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 1775984935 343 SYPQIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQLWEYD 422
Cdd:cd23467     5 SLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNQLWEYD 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1775984935 423 AERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 465
Cdd:cd23467    85 AERLTLRHVNSNQCLDEPSEEDKMVPTMKDCSGSRSQQWLLRN 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 1775984935 343 SYPQIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQLWEYD 422
Cdd:cd23467     5 SLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNQLWEYD 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1775984935 423 AERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 465
Cdd:cd23467    85 AERLTLRHVNSNQCLDEPSEEDKMVPTMKDCSGSRSQQWLLRN 127

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775984935 346 QIRNVETNQCLDNMGRKE-NEKVGIFNCHGMGGNQVFSYTADKEIRT--DDLCLDVSR--LNGPVIMLKCHHMRGNQLWE 420
Cdd:pfam00652   4 RIRNRASGKCLDVPGGSSaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDVGStaDGAKVVLWPCHPGNGNQRWR 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1775984935 421 YDAERLTLRHVNSNQCLDEPSEEDKMVP-TMQDC-SGSRSQQW 461
Cdd:pfam00652  84 YDEDGTQIRNPQSGKCLDVSGAGTSNGKvILWTCdSGNPNQQW 126

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775984935  347 IRNVETNQCLDNMGRKENekVGIFNCHGMGGNQVFSYTADKEIRT--DDLCLDVSRLNG-PVIMLKCHHMRGNQLWEYDA 423
Cdd:smart00458   1 IISGNTGKCLDVNGNKNP--VGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGsTVTLYSCDGTNDNQYWEVNK 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1775984935  424 ERlTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLR 464
Cdd:smart00458  79 DG-TIRNPDSGKCLDVKDGNTGTKVILWTCSGNPNQKWIFE 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 1775984935 346 QIRnVETNQCLDNMGR-KENEKVGIFNCHGmGGNQVFSYTADKEIRTDDLCLDVSRLN----GPVIMLKCHHMRgNQLWe 420
Cdd:NF035930  121 EIR-GKGGLCLDVSGGlRPGNGLIVYNCNG-GENQRFTWGRGGELRVGDLCLDVADGNtrdgARVIAWSCSGGP-NQRW- 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1775984935 421 yDAERLTLRHVNSNQCLDepSEEDKMVP----TMQDCSGSRSQQW 461
Cdd:NF035930  197 -RWRGGQIRSRLSGKCLD--IEGGRARPgqpvIVWSCNGGPNQRW 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 1775984935 343 SYPQIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQLWEYD 422
Cdd:cd23467     5 SLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNQLWEYD 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1775984935 423 AERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 465
Cdd:cd23467    85 AERLTLRHVNSNQCLDEPSEEDKMVPTMKDCSGSRSQQWLLRN 127

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1) and similar proteins; GALNT1 (EC 2.4.1.41), also called polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, 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 broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT1 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 is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775984935 343 SYPQIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQLWEYD 422
Cdd:cd23466     5 SLGEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDDLCLDVSKLNGPVMMLKCHHLKGNQLWEYD 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1775984935 423 AERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 465
Cdd:cd23466    85 PVKLTLLHVNSNQCLDKATEEDSQVPSIRDCNGSRSQQWLLRN 127

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775984935 346 QIRNVETNQCLDNMGRK--ENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQLWEYDA 423
Cdd:cd23462     7 EIRNLAGKLCLDAPGRKkeLNKPVGLYPCHGQGGNQYWMLTKDGEIRRDDLCLDYAGGSGDVTLYPCHGMKGNQFWIYDE 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1775984935 424 ERLTLRHVNSNQCLDepSEEDKMVPTMQDCSG-SRSQQWLLR 464
Cdd:cd23462    87 ETKQIVHGTSKKCLE--LSDDSSKLVMEPCNGsSPRQQWEFE 126

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775984935 346 QIRNVETNQCLDNMGRKE-NEKVGIFNCHGMGGNQVFSYTADKEIRT--DDLCLDVSR--LNGPVIMLKCHHMRGNQLWE 420
Cdd:pfam00652   4 RIRNRASGKCLDVPGGSSaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDVGStaDGAKVVLWPCHPGNGNQRWR 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1775984935 421 YDAERLTLRHVNSNQCLDEPSEEDKMVP-TMQDC-SGSRSQQW 461
Cdd:pfam00652  84 YDEDGTQIRNPQSGKCLDVSGAGTSNGKvILWTCdSGNPNQQW 126

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775984935  347 IRNVETNQCLDNMGRKENekVGIFNCHGMGGNQVFSYTADKEIRT--DDLCLDVSRLNG-PVIMLKCHHMRGNQLWEYDA 423
Cdd:smart00458   1 IISGNTGKCLDVNGNKNP--VGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGsTVTLYSCDGTNDNQYWEVNK 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1775984935  424 ERlTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLR 464
Cdd:smart00458  79 DG-TIRNPDSGKCLDVKDGNTGTKVILWTCSGNPNQKWIFE 118

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 1775984935 341 STSYPQIRNVETNQCLDNMGRKENEK--VGIFNCHGMG-GNQVFSYTADKEIRTDDLCLDVS-RLNGPVIMLKCHH-MRG 415
Cdd:cd23459     4 VLAYGQVRNPGTNLCLDTLQRDEDKGynLGLYPCQGGLsSNQLFSLSKKGELRREESCADVQgTEESKVILITCHGlEKF 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1775984935 416 NQLWEYDAERlTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQW 461
Cdd:cd23459    84 NQKWKHTKGG-QIVHLASGKCLDAEGLKSGDDVTLAKCDGSLSQKW 128

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 1775984935 346 QIRNVETNQCLDNMGRKENEK-VGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVsRLNGPVIMLKCHHMRGNQLWEYDAE 424
Cdd:cd23460     4 QIKHTESGLCLDWAGESNGDKtVALKPCHGGGGNQFWMYTGDGQIRQDHLCLTA-DEGNKVTLRECADQLPSQEWSYDEK 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1775984935 425 RLTLRHVNSNQCLDEPSEEDkmVPTMQDCSGSR-SQQWLLR 464
Cdd:cd23460    83 TGTIRHRSTGLCLTLDANND--VVILKECDSNSlWQKWIFQ 121

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 1775984935 346 QIRNVETNQCLDNM--GRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDD--LCLDVSrlNGPVIMLKCHHMRGNQLWEY 421
Cdd:cd23442     7 QLYNTGTGYCADYIhgWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSlqLCLDVR--QEQVVLQNCTKEKTSQKWDF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1775984935 422 DAERlTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQW 461
Cdd:cd23442    85 QETG-RIVHILSGKCIEAVESENSKLLFLSPCNGQRNQMW 123

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 1775984935 345 PQIRNVETNQCLD--NMGRKENEKVGIFNCHGmGGNQVFSYTADKEIR-TDDLCLDVS---RLNG-PVIMLKCHHmRGNQ 417
Cdd:cd23418     6 GQIRGYGSGRCLDvpGGSTTNGTRLILWDCHG-GANQQFTFTSAGELRvGGDKCLDAAgggTTNGtPVVIWPCNG-GANQ 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1775984935 418 LWEYDAERlTLRHVNSNQCLDEPSEEDKMVPTMQ--DCSGSRSQQW 461
Cdd:cd23418    84 KWRFNSDG-TIRNVNSGLCLDVAGGGTANGTRLIlwSCNGGSNQRW 128

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 1775984935 342 TSYPQIRNVETNQCLDnMGrkENEKVG----IFNCHGMGGNQVFSYTADKEIRTD---DLCLDVSRlnGPVIMLKCHH-- 412
Cdd:cd23470     2 TFYGAIKNEGTNQCLD-VG--ENNRGGkpliMYSCHGMGGNQYFEYTTHKELRHNiakQLCLRVSK--GPVQLGECHYkg 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1775984935 413 ----MRGNQLWEYDAERLtLRHVNSNQCLDEPSEEdkmvPTMQDCSGSRSQQ-WL 462
Cdd:cd23470    77 knsqVPPDEEWELTQDHL-IRNSGSNMCLTARGKH----PAMAPCNPADPHQlWS 126

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 1775984935 346 QIRNVETNQCLDNMGRK--ENEKVGIFNCHGmGGNQVFSYTADKEIRTDDLCLDVSR---LNG-PVIMLKCHHMrGNQLW 419
Cdd:cd23451     4 PVRLANAGKCLDVPGSStaDGNPVQIYTCNG-TAAQKWTLGTDGTLRVLGKCLDVSGggtANGtLVQLWDCNGT-GAQKW 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1775984935 420 EYDAERlTLRHVNSNQCLDEPSeeDKMVPTMQ----DCSGSRSQQW 461
Cdd:cd23451    82 VPRADG-TLYNPQSGKCLDAPG--GSTTDGTQlqlyTCNGTAAQQW 124

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775984935 115 PNTSVVIVFHNEAwSTLLRTVYSVIN-RSPHYllsEVILVDDASERDFLKLtLENYVKNLEvPVKIIRMEERSGLIRARL 193
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAqTYPDF---EIIVVDDGSTDGTAEI-LRELAAKDP-RIRVIRLERNRGKGAARN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775984935 194 RGAAASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMAGSDMTYgGFNWKLNFRWYPVPQRE 273
Cdd:COG0463    76 AGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLTNLPDSTSGFRL 154

                  ....
gi 1775984935 274 MDRR 277
Cdd:COG0463   155 FRRE 158

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 1775984935 347 IRNVETNQCLDNMGRKENEKVGI-FNCHGMGGNQVFSYTADKEIRTD---DLCLDVSRlnGPVIMLKCHH------MRGN 416
Cdd:cd23468     8 IKNVGKELCLDVGENNHGGKPLImYNCHGLGGNQYFEYSTHHEIRHNiqkELCLHGSQ--GSVQLKECTYkgrntaVLPE 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1775984935 417 QLWEYDAERLtLRHVNSNQCLDEPSEEDKMVPtmqdCSGSRS-QQWLLR 464
Cdd:cd23468    86 EKWELQKDQL-LYNPALNMCLSANGENPSLVP----CNPSDPfQQWIFR 129

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775984935 115 PNTSVVIVFHNEaWSTLLRTVYSVINRSphYLLSEVILVDDASERDFLkltleNYVKNLEVP-VKIIRMEERSGLIRARL 193
Cdd:COG1216     3 PKVSVVIPTYNR-PELLRRCLESLLAQT--YPPFEVIVVDNGSTDGTA-----ELLAALAFPrVRVIRNPENLGFAAARN 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1775984935 194 RGAAASKGQVITFLDAHCECTLGWLEPLLA 223
Cdd:COG1216    75 LGLRAAGGDYLLFLDDDTVVEPDWLERLLA 104

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 1775984935 344 YPQIRNveTNQCLDNMGRK--ENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDV--SRLNGPVIMLKCHHmRGNQLW 419
Cdd:cd23441     5 YGQIKQ--GNLCLDSDEQLfqGPALLILAPCSNSSDSQEWSFTKDGQLQTQGLCLTVdsSSKDLPVVLETCSD-DPKQKW 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1775984935 420 EYdaERLTLRHVNSNQCLDEPSeedKMVPTMQDC-SGSRSQQW 461
Cdd:cd23441    82 TR--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 1775984935 352 TNQCLDNMGRKEN---EKVGIFNCHGMGGNQVFSYTADKEIRTD---DLCLDVSRLNGPVIMLKCHH----MRGNQLWEY 421
Cdd:cd23469    13 SSECLDYNSPEHNptgAHLSLFGCHGQGGNQFFEYTSNKEIRFNsvtELCAEVPDQKNYIGMKHCPKdgspVPANIIWHF 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1775984935 422 dAERLTLRHVNSNQCLDE-PSEEDKMVPTMQDCS-GSRSQQW 461
Cdd:cd23469    93 -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 1775984935 346 QIRNVETNQCLDNmgrKENEKVGIFNCHGmGGNQVFSYTADKE-------IRTdDLCLDvSRLNGPVIMLKCHHMRgNQL 418
Cdd:cd23415     4 RLRNVATGRCLDS---NAGGNVYTGPCNG-GPYQRWTWSGVGDgtvtlrnAAT-GRCLD-SNGNGGVYTLPCNGGS-YQR 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1775984935 419 WE---YDAERLTLRHVNSNQCLDepSEEDKMVpTMQDCSGSRSQQW 461
Cdd:cd23415    77 WRvtsTSGGGVTLRNVATGRCLD--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 1775984935 393 DLCLDV---SRLNG-PVIMLKCHHmRGNQLWEYDAERL---TLRHVNSNQCLD--EPSEEDKMVPTMQDCSGSRSQQWLL 463
Cdd:cd00161    11 GKCLDVaggSTANGaPVQQWTCNG-GANQQWTLTPVGDgyyTIRNVASGKCLDvaGGSTANGANVQQWTCNGGDNQQWRL 89

                  ....*..
gi 1775984935 464 RNMTLGT 470
Cdd:cd00161    90 EPVGDGY 96

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775984935 119 VVIVFHNEAwSTLLRTVYSVINRS-PHYLLsEVILVDDASERDFLKLtLENYVKNLEVPVKIIRMEER--SGLIRARLRG 195
Cdd:cd04192     1 VVIAARNEA-ENLPRLLQSLSALDyPKEKF-EVILVDDHSTDGTVQI-LEFAAAKPNFQLKILNNSRVsiSGKKNALTTA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1775984935 196 AAASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTF-------EYMAGSDMTYGGFNWKLNF 264
Cdd:cd04192    78 IKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFKGKSLlakfqrlDWLSLLGLIAGSFGLGKPF 153

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775984935 317 ALVMSSTRTTGDWQKFGWMNLkiSSTSYpQIRNVETNQCLD--NMGRKENEKVGIFNCHGmGGNQVFSYTA----DKEIR 390
Cdd:cd00161    25 APVQQWTCNGGANQQWTLTPV--GDGYY-TIRNVASGKCLDvaGGSTANGANVQQWTCNG-GDNQQWRLEPvgdgYYRIV 100

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1775984935 391 T--DDLCLDV---SRLNG-PVIMLKCHHmRGNQLW 419
Cdd:cd00161   101 NkhSGKCLDVsggSTANGaNVQQWTCNG-GANQQW 134

ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1775984935 393 DLCLDVS---RLNGPVIMLKCHHmRGNQLWEYDAERLTLRHVNSNQCLD---EPSEEDKMVptMQDCSGSRSQQW 461
Cdd:cd23456    11 GLCLDVSggaTNGANVVVYDCNN-SNSQKWYYDATGRLHSKANPGKCLDaggENSNGANVV--LWACNDSANQRW 82