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 1775678398 425 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQL 504
Cdd:cd23467     1 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNQL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1775678398 505 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 551
Cdd:cd23467    81 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMKDCSGSRSQQWLLRN 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 1775678398 425 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQL 504
Cdd:cd23467     1 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNQL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1775678398 505 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 551
Cdd:cd23467    81 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMKDCSGSRSQQWLLRN 127

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLDNMGRKE-NEKVGIFNCHGMGGNQVFSYTADKEIRT--DDLCLDVSR--LNGPVIMLKCHHMRGNQLW 505
Cdd:pfam00652   3 GRIRNRASGKCLDVPGGSSaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDVGStaDGAKVVLWPCHPGNGNQRW 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1775678398 506 EYDAERLTLRHVNSNQCLDEPSEEDKMVP-TMQDC-SGSRSQQW 547
Cdd:pfam00652  83 RYDEDGTQIRNPQSGKCLDVSGAGTSNGKvILWTCdSGNPNQQW 126

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 115 PNTSVVIVFHNEAwSTLLRTVYSVINRSphYLLSEVILVDDASERDFLKLtLENYVKNLEvPVKIIRMEERSGLIRARLR 194
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQT--YPDFEIIVVDDGSTDGTAEI-LRELAAKDP-RIRVIRLERNRGKGAARNA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 195 GAAASKGQVITFLDAHCECTLGWLEPLLARIKEDrktvvcpiidvisddtfeymaGSDMTYGGFNWKLNFRWYPVPQREM 274
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEG---------------------PADLVYGSRLIREGESDLRRLGSRL 135

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1775678398 275 DRRkgdRTLPVRTPTMAGGLFSIDRNYFEEIGtYDAGM 312
Cdd:COG0463   136 FNL---VRLLTNLPDSTSGFRLFRREVLEELG-FDEGF 169

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 1775678398 425 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQL 504
Cdd:cd23467     1 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNQL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1775678398 505 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 551
Cdd:cd23467    81 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMKDCSGSRSQQWLLRN 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 1775678398 425 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQL 504
Cdd:cd23433     1 LDYYSLGEIRNVETNLCLDTMGRKAGEKVGLSSCHGQGGNQVFSYTAKGEIRSDDLCLDASRKGGPVKLEKCHGMGGNQE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1775678398 505 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 551
Cdd:cd23433    81 WEYDKETKQIRHVNSGLCLTAPNEDDPNEPVLRPCDGGPSQKWELEG 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 1775678398 431 GEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKChHMRGNQLWEYDAE 510
Cdd:cd23437     6 GEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKC-NLGETGKWEYDEA 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1775678398 511 RLTLRHVNSNQCLDEPSEEDKMvpTMQDCSGSR-SQQW 547
Cdd:cd23437    85 TGQIRHKGTGKCLDLNEGTNKL--ILQPCDSSSpSQKW 120

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLDNMGRKE-NEKVGIFNCHGMGGNQVFSYTADKEIRT--DDLCLDVSR--LNGPVIMLKCHHMRGNQLW 505
Cdd:pfam00652   3 GRIRNRASGKCLDVPGGSSaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDVGStaDGAKVVLWPCHPGNGNQRW 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1775678398 506 EYDAERLTLRHVNSNQCLDEPSEEDKMVP-TMQDC-SGSRSQQW 547
Cdd:pfam00652  83 RYDEDGTQIRNPQSGKCLDVSGAGTSNGKvILWTCdSGNPNQQW 126

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 1775678398 431 GEIRNveTNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDV--SRLNGPVIMLKCHHMRGNQLWEYD 508
Cdd:cd23434     3 GSLKQ--GNLCLDTLGHKAGGTVGLYPCHGTGGNQEWSFTKDGQIKHDDLCLTVvdRAPGSLVTLQPCREDDSNQKWEQI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1775678398 509 AERLTLRHVNSNQCLDEPSEEDKMVpTMQDCSG-SRSQQW 547
Cdd:cd23434    81 ENNSKLRHVGSNLCLDSRNAKSGGL-TVETCDPsSGSQQW 119

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 1775678398 429 SLGEIRNVETNQCLDNMGRKENEK-VGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVsRLNGPVIMLKCHHMRGNQLWEY 507
Cdd:cd23460     1 GLGQIKHTESGLCLDWAGESNGDKtVALKPCHGGGGNQFWMYTGDGQIRQDHLCLTA-DEGNKVTLRECADQLPSQEWSY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1775678398 508 DAERLTLRHVNSNQCLDEPSEEDkmVPTMQDCSGSR-SQQWLLR 550
Cdd:cd23460    80 DEKTGTIRHRSTGLCLTLDANND--VVILKECDSNSlWQKWIFQ 121

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 1775678398 424 PRRYyslGEIRNVETNQCLDNMGRKENE--KVGIFNCHGMGGNQVFSYTADKEIRTD---DLCLDVSRlNGPVIMLKCHH 498
Cdd:cd23435     1 PGYY---GALRNKGSELCLDVNNPNGQGgkPVIMYGCHGLGGNQYFEYTSKGEIRHNigkELCLHASG-SDEVILQHCTS 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1775678398 499 ----MRGNQLWEYDAERlTLRHVNSNQCLdepsEEDKMVPTMQDCSGS-RSQQWL 548
Cdd:cd23435    77 kgkdVPPEQKWLFTQDG-TIRNPASGLCL----HASGYKVLLRTCNPSdDSQKWT 126

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 1775678398 431 GEIRNVETNQCLDNMGRKENEKVGIFNC-HGMGG-----NQVFSYTADKEIRTDD------LCLDVSRLNGPVIMLKCHH 498
Cdd:cd23476     8 GEIRNVGTGLCADTKHGALGSPLRLEGCvKGRGEaawnnGQVFTFGWREDIRPGDpqhtkkFCFDAISHNSPVTLYDCHG 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1775678398 499 MRGNQLWEYDAERlTLRHVNSNQCLDEPSEEDKMVptMQDCS-GSRSQQWLL 549
Cdd:cd23476    88 MKGNQLWRYRKDK-TLYHPVSNSCMDCSESDHRIF--MNTCNpSSPTQQWLF 136

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 1775678398 429 SLGEIRNVETNQCLD--NMGRKENEKVGIFNCHGmGGNQVFSYTADKEIR-TDDLCLDVS---RLNG-PVIMLKCHHmRG 501
Cdd:cd23418     4 GGGQIRGYGSGRCLDvpGGSTTNGTRLILWDCHG-GANQQFTFTSAGELRvGGDKCLDAAgggTTNGtPVVIWPCNG-GA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1775678398 502 NQLWEYDAERlTLRHVNSNQCLDEPSEEDKMVPTMQ--DCSGSRSQQW 547
Cdd:cd23418    82 NQKWRFNSDG-TIRNVNSGLCLDVAGGGTANGTRLIlwSCNGGSNQRW 128

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 1775678398 431 GEIRNVETNQCLdnMGRKENEKVG----IFNCHGMGGNQVFSYTADKEIRTDD-LCLDVSRLNGPVIML-KCHHMRGNQL 504
Cdd:cd23440     6 GQLKHAGSGLCL--VAEDEVSQKGsllvLRPCSRNDKKQLWYYTEDGELRLANlLCLDSSETSSDFPRLmKCHGSGGSQQ 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1775678398 505 WEYDAERlTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLL 549
Cdd:cd23440    84 WRFKKDN-RLYNPASGQCLAASKNGTSGYVTMDICSDSPSQKWVF 127

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 1775678398 429 SLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGN------QVFSYTADKEIR------TDDLCLDVSRLNGPVIMLKC 496
Cdd:cd23477     6 AWGEIRNVAANLCVDSKHGATGTELRLDICVKDGSErtwsheQLFTFGWREDIRpgeplhTRKFCFDAISHNSPVTLYDC 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1775678398 497 HHMRGNQLWEYDAERlTLRHVNSNQCLDEPSEEDKMVptMQDCS-GSRSQQWLLR--NMTL 554
Cdd:cd23477    86 HGMKGNQLWSYRKDK-TLFHPVSNSCMDCNPADKKIF--MNRCDpLSETQQWIFEhtNMTV 143

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 426 RYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTAD-KEIR--TDDLCLDVSR---LNGPVIMLKCHHM 499
Cdd:pfam00652  41 TLTGDGTIRSVASDLCLDVGSTADGAKVVLWPCHPGNGNQRWRYDEDgTQIRnpQSGKCLDVSGagtSNGKVILWTCDSG 120

                  ....*.
gi 1775678398 500 RGNQLW 505
Cdd:pfam00652 121 NPNQQW 126

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 115 PNTSVVIVFHNEAwSTLLRTVYSVINRSphYLLSEVILVDDASERDFLKLtLENYVKNLEvPVKIIRMEERSGLIRARLR 194
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQT--YPDFEIIVVDDGSTDGTAEI-LRELAAKDP-RIRVIRLERNRGKGAARNA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 195 GAAASKGQVITFLDAHCECTLGWLEPLLARIKEDrktvvcpiidvisddtfeymaGSDMTYGGFNWKLNFRWYPVPQREM 274
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEG---------------------PADLVYGSRLIREGESDLRRLGSRL 135

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1775678398 275 DRRkgdRTLPVRTPTMAGGLFSIDRNYFEEIGtYDAGM 312
Cdd:COG0463   136 FNL---VRLLTNLPDSTSGFRLFRREVLEELG-FDEGF 169

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 115 PNTSVVIVFHNEaWSTLLRTVYSVINRSphYLLSEVILVDDASERDFLkltleNYVKNLEVP-VKIIRMEERSGLIRARL 193
Cdd:COG1216     3 PKVSVVIPTYNR-PELLRRCLESLLAQT--YPPFEVIVVDNGSTDGTA-----ELLAALAFPrVRVIRNPENLGFAAARN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 194 RGAAASKGQVITFLDAHCECTLGWLEPLLArikedrktvvcpiidvisddtfeymagsdmtyggfnwklnfrwypvpqre 273
Cdd:COG1216    75 LGLRAAGGDYLLFLDDDTVVEPDWLERLLA-------------------------------------------------- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 274 mdrrkgdrtlpvrtptmAGGLFsIDRNYFEEIGTYDAGMDIWGGEnLEMSFRIWQCGGSLEIVTCSHVGHVFRKAtpyTF 353
Cdd:COG1216   105 -----------------AACLL-IRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGAS---SG 162

                         250       260       270
                  ....*....|....*....|....*....|
gi 1775678398 354 PGGTGHVINKNNRRLAEVWMDEFKDFFYII 383
Cdd:COG1216   163 PLLRAYYLGRNRLLFLRKHGPRPLLRLALL 192

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 1775678398 431 GEIRNveTNQCLDNMGRK--ENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDV--SRLNGPVIMLKCHHmRGNQLWE 506
Cdd:cd23441     6 GQIKQ--GNLCLDSDEQLfqGPALLILAPCSNSSDSQEWSFTKDGQLQTQGLCLTVdsSSKDLPVVLETCSD-DPKQKWT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1775678398 507 YdaERLTLRHVNSNQCLDEPSeedKMVPTMQDC-SGSRSQQW 547
Cdd:cd23441    83 R--TGRQLVHSESGLCLDSRK---KKGLVVSPCrSGAPSQKW 119

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 1775678398 431 GEIRNVE-TNQCLDNMGRKEN---EKVGIFNCHGMGGNQVFSYTADKEIRTD---DLCLDVSRLNGPVIMLKCHH----M 499
Cdd:cd23469     5 GAVRSMGiSSECLDYNSPEHNptgAHLSLFGCHGQGGNQFFEYTSNKEIRFNsvtELCAEVPDQKNYIGMKHCPKdgspV 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1775678398 500 RGNQLWEYdAERLTLRHVNSNQCLDE-PSEEDKMVPTMQDCS-GSRSQQW 547
Cdd:cd23469    85 PANIIWHF-KEDGTIYHPHSGMCISAyRTPEGRADVQMRTCDaGDKNQLW 133

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 433 IRNVETNQCLDNmgrKENEKVGIFNCHGmGGNQVFSYTADKE-------IRTdDLCLDvSRLNGPVIMLKCHHMRgNQLW 505
Cdd:cd23415     5 LRNVATGRCLDS---NAGGNVYTGPCNG-GPYQRWTWSGVGDgtvtlrnAAT-GRCLD-SNGNGGVYTLPCNGGS-YQRW 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1775678398 506 E---YDAERLTLRHVNSNQCLDepSEEDKMVpTMQDCSGSRSQQW 547
Cdd:cd23415    78 RvtsTSGGGVTLRNVATGRCLD--SNGSGGV-YTRPCNGGSYQRW 119

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 1775678398 479 DLCLDV---SRLNG-PVIMLKCHHmRGNQLWEYDAERL---TLRHVNSNQCLD--EPSEEDKMVPTMQDCSGSRSQQWLL 549
Cdd:cd00161    11 GKCLDVaggSTANGaPVQQWTCNG-GANQQWTLTPVGDgyyTIRNVASGKCLDvaGGSTANGANVQQWTCNGGDNQQWRL 89

                  ....*..
gi 1775678398 550 RNMTLGT 556
Cdd:cd00161    90 EPVGDGY 96