ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14) and similar proteins; GALNT14 (EC 2.4.1.41), also called polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, protein-UDP acetylgalactosaminyltransferase 14, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. GALNT14 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024394911 335 IPEELLYQTGMIRQRQSCLESHKSEDQELPILSLNPCITSKGTSATAQEWTYTYNHQVRQQQLCLSVYTLFPGSPVLLSP 414
Cdd:cd23478     1 IPDESDIQSGVIRQRQNCLESRRVEGQELPNLSLSPCIKSKGVPAKSQEWAYTYNQQIRQQQLCLSVHTLFPGSPVVLVP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024394911 415 CKESDNKqQQWGKVGSHLEHIASRFCLDTETVGDTNESTKELVINPCESTSMSQRWDMVMS 475
Cdd:cd23478    81 CKEGDGK-QRWTKVGSHIEHMASRFCLDTEMFGDGTESSKEIVINPCESSAMSQRWDMVLS 140

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14) and similar proteins; GALNT14 (EC 2.4.1.41), also called polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, protein-UDP acetylgalactosaminyltransferase 14, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. GALNT14 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024394911 335 IPEELLYQTGMIRQRQSCLESHKSEDQELPILSLNPCITSKGTSATAQEWTYTYNHQVRQQQLCLSVYTLFPGSPVLLSP 414
Cdd:cd23478     1 IPDESDIQSGVIRQRQNCLESRRVEGQELPNLSLSPCIKSKGVPAKSQEWAYTYNQQIRQQQLCLSVHTLFPGSPVVLVP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024394911 415 CKESDNKqQQWGKVGSHLEHIASRFCLDTETVGDTNESTKELVINPCESTSMSQRWDMVMS 475
Cdd:cd23478    81 CKEGDGK-QRWTKVGSHIEHMASRFCLDTEMFGDGTESSKEIVINPCESSAMSQRWDMVLS 140

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024394911 343 TGMIRQRQS--CLEShKSEDQELPILSLNPCitskGTSATAQEWTYTYNHQVRQ--QQLCLSVYTLFPGSPVLLSPCkES 418
Cdd:pfam00652   2 TGRIRNRASgkCLDV-PGGSSAGGPVGLYPC----HGSNGNQLWTLTGDGTIRSvaSDLCLDVGSTADGAKVVLWPC-HP 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024394911 419 DNKQQQW--GKVGSHLEHIASRFCLDtetVGDTNESTKELVINPCESTSMSQRW 470
Cdd:pfam00652  76 GNGNQRWryDEDGTQIRNPQSGKCLD---VSGAGTSNGKVILWTCDSGNPNQQW 126

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024394911  366 LSLNPCITSKGtsatAQEWTYTYNHQVRQQ--QLCLSVYTLfPGSPVLLSPCKESDNKQQ-QWGKVGShLEHIASRFCLD 442
Cdd:smart00458  19 VGLFDCHGTGG----NQLWKLTSDGAIRIKdtDLCLTANGN-TGSTVTLYSCDGTNDNQYwEVNKDGT-IRNPDSGKCLD 92

                           90       100
                   ....*....|....*....|....*...
gi 2024394911  443 TetvgDTNESTKELVINPCESTSmSQRW 470
Cdd:smart00458  93 V----KDGNTGTKVILWTCSGNP-NQKW 115

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14) and similar proteins; GALNT14 (EC 2.4.1.41), also called polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, protein-UDP acetylgalactosaminyltransferase 14, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. GALNT14 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024394911 335 IPEELLYQTGMIRQRQSCLESHKSEDQELPILSLNPCITSKGTSATAQEWTYTYNHQVRQQQLCLSVYTLFPGSPVLLSP 414
Cdd:cd23478     1 IPDESDIQSGVIRQRQNCLESRRVEGQELPNLSLSPCIKSKGVPAKSQEWAYTYNQQIRQQQLCLSVHTLFPGSPVVLVP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024394911 415 CKESDNKqQQWGKVGSHLEHIASRFCLDTETVGDTNESTKELVINPCESTSMSQRWDMVMS 475
Cdd:cd23478    81 CKEGDGK-QRWTKVGSHIEHMASRFCLDTEMFGDGTESSKEIVINPCESSAMSQRWDMVLS 140

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 16 (GALNT16) and similar proteins; GALNT16 (EC 2.4.1.41), also called polypeptide GalNAc transferase 16, GalNAc-T16, polypeptide GalNAc transferase-like protein 1, GalNAc-T-like protein 1, pp-GaNTase-like protein 1, polypeptide N-acetylgalactosaminyltransferase-like protein 1, protein-UDP acetylgalactosaminyltransferase-like protein 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. GALNT16 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 2024394911 344 GMIRQRQSCLESHKSEDQELPILSLNPCITSKGTSATAQEWTYTyNHQVRQQQLCLSVYTLFPGSPVLLSPCKESDNKqQ 423
Cdd:cd23479     8 GLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASQEWVLS-DPLIRQQDKCLAITSFSPGSKVILELCNQKDGR-Q 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2024394911 424 QWGKVGSHLEHIASRFCLDTEtvgdtnesTKELVINPCESTSMSQRWDM 472
Cdd:cd23479    86 KWKLKGSFIQHQVSGLCLDSQ--------SGRVVINQCQADLASQQWEL 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 2024394911 344 GMIRQRQSCLES--HKSEDQelpiLSLNPCITSKGTsataQEWTYTYNHQVRQQQLCLSVYTLFPGSPVLLSPCKESDNK 421
Cdd:cd23434     3 GSLKQGNLCLDTlgHKAGGT----VGLYPCHGTGGN----QEWSFTKDGQIKHDDLCLTVVDRAPGSLVTLQPCREDDSN 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024394911 422 QQ-QWGKVGSHLEHIASRFCLDTetvgdTNESTKELVINPCESTSMSQRWD 471
Cdd:cd23434    75 QKwEQIENNSKLRHVGSNLCLDS-----RNAKSGGLTVETCDPSSGSQQWK 120

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10)-like subfamily; The GALNT10-like subfamily includes GALNT10 and GALNTL6. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024394911 344 GMIRQRQS--CLES-HKSEDQELpilSLNPCItsKGTSATAQEWTYTYNHQVRQ--QQLCLSVYTLFPGSPVLLSPCKES 418
Cdd:cd23439     3 GEIRNVGSglCIDTkHGGENDEV---RLSKCV--KDGGGGEQQFELTWHEDIRPkkRKVCFDVSSHTPGAPVILYACHGM 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024394911 419 dnKQQQWGK---VGSHLEHIASRFCLDTetvgdtNESTKELVINPCESTSMSQRW 470
Cdd:cd23439    78 --KGNQLWKyrpNTKQLYHPVSGLCLDA------DPGSGKVFMNHCDESSDTQKW 124

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 2024394911 344 GMIRQRQS--CLESHKSEDQElPILSLNPCITSKGTsataQEWTYTYNHQVRQQQLCLSVytlFPGSPVLLSPCkESDNK 421
Cdd:cd23460     3 GQIKHTESglCLDWAGESNGD-KTVALKPCHGGGGN----QFWMYTGDGQIRQDHLCLTA---DEGNKVTLREC-ADQLP 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024394911 422 QQQW--GKVGSHLEHIASRFCLdtetvgDTNESTKELVINPCESTSMSQRWDM 472
Cdd:cd23460    74 SQEWsyDEKTGTIRHRSTGLCL------TLDANNDVVILKECDSNSLWQKWIF 120

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024394911  33 PPTSIVITFHNEARsTLLRTIRSVMNRTPVHLihEIILV------------DdfsddpddcRLLAKLPKVKCLRNRQREG 100
Cdd:COG0463     2 PLVSVVIPTYNEEE-YLEEALESLLAQTYPDF--EIIVVddgstdgtaeilR---------ELAAKDPRIRVIRLERNRG 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2024394911 101 LIRSRIQGADVAQAGVLTFLDSHCEVNKDWLLPLLQRIKEDPTRVV 146
Cdd:COG0463    70 KGAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024394911  37 IVITFHNEARsTLLRTIRSVMNRTpvHLIHEIILV---DDFSDDPDDCRLLAKLPKVKCLRNRQREGLIRSRIQGADVAQ 113
Cdd:cd00761     1 VIIPAYNEEP-YLERCLESLLAQT--YPNFEVIVVddgSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2024394911 114 AGVLTFLDSHCEVNKDWLLPLLQRIKEDPTRVV 146
Cdd:cd00761    78 GEYILFLDADDLLLPDWLERLVAELLADPEADA 110

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 2024394911 382 QEWTYTYNHQVRQQQLCLSVYTlfPGSPVLLSPCKESDnKQQQW--GKVGSHLEHIASRFCLDTETVGDTNestkELVIN 459
Cdd:cd23433    41 QVFSYTAKGEIRSDDLCLDASR--KGGPVKLEKCHGMG-GNQEWeyDKETKQIRHVNSGLCLTAPNEDDPN----EPVLR 113

                          90
                  ....*....|...
gi 2024394911 460 PCESTSmSQRWDM 472
Cdd:cd23433   114 PCDGGP-SQKWEL 125

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024394911  36 SIVITFHNEARsTLLRTIRSVMNRTPVHLIHEIILV---DDFSDDPDDCRLLAKLPKVKCLRNRQReglIRS--RIQGAD 110
Cdd:cd02525     3 SIIIPVRNEEK-YIEELLESLLNQSYPKDLIEIIVVdggSTDGTREIVQEYAAKDPRIRLIDNPKR---IQSagLNIGIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024394911 111 VAQAGVLTFLDSHCEVNKDWLLPLLQRIKEDPTRVVSPVIDIINLDTFAYVAA---SSDLRGGFdwSLHfkweqlspeqk 187
Cdd:cd02525    79 NSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIAvaqSSPLGSGG--SAY----------- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024394911 188 akRLDPTKPIKTPIIAGGLFviDKAWFNHLGKYDNAMDIwgGENFEISFRVWMCGGSLEIIPCSRVGHVFR 258
Cdd:cd02525   146 --RGGAVKIGYVDTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPR 210

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-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. One member of this family, MRC1, is missing the gamma subdomain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024394911 345 MIRQRQS--CLESHKSEDQelpiLSLNPCitskGTSATAQEWTYTYNHQVRQQ--QLCLSVYTLFPGSPVLLSPCKESDN 420
Cdd:cd23385     4 LIYNEDLgkCLAARSSSSK----VSLSTC----NPNSPNQQWKWTSGHRLFNVgtGKCLGVSSSSPSSPLRLFECDSEDE 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024394911 421 KqQQWgKVGSHLEHIASRFCLDTETVGDTNESTkelvinPCESTSMSQRW 470
Cdd:cd23385    76 L-QKW-KCSKDGLLLLKGLGLLLLYDKSGKNVV------VSKGSGLSSRW 117

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 2024394911 341 YQTGMIRQRQS--CL--ESHKSEDQELpiLSLNPCitsKGTSATaQEWTYTYNHQVR-QQQLCLSVYTlFPGSPVLLSPC 415
Cdd:cd23440     3 IRKGQLKHAGSglCLvaEDEVSQKGSL--LVLRPC---SRNDKK-QLWYYTEDGELRlANLLCLDSSE-TSSDFPRLMKC 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024394911 416 KESDNKQQ-QWGKVGsHLEHIASRFCLdtetVGDTNESTKELVINPCESTSmSQRWDM 472
Cdd:cd23440    76 HGSGGSQQwRFKKDN-RLYNPASGQCL----AASKNGTSGYVTMDICSDSP-SQKWVF 127

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 2024394911 366 LSLNPCitskgTSATAQEWTYTYNHQVRQQ-QLCLSVYTL--FPGSPVLLSPCKESDNKQQQWGKVGShLEHIASRFCLD 442
Cdd:cd23418    30 LILWDC-----HGGANQQFTFTSAGELRVGgDKCLDAAGGgtTNGTPVVIWPCNGGANQKWRFNSDGT-IRNVNSGLCLD 103

                          90       100
                  ....*....|....*....|....*...
gi 2024394911 443 TEtvGDTNESTKELVINPCESTSmSQRW 470
Cdd:cd23418   104 VA--GGGTANGTRLILWSCNGGS-NQRW 128

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 2024394911 342 QTGMIRQRQS--CLESHKSEDQELPILSLNPCITSKGtsatAQEWTYTYNHQVR---QQQLCLSVYtlfPGSPVLLSPCk 416
Cdd:cd23435     3 YYGALRNKGSelCLDVNNPNGQGGKPVIMYGCHGLGG----NQYFEYTSKGEIRhniGKELCLHAS---GSDEVILQHC- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024394911 417 ESDNK----QQQWGKV-GSHLEHIASRFCLDTetvgdtneSTKELVINPCESTSMSQRW 470
Cdd:cd23435    75 TSKGKdvppEQKWLFTqDGTIRNPASGLCLHA--------SGYKVLLRTCNPSDDSQKW 125

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024394911  345 MIRQRQSCLESHKSEDQelpILSLNPCITSKGtsatAQEWTYTYNHQVRQQQ--LCLSVYTLFPGSPVLLSPCKESDNkq 422
Cdd:smart00458  42 RIKDTDLCLTANGNTGS---TVTLYSCDGTND----NQYWEVNKDGTIRNPDsgKCLDVKDGNTGTKVILWTCSGNPN-- 112

                   ...
gi 2024394911  423 QQW 425
Cdd:smart00458 113 QKW 115

GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; Gellin proteins act as central effectors of wound-induced protoplasmic gelation. They possess ten related N-terminal beta-trefoil domains (Gll-1 to Gll-10) that contribute to distinct gelation-related activities. The beta-trefoil domains show low sequence similarity to members of the functionally diverse ricin B lectin domain family. They 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. Each subdomain bears a potential sugar binding site. Gellin from M. circinelloides has been called GellinA (also known as GllA). The model corresponds to GllA-1 domain, which is a remote family member of the ricin B-type lectin domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024394911 391 QVRQQQLCLSVYTLF--PGSPVLLSPCKESDNKQQQWGKVGSHLEHIASRFCLDTEtvGDTNESTKELVINPCESTSMS- 467
Cdd:cd23454     6 KSSSNGLVLDVEHGSlkSGAKVVLAPLKTKDYESQLWRYDDGYLVNKASGLVLDIQ--GGVVKSGTRLVQSPKKPSKDAn 83

                  ....
gi 2024394911 468 -QRW 470
Cdd:cd23454    84 nQRW 87