYDEA 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462569737 330 THTLLHIITQSCLSVNKvadGSQHPTVETC-NDSTLQKW 367
Cdd:cd23437    85 TGQIRHKGTGKCLDLNE---GTNKLILQPCdSSSPSQKW 120

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10)-like subfamily; The GALNT10-like subfamily includes GALNT10 and GALNTL6. 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. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. 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 2462569737 250 GEIRNVETNQCLDNMGRKENEKVGIFNC--HGMGGNQVFSYTADKEIR--TDDLCLDVSRL--NGPVIMLKCHHMRGNQL 323
Cdd:cd23439     3 GEIRNVGSGLCIDTKHGGENDEVRLSKCvkDGGGGEQQFELTWHEDIRpkKRKVCFDVSSHtpGAPVILYACHGMKGNQL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462569737 324 WEYDAETHTLLHIITQSCLSVNkvaDGSQHPTVETCN-DSTLQKW 367
Cdd:cd23439    83 WKYRPNTKQLYHPVSGLCLDAD---PGSGKVFMNHCDeSSDTQKW 124

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 2462569737 250 GEIRNveTNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDV--SRLNGPVIMLKCHHMRGNQLWEYD 327
Cdd:cd23434     3 GSLKQ--GNLCLDTLGHKAGGTVGLYPCHGTGGNQEWSFTKDGQIKHDDLCLTVvdRAPGSLVTLQPCREDDSNQKWEQI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462569737 328 AETHTLLHIITQSCLSVNkvaDGSQH-PTVETCNDSTL-QKW 367
Cdd:cd23434    81 ENNSKLRHVGSNLCLDSR---NAKSGgLTVETCDPSSGsQQW 119

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569737  252 IRNVETNQCLDNMGRKENekVGIFNCHGMGGNQVFSYTADKEIRT--DDLCLDVSRLNG-PVIMLKCHHMRGNQLWEYDa 328
Cdd:smart00458   1 IISGNTGKCLDVNGNKNP--VGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGsTVTLYSCDGTNDNQYWEVN- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462569737  329 ETHTLLHIITQSCLSVNKvADGSQHPTVETCNDSTLQKWLLR 370
Cdd:smart00458  78 KDGTIRNPDSGKCLDVKD-GNTGTKVILWTCSGNPNQKWIFE 118

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 2462569737   1 MEERSGLIRARLRGAAASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMagsdmtyggfnWK 80
Cdd:pfam00535  60 LPENRGKAGARNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR-----------RA 128

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462569737  81 LNFRWYPVPQREMDRRKGdRTLPVRTPTMAGGLFSIDR 118
Cdd:pfam00535 129 SRITLSRLPFFLGLRLLG-LNLPFLIGGFALYRREALE 165

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 2462569737 245 RYYSLGEIRNVETNQCLDNM--GRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDD--LCLDVSrlNGPVIMLKCHHMRG 320
Cdd:cd23442     1 APYFSGQLYNTGTGYCADYIhgWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSlqLCLDVR--QEQVVLQNCTKEKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462569737 321 NQLWEYDaETHTLLHIITQSCLSVNKvADGSQHPTVETCNDSTLQKW 367
Cdd:cd23442    79 SQKWDFQ-ETGRIVHILSGKCIEAVE-SENSKLLFLSPCNGQRNQMW 123

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 11 (GALNT11) and similar proteins; GALNT11 (EC 2.4.1.41), also called polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, 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 is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes its activation, modulating the balance between motile and immotile (sensory) cilia at the left-right organizer (LRO). GALNT11 displays the same enzyme activity toward MUC1, MUC4, and EA2 as GALNT1. It is not involved in glycosylation of erythropoietin (EPO). GALNT11 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 2462569737 250 GEIRNVETNQCLdnMGRKENEKVG----IFNCHGMGGNQVFSYTADKEIRTDD-LCLDVSRLNGPVIML-KCHHMRGNQL 323
Cdd:cd23440     6 GQLKHAGSGLCL--VAEDEVSQKGsllvLRPCSRNDKKQLWYYTEDGELRLANlLCLDSSETSSDFPRLmKCHGSGGSQQ 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462569737 324 WEYDAETHtLLHIITQSCLSVNKVADgSQHPTVETCNDSTLQKWLL 369
Cdd:cd23440    84 WRFKKDNR-LYNPASGQCLAASKNGT-SGYVTMDICSDSPSQKWVF 127

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569737 245 RYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTAD-KEIR--TDDLCLDVSR---LNGPVIMLKCHHM 318
Cdd:pfam00652  41 TLTGDGTIRSVASDLCLDVGSTADGAKVVLWPCHPGNGNQRWRYDEDgTQIRnpQSGKCLDVSGagtSNGKVILWTCDSG 120

                  ....*.
gi 2462569737 319 RGNQLW 324
Cdd:pfam00652 121 NPNQQW 126

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 6 (GALNT6) and similar proteins; GALNT6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 6, GalNAc-T6, pp-GaNTase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6, 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. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT6 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 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 2462569737 250 GEIRNVETNQCLDnMGrkENEKVG----IFNCHGMGGNQVFSYTADKEIRTD---DLCLDVSRlnGPVIMLKCHH----- 317
Cdd:cd23470     5 GAIKNEGTNQCLD-VG--ENNRGGkpliMYSCHGMGGNQYFEYTTHKELRHNiakQLCLRVSK--GPVQLGECHYkgkns 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462569737 318 -MRGNQLWEYdAETHTLLHIITQSCLSVNkvadgSQHPTVETCNDSTL-QKWL 368
Cdd:cd23470    80 qVPPDEEWEL-TQDHLIRNSGSNMCLTAR-----GKHPAMAPCNPADPhQLWS 126

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 12 (GALNT12) and similar proteins; GALNT12 (EC 2.4.1.41), also called polypeptide GalNAc transferase 12, GalNAc-T12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12, 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. 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. GALNT12 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 2462569737 257 TNQCLDNMGRKENEKVG----IFNCHGMGGNQVFSYTADKEIRTD----DLCLDVSRLNGPVIMLKC----HHMRGNQLW 324
Cdd:cd23471    13 TNYCFDYNPPDEHQIAGhqviLYQCHGMGQNQFFEYTSQNEIRYNtrqpEGCAAVDAGTDFLTMHLCrenrQAVPENQKF 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462569737 325 EYDaETHTLLHIITQSCL-SVNKVADGSQHPTVETCNDSTLQKWLLR 370
Cdd:cd23471    93 IFR-EDGSLFHVQTQKCVqAVRNESSGSPAPVLRPCTDSDHQKWFFK 138

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 2462569737 250 GEIRNVETNQCLDNMG--RKENEKVGIFNCHGmGGNQVFSYTADK----EIRT--DDLCLDV---SRLNG-PVIMLKCHH 317
Cdd:cd00161     3 YRIVNAASGKCLDVAGgsTANGAPVQQWTCNG-GANQQWTLTPVGdgyyTIRNvaSGKCLDVaggSTANGaNVQQWTCNG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462569737 318 mRGNQLWEYDAETHTLLHIITQS---CLSV--NKVADGSQhPTVETCNDSTLQKW 367
Cdd:cd00161    82 -GDNQQWRLEPVGDGYYRIVNKHsgkCLDVsgGSTANGAN-VQQWTCNGGANQQW 134

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 4 (GALNT4) and similar proteins; GALNT4 (EC 2.4.1.41), also called polypeptide GalNAc transferase 4, GalNAc-T4, pp-GaNTase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4, 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. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT4 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 2462569737 250 GEIRNVE-TNQCLDNMGRKEN---EKVGIFNCHGMGGNQVFSYTADKEIRTD---DLCLDVSRLNGPVIMLKCHH----M 318
Cdd:cd23469     5 GAVRSMGiSSECLDYNSPEHNptgAHLSLFGCHGQGGNQFFEYTSNKEIRFNsvtELCAEVPDQKNYIGMKHCPKdgspV 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462569737 319 RGNQLWEYdAETHTLLHIITQSCLSVNKVADGSQHPTVETCN 360
Cdd:cd23469    85 PANIIWHF-KEDGTIYHPHSGMCISAYRTPEGRADVQMRTCD 125

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 2462569737 250 GEIRNveTNQCLDNMGRK--ENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDV--SRLNGPVIMLKCHHmRGNQLWE 325
Cdd:cd23441     6 GQIKQ--GNLCLDSDEQLfqGPALLILAPCSNSSDSQEWSFTKDGQLQTQGLCLTVdsSSKDLPVVLETCSD-DPKQKWT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462569737 326 YdAETHtLLHIITQSCLSVNKVADgsqhPTVETCNDSTL-QKW 367
Cdd:cd23441    83 R-TGRQ-LVHSESGLCLDSRKKKG----LVVSPCRSGAPsQKW 119

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 2462569737 250 GEIRnvETNQCLDNMgRKENEKVGIFN---CHGMGG----NQVFSYTADKEIRTDDLCLDVSRL--NGPVIMLKCHHMRG 320
Cdd:cd23478    10 GVIR--QRQNCLESR-RVEGQELPNLSlspCIKSKGvpakSQEWAYTYNQQIRQQQLCLSVHTLfpGSPVVLVPCKEGDG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462569737 321 NQLWEYDAeTHtLLHIITQSCLSVNKVADG---SQHPTVETCNDSTL-QKW 367
Cdd:cd23478    87 KQRWTKVG-SH-IEHMASRFCLDTEMFGDGtesSKEIVINPCESSAMsQRW 135

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 9 (GALNT9) and similar proteins; GALNT9 (EC 2.4.1.41), also called polypeptide GalNAc transferase 9, GalNAc-T9, pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9, 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. GALNT9 does not glycosylate apomucin or SDC3. GALNT9 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 2462569737 250 GEIRNVE-TNQCLDNmGRKENEKVGIFNCHGMgGNQVFSYTADKEIR----------TDDLCL-DVSRLNGPVIMlKCHH 317
Cdd:cd23473    11 GEVRNSKaSGYCLDQ-GSEEDDKAILYPCHGM-SSQLVRYSTEGLLQlgplgstaflPDTKCLvDDGRGRTPTLK-KCED 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462569737 318 M-RGNQ-LWEYdAETHTLLHIITQSCLSV--NKVADGSQHPTVETCNDstlQKWLLRNYTR 374
Cdd:cd23473    88 VaRPAQrLWDF-TQNGPIISRDTGRCLEVemSKDANFGLRLVVQRCSG---QKWMIRNWIK 144

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569737   2 EERSGLIRARLRGAAASKGQVITFLDAHCECTLGWLEPLLARIKEDrktvvcpiidvisddtfeymaGSDMTYGGFNWKL 81
Cdd:COG0463    65 ERNRGKGAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEG---------------------PADLVYGSRLIRE 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462569737  82 NFRWYPVPQREMDRRkgdRTLPVRTPTMAGGLFSIDRNYFEEIGtYDAGM 131
Cdd:COG0463   124 GESDLRRLGSRLFNL---VRLLTNLPDSTSGFRLFRREVLEELG-FDEGF 169

second ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2+-dependent hemolytic lectin CEL-III and similar proteins; CEL-III is a Ca2+-dependent and galactose-specific lectin that exhibits hemolytic and hemagglutinating activities. It functions as an oligomer that forms an ion-permeable pore in the cell membrane. CEL-III consists of three domains: two N-terminal ricin B-type lectin domains, and a C-terminal pore-forming domain. The ricin B-type lectin domains show a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. The model corresponds to the second ricin B-type lectin domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569737 250 GEIRNVETNQCLDNMGRKENEKVGIFNCHGmGGNQVFSYTADKEIRTDD--LCLDVSRLNGP--VIMLKCHHMRgNQLWE 325
Cdd:cd23420     6 GRLRNEKSDLCLDVEGSDGKGNVLMYSCED-NLDQWFRYYENGEIVNAKsrMCLDVSGSDGSgnVGIYRCEDLR-DQMWS 83

                          90       100
                  ....*....|....*....|....
gi 2462569737 326 Y-----DAETHTLLHIITQSCLSV 344
Cdd:cd23420    84 RpnqycNGDYCSFLNKESNKCLDV 107

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 2462569737 293 EIRTDDLCLDVSRLNGP----VIMLKCHHMRGNQLWEYdAETHTllhIITQS-CLSVNKVADGsQHPTVETCNDSTLQKW 367
Cdd:cd23441     7 QIKQGNLCLDSDEQLFQgpalLILAPCSNSSDSQEWSF-TKDGQ---LQTQGlCLTVDSSSKD-LPVVLETCSDDPKQKW 81

                  .
gi 2462569737 368 L 368
Cdd:cd23441    82 T 82

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 2462569737 298 DLCLDV---SRLNG-PVIMLKCHHmRGNQLWEYDAE---THTLLHIITQSCLSV--NKVADGSQhPTVETCNDSTLQKWL 368
Cdd:cd00161    11 GKCLDVaggSTANGaPVQQWTCNG-GANQQWTLTPVgdgYYTIRNVASGKCLDVagGSTANGAN-VQQWTCNGGDNQQWR 88