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 161077156 518 DSVAHGEIANVPNGMCLDAKEKS-EEETPVSIYECHGQGGNQYWMLSKAGEIRRDDSCLDYAG--KDVTLFGCHGGKGNQ 594
Cdd:cd23462    1 EALAYGEIRNLAGKLCLDAPGRKkELNKPVGLYPCHGQGGNQYWMLTKDGEIRRDDLCLDYAGgsGDVTLYPCHGMKGNQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 161077156 595 FWTYRENTKQLHHGTSGKCLAISESKDKLLMEECSASLSRQQWTLE 640
Cdd:cd23462   81 FWIYDEETKQIVHGTSKKCLELSDDSSKLVMEPCNGSSPRQQWEFE 126

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 161077156 518 DSVAHGEIANVPNGMCLDAKEKS-EEETPVSIYECHGQGGNQYWMLSKAGEIRRDDSCLDYAG--KDVTLFGCHGGKGNQ 594
Cdd:cd23462    1 EALAYGEIRNLAGKLCLDAPGRKkELNKPVGLYPCHGQGGNQYWMLTKDGEIRRDDLCLDYAGgsGDVTLYPCHGMKGNQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 161077156 595 FWTYRENTKQLHHGTSGKCLAISESKDKLLMEECSASLSRQQWTLE 640
Cdd:cd23462   81 FWIYDEETKQIVHGTSKKCLELSDDSSKLVMEPCNGSSPRQQWEFE 126

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 161077156  212 DVIICFHNEaWTVLLRTVHSVLDRSPEHLigKIILVDDYSdMPHLKRQLEDYFAAYPKVQIIRGQKREGLIRARILGANH 291
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077156  292 AKSPVLTYLDSHCECTEGWLEPLLDRIARNSTTVVCPVIDVISDETLEYHyrdsggvnvggfdWNLQFSWHPVPERERKR 371
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR-------------RASRITLSRLPFFLGLR 143

                         170       180
                  ....*....|....*....|...
gi 161077156  372 HNSTAEPVYSPTMAGGLFSIDRE 394
Cdd:pfam00535 144 LLGLNLPFLIGGFALYRREALEE 166

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077156 209 PKTDVIICFHNEAwTVLLRTVHSVLDRSPEHLigKIILVDDYSDmPHLKRQLEDYFAAYPKVQIIRGQKREGLIRARILG 288
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGST-DGTAEILRELAAKDPRIRVIRLERNRGKGAARNAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077156 289 ANHAKSPVLTYLDSHCECTEGWLEPLLDRIARNSTTVVCPVIdVISDETLEYHYRDSGGVNVGGFDWNLqfswhpvpere 368
Cdd:COG0463   78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSR-LIREGESDLRRLGSRLFNLVRLLTNL----------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077156 369 rkrhnstaepvysPTMAGGLFSIDREFFDRLGtYDSGFdiwgGENLELsFKTWMCGGTLEIVPCSHVGHifrkRSPYKWR 448
Cdd:COG0463  146 -------------PDSTSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVPVRYRAG----ESKLNLR 202

                 ....*.
gi 161077156 449 SGVNVL 454
Cdd:COG0463  203 DLLRLL 208

cell envelope integrity inner membrane protein TolA; Provisional

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 161077156  91 QKQAHDEADIPPTVGKHKADLQAERMR---KKAAEQPKKKPQEDSKK 134
Cdd:PRK09510 131 QKQAEEAAAKAAAAAKAKAEAEAKRAAaaaKKAAAEAKKKAEAEAAK 177

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 161077156 518 DSVAHGEIANVPNGMCLDAKEKS-EEETPVSIYECHGQGGNQYWMLSKAGEIRRDDSCLDYAG--KDVTLFGCHGGKGNQ 594
Cdd:cd23462    1 EALAYGEIRNLAGKLCLDAPGRKkELNKPVGLYPCHGQGGNQYWMLTKDGEIRRDDLCLDYAGgsGDVTLYPCHGMKGNQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 161077156 595 FWTYRENTKQLHHGTSGKCLAISESKDKLLMEECSASLSRQQWTLE 640
Cdd:cd23462   81 FWIYDEETKQIVHGTSKKCLELSDDSSKLVMEPCNGSSPRQQWEFE 126

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 161077156 523 GEIANVPNGMCLDAKEKSEEEtPVSIYECHGQGGNQYWMLSKAGEIRRDDSCLD--YAGKDVTLFGCHGGKGNQFWTYRE 600
Cdd:cd23433    7 GEIRNVETNLCLDTMGRKAGE-KVGLSSCHGQGGNQVFSYTAKGEIRSDDLCLDasRKGGPVKLEKCHGMGGNQEWEYDK 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 161077156 601 NTKQLHHGTSGKCLAISE--SKDKLLMEECSASLSrQQWTLEN 641
Cdd:cd23433   86 ETKQIRHVNSGLCLTAPNedDPNEPVLRPCDGGPS-QKWELEG 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 161077156 520 VAHGEIANVPNGMCLDAKEKSEEeTPVSIYECHGQGGNQYWMLSKAGEIRRDDSCLDYAGKD--VTLFGCHGGkGNQFWT 597
Cdd:cd23437    3 LAWGEIRNLGTGLCLDTMGHQNG-GPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGgkVKLRKCNLG-ETGKWE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 161077156 598 YRENTKQLHHGTSGKCLAISESKDKLLMEECSASLSRQQWTLEN 641
Cdd:cd23437   81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124

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 161077156 521 AHGEIANVPNGMCLDAKEKsEEETPVSIYEC--HGQGGNQYWMLSKAGEIR--RDDSCLD----YAGKDVTLFGCHGGKG 592
Cdd:cd23439    1 ASGEIRNVGSGLCIDTKHG-GENDEVRLSKCvkDGGGGEQQFELTWHEDIRpkKRKVCFDvsshTPGAPVILYACHGMKG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 161077156 593 NQFWTYRENTKQLHHGTSGKCLAISESKDKLLMEECSASLSRQQWT 638
Cdd:cd23439   80 NQLWKYRPNTKQLYHPVSGLCLDADPGSGKVFMNHCDESSDTQKWT 125

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 1 (Pgant1) and similar proteins; Pgant1, also called pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, 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. Pgant1 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 the monoglycosylated Muc5AC-3 as a substrate. 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 161077156 518 DSVAHGEIANVPNGMCLDAKEKSEE-ETPVSIYECHGQG-GNQYWMLSKAGEIRRDDSCLDYAGKD---VTLFGCHGG-K 591
Cdd:cd23459    3 DVLAYGQVRNPGTNLCLDTLQRDEDkGYNLGLYPCQGGLsSNQLFSLSKKGELRREESCADVQGTEeskVILITCHGLeK 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161077156 592 GNQFWTYRENtKQLHHGTSGKCLAIS--ESKDKLLMEECSASLSrQQWTLEN 641
Cdd:cd23459   83 FNQKWKHTKG-GQIVHLASGKCLDAEglKSGDDVTLAKCDGSLS-QKWTFEH 132

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 161077156 523 GEIANVPNGMCLDAKEKSEEETpVSIYECHGQGGNQYWMLSKAGEIRRDDSCLDYA--GKDVTLFGCHGGKGNQFWTYRE 600
Cdd:cd23467    7 GEIRNVETNQCLDNMGRKENEK-VGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSrlNGPVVMLKCHHMRGNQLWEYDA 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 161077156 601 NTKQLHHGTSGKCLAISESKDKLL--MEECSASLSrQQWTLEN 641
Cdd:cd23467   86 ERLTLRHVNSNQCLDEPSEEDKMVptMKDCSGSRS-QQWLLRN 127

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3)-like subfamily; The GALNT3-like subfamily includes GALNT3, GALNT4, GALNT6 and GALNT12. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT3 has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. It probably glycosylates fibronectin in vivo as well as FGF23. It plays a central role in phosphate homeostasis. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT12 has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with non-glycosylated Muc2 and Muc7. It displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. It may play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs. Members of this family comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077156 520 VAHGEIANVPNGMCLDAKE-KSEEETPVSIYECHGQGGNQYWMLSKAGEIRRDDS---CLDYAGKD-VTLFGCHGGK--- 591
Cdd:cd23435    2 GYYGALRNKGSELCLDVNNpNGQGGKPVIMYGCHGLGGNQYFEYTSKGEIRHNIGkelCLHASGSDeVILQHCTSKGkdv 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 161077156 592 -GNQFWTYRENtKQLHHGTSGKCLAIseSKDKLLMEECSASLSRQQWTLE 640
Cdd:cd23435   82 pPEQKWLFTQD-GTIRNPASGLCLHA--SGYKVLLRTCNPSDDSQKWTFI 128

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). 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. Pgant8 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 both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. 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 161077156 520 VAHGEIANVPN-GMCLDAKEKSEEEtPVSIYECHG----QGGNQYWMLSKAGEIRRDDS--CLDYAGKDVTLFGCHGGKG 592
Cdd:cd23461    1 FASGVIQSVAFpNLCLDILGRSHGG-PPVLAKCSSnksmPGTFQNFSLTFHRQIKHGTSddCLEVRGNNVRLSRCHYQGG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 161077156 593 NQFWTYRENTKQLHHGTSG-KCLAISESKDKLLMEECSASLSRQQW 637
Cdd:cd23461   80 NQYWKYDYETHQLINGGQNnKCLEADVESLKITLSICDSDNVEQKW 125

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase-like 6 (GALNTL6) and similar proteins; GALNTL6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 17, GalNAc-T17, pp-GaNTase 17, protein-UDP acetylgalactosaminyltransferase 17, putative polypeptide N-acetylgalactosaminyltransferase 17, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNTL6 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077156 521 AHGEIANVPNGMCLDAKEKSEEeTPVSIYECHGQGGNQYW------MLSKAGEIRRDDS------CLDYAGKD--VTLFG 586
Cdd:cd23477    6 AWGEIRNVAANLCVDSKHGATG-TELRLDICVKDGSERTWsheqlfTFGWREDIRPGEPlhtrkfCFDAISHNspVTLYD 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077156 587 CHGGKGNQFWTYRENtKQLHHGTSGKCLAISESKDKLLMEECSASLSRQQWTLENYDSSKL 647
Cdd:cd23477   85 CHGMKGNQLWSYRKD-KTLFHPVSNSCMDCNPADKKIFMNRCDPLSETQQWIFEHTNMTVL 144

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 161077156 523 GEIANVPNGMCLDAKEKSEEE-TPVSIYECHGqGGNQYWMLSKAG----EIRRDDS--CLDYAGKD------VTLFGCHG 589
Cdd:cd00161    3 YRIVNAASGKCLDVAGGSTANgAPVQQWTCNG-GANQQWTLTPVGdgyyTIRNVASgkCLDVAGGStanganVQQWTCNG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161077156 590 GKgNQFWTYREN---TKQLHHGTSGKCLAISESKD----KLLMEECSASLSrQQW 637
Cdd:cd00161   82 GD-NQQWRLEPVgdgYYRIVNKHSGKCLDVSGGSTangaNVQQWTCNGGAN-QQW 134

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 161077156 523 GEIANVPNGMCLDAK-EKSEEETPVSIYECHGQGGNQYWMLSKAGEIRRDDS--CLDYAGKDVTLFGCHGGKGNQFWTYR 599
Cdd:cd23442    6 GQLYNTGTGYCADYIhGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSLqlCLDVRQEQVVLQNCTKEKTSQKWDFQ 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 161077156 600 EnTKQLHHGTSGKCLAISESKDK--LLMEECSaSLSRQQWT 638
Cdd:cd23442   86 E-TGRIVHILSGKCIEAVESENSklLFLSPCN-GQRNQMWK 124

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 161077156 523 GEIaNVPNGMCLDAKEKSEEETPVSIYECHGqGGNQYWMLSKAGEIRRDDSCLDYAGKD------VTLFGCHGGKgNQFW 596
Cdd:NF035930 120 REI-RGKGGLCLDVSGGLRPGNGLIVYNCNG-GENQRFTWGRGGELRVGDLCLDVADGNtrdgarVIAWSCSGGP-NQRW 196

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 161077156 597 TYRENtkQLHHGTSGKCLAISESKDK----LLMEECSASlSRQQW 637
Cdd:NF035930 197 RWRGG--QIRSRLSGKCLDIEGGRARpgqpVIVWSCNGG-PNQRW 238

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 161077156 522 HGEIANVPNGMCLDAKEKSEEETPVSIYECHGQGGNQYWMLSKAGEIRRD---DSCLDYAGKDVTLFGCH--GGK----G 592
Cdd:cd23468    5 FGAIKNVGKELCLDVGENNHGGKPLIMYNCHGLGGNQYFEYSTHHEIRHNiqkELCLHGSQGSVQLKECTykGRNtavlP 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 161077156 593 NQFWTYRENtKQLHHGTSGKCLAISESKDKLLmeECSASLSRQQWTL 639
Cdd:cd23468   85 EEKWELQKD-QLLYNPALNMCLSANGENPSLV--PCNPSDPFQQWIF 128

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 161077156 523 GEIANVPNGMCLDAKEKSEEE-TPVSIYECHGqGGNQYWMLSKAGEIR-RDDSCLD------YAGKDVTLFGCHGGkGNQ 594
Cdd:cd23418    6 GQIRGYGSGRCLDVPGGSTTNgTRLILWDCHG-GANQQFTFTSAGELRvGGDKCLDaagggtTNGTPVVIWPCNGG-ANQ 83

                         90       100
                 ....*....|....*....|
gi 161077156 595 FWTYRENtKQLHHGTSGKCL 614
Cdd:cd23418   84 KWRFNSD-GTIRNVNSGLCL 102

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal 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 bears a potential sugar binding site.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077156 523 GEIANVPNGMCLD-AKEKSEEETPVSIYECHGqGGNQYWMLSKAGEIRRDDSCLDYA------GKDVTLFGCHGGkGNQF 595
Cdd:cd23451    3 GPVRLANAGKCLDvPGSSTADGNPVQIYTCNG-TAAQKWTLGTDGTLRVLGKCLDVSgggtanGTLVQLWDCNGT-GAQK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 161077156 596 WTYRENtKQLHHGTSGKCLAISESKD----KLLMEECSASlSRQQWT 638
Cdd:cd23451   81 WVPRAD-GTLYNPQSGKCLDAPGGSTtdgtQLQLYTCNGT-AAQQWT 125

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161077156 530 NGMCLDAKEKS-EEETPVSIYECHGqGGNQYWMLSKAGEIRRDDS--CLDYA------GKDVTLFGCHGGkGNQFWT 597
Cdd:cd23418   55 GDKCLDAAGGGtTNGTPVVIWPCNG-GANQKWRFNSDGTIRNVNSglCLDVAgggtanGTRLILWSCNGG-SNQRWR 129