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 968115045 465 KNVKAWGRIKAVHANLCADDLLSNNEKPYNLGLYPCGKELQKSQLFSYTKSQVLRNEISCATVQHSSspPYRIVMVPCLE 544
Cdd:cd23459    2 EDVLAYGQVRNPGTNLCLDTLQRDEDKGYNLGLYPCQGGLSSNQLFSLSKKGELRREESCADVQGTE--ESKVILITCHG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 968115045 545 NDDYNEQWKYE-NQQLVHSNTGMCLDHEGLKSMDDAQVAPCDLtSETQRWIIGH 597
Cdd:cd23459   80 LEKFNQKWKHTkGGQIVHLASGKCLDAEGLKSGDDVTLAKCDG-SLSQKWTFEH 132

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 968115045 465 KNVKAWGRIKAVHANLCADDLLSNNEKPYNLGLYPCGKELQKSQLFSYTKSQVLRNEISCATVQHSSspPYRIVMVPCLE 544
Cdd:cd23459    2 EDVLAYGQVRNPGTNLCLDTLQRDEDKGYNLGLYPCQGGLSSNQLFSLSKKGELRREESCADVQGTE--ESKVILITCHG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 968115045 545 NDDYNEQWKYE-NQQLVHSNTGMCLDHEGLKSMDDAQVAPCDLtSETQRWIIGH 597
Cdd:cd23459   80 LEKFNQKWKHTkGGQIVHLASGKCLDAEGLKSGDDVTLAKCDG-SLSQKWTFEH 132

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968115045  469 AWGRIKAVHANLCADDLlSNNEKPYNLGLYPCGKELQKsQLFSYTKSQVLRNEIS--CATVqHSSSPPYRIVMVPCLEND 546
Cdd:pfam00652   1 ATGRIRNRASGKCLDVP-GGSSAGGPVGLYPCHGSNGN-QLWTLTGDGTIRSVASdlCLDV-GSTADGAKVVLWPCHPGN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 968115045  547 DyNEQWKYE--NQQLVHSNTGMCLD-HEGLKSMDDAQVAPCDLTSETQRW 593
Cdd:pfam00652  78 G-NQRWRYDedGTQIRNPQSGKCLDvSGAGTSNGKVILWTCDSGNPNQQW 126

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968115045   479 NLCADDLLSNNekpyNLGLYPCgKELQKSQLFSYTKSQVLRNEIS--CATVqhSSSPPYRIVMVPClENDDYNEQWKYE- 555
Cdd:smart00458   7 GKCLDVNGNKN----PVGLFDC-HGTGGNQLWKLTSDGAIRIKDTdlCLTA--NGNTGSTVTLYSC-DGTNDNQYWEVNk 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 968115045   556 NQQLVHSNTGMCLDHEGLKSMDDAQVAPCDLTSeTQRWII 595
Cdd:smart00458  79 DGTIRNPDSGKCLDVKDGNTGTKVILWTCSGNP-NQKWIF 117

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 968115045 465 KNVKAWGRIKAVHANLCADDLLSNNEKPYNLGLYPCGKELQKSQLFSYTKSQVLRNEISCATVQHSSspPYRIVMVPCLE 544
Cdd:cd23459    2 EDVLAYGQVRNPGTNLCLDTLQRDEDKGYNLGLYPCQGGLSSNQLFSLSKKGELRREESCADVQGTE--ESKVILITCHG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 968115045 545 NDDYNEQWKYE-NQQLVHSNTGMCLDHEGLKSMDDAQVAPCDLtSETQRWIIGH 597
Cdd:cd23459   80 LEKFNQKWKHTkGGQIVHLASGKCLDAEGLKSGDDVTLAKCDG-SLSQKWTFEH 132

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968115045  469 AWGRIKAVHANLCADDLlSNNEKPYNLGLYPCGKELQKsQLFSYTKSQVLRNEIS--CATVqHSSSPPYRIVMVPCLEND 546
Cdd:pfam00652   1 ATGRIRNRASGKCLDVP-GGSSAGGPVGLYPCHGSNGN-QLWTLTGDGTIRSVASdlCLDV-GSTADGAKVVLWPCHPGN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 968115045  547 DyNEQWKYE--NQQLVHSNTGMCLD-HEGLKSMDDAQVAPCDLTSETQRW 593
Cdd:pfam00652  78 G-NQRWRYDedGTQIRNPQSGKCLDvSGAGTSNGKVILWTCDSGNPNQQW 126

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 968115045 466 NVKAWGRIKAVHANLCADDLlsNNEKPYNLGLYPC----GkelqkSQLFSYTKSQVLRNEISCATVqhsSSPPYRIVMVP 541
Cdd:cd23437    1 KNLAWGEIRNLGTGLCLDTM--GHQNGGPVGLYPChgmgG-----NQLFRLNEAGQLAVGEQCLTA---SGSGGKVKLRK 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 968115045 542 CLENDDYneQWKY--ENQQLVHSNTGMCLDHEGLKSMddAQVAPCDLTSETQRWIIGH 597
Cdd:cd23437   71 CNLGETG--KWEYdeATGQIRHKGTGKCLDLNEGTNK--LILQPCDSSSPSQKWEFNE 124

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 968115045 469 AWGRIKAVHANLCADDLLSNNEKPYNLGLYPCGKeLQKSQLFSYTKSQVLRNEISCATVQHSSSPpyrIVMVPClendDY 548
Cdd:cd23462    4 AYGEIRNLAGKLCLDAPGRKKELNKPVGLYPCHG-QGGNQYWMLTKDGEIRRDDLCLDYAGGSGD---VTLYPC----HG 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 968115045 549 ---NEQWKY--ENQQLVHSNTGMCLDHEGLKSmdDAQVAPCDLTSETQRWI 594
Cdd:cd23462   76 mkgNQFWIYdeETKQIVHGTSKKCLELSDDSS--KLVMEPCNGSSPRQQWE 124

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968115045 478 ANLCADDLLSNNEKPynLGLYPC----GkelqkSQLFSYTKSQVLRNEISCATVQhSSSPPYRIVMVPClENDDYNEQWK 553
Cdd:cd23434    8 GNLCLDTLGHKAGGT--VGLYPChgtgG-----NQEWSFTKDGQIKHDDLCLTVV-DRAPGSLVTLQPC-REDDSNQKWE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 968115045 554 YE--NQQLVHSNTGMCLD--HEGLKSMddaQVAPCDLTSETQRWII 595
Cdd:cd23434   79 QIenNSKLRHVGSNLCLDsrNAKSGGL---TVETCDPSSGSQQWKF 121

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968115045 145 PTASVIIIFYNEPySVLVRTVHSTLNTCNQKAlkEVILVDDGSDNaelgGKLDHYTRTRFPsgKVTILRLKNRLGLIRAR 224
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTD----GTAELLAALAFP--RVRVIRNPENLGFAAAR 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 968115045 225 LAGARIASGDVLIFLDAHCEANVGWCEPLLQ 255
Cdd:COG1216   74 NLGLRAAGGDYLLFLDDDTVVEPDWLERLLA 104

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 968115045 469 AWGRIKAVHANLCADDLLSNNEKPYNLGLYPCGKelQKSQLFSYTKSQ----VLRNEIS--CATVQHSSSPPY-RIVMVP 541
Cdd:cd00161    1 GTYRIVNAASGKCLDVAGGSTANGAPVQQWTCNG--GANQQWTLTPVGdgyyTIRNVASgkCLDVAGGSTANGaNVQQWT 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 968115045 542 CleNDDYNEQWKYENQ-----QLVHSNTGMCLDHEGLKSMDDAQV--APCDlTSETQRW 593
Cdd:cd00161   79 C--NGGDNQQWRLEPVgdgyyRIVNKHSGKCLDVSGGSTANGANVqqWTCN-GGANQQW 134

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 968115045 149 VIIIFYNEPySVLVRTVHSTLNtcnQKALK-EVILVDDGS-DNAELggKLDHYTRTRFPsgkVTILRLKNRLGLIRARLA 226
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLA---QTYPNfEVIVVDDGStDGTLE--ILEEYAKKDPR---VIRVINEENQGLAAARNA 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 968115045 227 GARIASGDVLIFLDAHCEANVGWCEPLLQRIKDSRTSVLV 266
Cdd:cd00761   72 GLKAARGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111

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 968115045 146 TASVIIIFYNEPySVLVRTVHSTLNTCNQKALKEVILVDDGSDNA--ELGGKLdhytRTRFPsgkvtILRLKNRLGLIR- 222
Cdd:cd02525    1 FVSIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTDGtrEIVQEY----AAKDP-----RIRLIDNPKRIQs 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968115045 223 -ARLAGARIASGDVLIFLDAHCEANVGWCEPLLQRIKDSRTSVLVPIIDVIDANDFQySTNGYKS---FQVGGfqwnghf 298
Cdd:cd02525   71 aGLNIGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQ-KAIAVAQsspLGSGG------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968115045 299 dwvnlserEKLRQSRECSQpreicpaYSPTMAGGLFAMDRryFWEVGSYDEQMDgwGGENLEMSFRIWQCGGTIETIPCS 378
Cdd:cd02525  143 --------SAYRGGAVKIG-------YVDTVHHGAYRREV--FEKVGGFDESLV--RNEDAELNYRLRKAGYKIWLSPDI 203

                 ....*...
gi 968115045 379 RVGHIFRD 386
Cdd:cd02525  204 RVYYYPRS 211

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 968115045 518 LRNEIS--CATVQHSSSppyRIVMVPCLENDDYNeQWK-YENQQLVHSNTGMCLDHEGLKSMDDAQVAPCDLTSETQRW 593
Cdd:cd23385    5 IYNEDLgkCLAARSSSS---KVSLSTCNPNSPNQ-QWKwTSGHRLFNVGTGKCLGVSSSSPSSPLRLFECDSEDELQKW 79

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968115045 139 DDPGTLPTASVIIIFYNEPySVLVRTVHSTLNTCNQKALKEVILVDDGS-DN-AELggkldhytRTRFPSGKVTILRLKN 216
Cdd:cd06439   23 PDPAYLPTVTIIIPAYNEE-AVIEAKLENLLALDYPRDRLEIIVVSDGStDGtAEI--------AREYADKGVKLLRFPE 93

                         90       100
                 ....*....|....*....|....*
gi 968115045 217 RLGLIRARLAGARIASGDVLIFLDA 241
Cdd:cd06439   94 RRGKAAALNRALALATGEIVVFTDA 118

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 968115045 471 GRIKAVHANLCADDL-LSNNEKpynLGLYPCgKELQKSQLFSYTKSQVLRNEISCATVQHSSSPpyrIVMVPClENDDYN 549
Cdd:cd23467    7 GEIRNVETNQCLDNMgRKENEK---VGIFNC-HGMGGNQVFSYTADKEIRTDDLCLDVSRLNGP---VVMLKC-HHMRGN 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 968115045 550 EQWKYENQQLV--HSNTGMCLDHEGlksmDDAQVAP----CDlTSETQRWII 595
Cdd:cd23467   79 QLWEYDAERLTlrHVNSNQCLDEPS----EEDKMVPtmkdCS-GSRSQQWLL 125

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 968115045 471 GRIKAVHANLCADDLLSNNEKPYNLGLYPCgKELQKSQLFSYTKSQVLRNEIS---CATVQHSSSppyrIVMVPC-LEND 546
Cdd:cd23435    5 GALRNKGSELCLDVNNPNGQGGKPVIMYGC-HGLGGNQYFEYTSKGEIRHNIGkelCLHASGSDE----VILQHCtSKGK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 968115045 547 DY--NEQWKY-ENQQLVHSNTGMCLDheglKSMDDAQVAPCDLTSETQRWIIG 596
Cdd:cd23435   80 DVppEQKWLFtQDGTIRNPASGLCLH----ASGYKVLLRTCNPSDDSQKWTFI 128

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968115045 514 KSQVLRNEIS--CATVQHSSSPPYRIVMVPCleNDDYNEQWKYENQQLVHS--NTGMCLDHEGLKSMD-DAQVAPCDlTS 588
Cdd:cd23456    1 KYFQLKSQASglCLDVSGGATNGANVVVYDC--NNSNSQKWYYDATGRLHSkaNPGKCLDAGGENSNGaNVVLWACN-DS 77

                 ....*
gi 968115045 589 ETQRW 593
Cdd:cd23456   78 ANQRW 82

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 968115045 528 QHSSSPPYRIVMVPCLENDDYNEQWKYENQQLVHSNTGMCLDHEGLKSMDDAQVAPC----DLTSETQRWIIGHE 598
Cdd:cd23454   18 HGSLKSGAKVVLAPLKTKDYESQLWRYDDGYLVNKASGLVLDIQGGVVKSGTRLVQSpkkpSKDANNQRWGLTAD 92

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968115045 149 VIIIFYNEPYSV--LVRTVHSTLNtcNQKALKEVILVDDGS-DN--AELGGKLDHYTRtrfpsgkVTILRLKNRLGLIRA 223
Cdd:cd04187    1 IVVPVYNEEENLpeLYERLKAVLE--SLGYDYEIIFVDDGStDRtlEILRELAARDPR-------VKVIRLSRNFGQQAA 71

                         90
                 ....*....|....*...
gi 968115045 224 RLAGARIASGDVLIFLDA 241
Cdd:cd04187   72 LLAGLDHARGDAVITMDA 89

putative glycosyl transferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968115045 145 PTASVIIIFYNEpySVLVRTVHSTLNTCNQKALkEVILVDDGS-DNAelGGKLDHYtRTRFPsgKVTILRLKNRlGLIRA 223
Cdd:PRK10073   6 PKLSIIIPLYNA--GKDFRAFMESLIAQTWTAL-EIIIVNDGStDNS--VEIAKHY-AENYP--HVRLLHQANA-GVSVA 76

                         90
                 ....*....|....*...
gi 968115045 224 RLAGARIASGDVLIFLDA 241
Cdd:PRK10073  77 RNTGLAVATGKYVAFPDA 94

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 968115045 471 GRIKAVHANLCaddLLSNNEKPYN---LGLYPCgKELQKSQLFSYTKSQVLRNEIS-CATVQHSSSPPYRivMVPClEND 546
Cdd:cd23440    6 GQLKHAGSGLC---LVAEDEVSQKgslLVLRPC-SRNDKKQLWYYTEDGELRLANLlCLDSSETSSDFPR--LMKC-HGS 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 968115045 547 DYNEQWKY-ENQQLVHSNTGMCLDHEGLKSMDDAQVAPCDLtSETQRWII 595
Cdd:cd23440   79 GGSQQWRFkKDNRLYNPASGQCLAASKNGTSGYVTMDICSD-SPSQKWVF 127

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968115045  179 EVILVDDGSDN---AELGGKLDHYTRTRFPSGKVTILrlknrlGLIRARLAGARIASGDVLIFLDAHCEANVGWCEPLLQ 255
Cdd:pfam10111  31 ELIIINDGSTDktlEEVSSIKDHNLQVYYPNAPDTTY------SLAASRNRGTSHAIGEYISFIDGDCLWSPDKFEKQLK 104