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 665401163 251 TKDVQGWGKVHAVNSNICLDDLLQNNEKPYNAGLYPCGKVLQKSQLFSFTNTNVLRNELSCATVQHSEspPYRVVMVPCM 330
Cdd:cd23459    1 DEDVLAYGQVRNPGTNLCLDTLQRDEDKGYNLGLYPCQGGLSSNQLFSLSKKGELRREESCADVQGTE--ESKVILITCH 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665401163 331 ENDEFNEQWRYE-HQHIIHSNTGMCLDHQGLKSLDDAQVAPCDPhSESQRWTIEH 384
Cdd:cd23459   79 GLEKFNQKWKHTkGGQIVHLASGKCLDAEGLKSGDDVTLAKCDG-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 665401163 251 TKDVQGWGKVHAVNSNICLDDLLQNNEKPYNAGLYPCGKVLQKSQLFSFTNTNVLRNELSCATVQHSEspPYRVVMVPCM 330
Cdd:cd23459    1 DEDVLAYGQVRNPGTNLCLDTLQRDEDKGYNLGLYPCQGGLSSNQLFSLSKKGELRREESCADVQGTE--ESKVILITCH 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665401163 331 ENDEFNEQWRYE-HQHIIHSNTGMCLDHQGLKSLDDAQVAPCDPhSESQRWTIEH 384
Cdd:cd23459   79 GLEKFNQKWKHTkGGQIVHLASGKCLDAEGLKSGDDVTLAKCDG-SLSQKWTFEH 132

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401163    1 MPCRLGLIRARLAGARIATGDVLIFLDAHCEGNIGWCEPLLQRIKESRTSVLVPIIDVIDANDFQYstngyksfqvggfQ 80
Cdd:pfam00535  60 LPENRGKAGARNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY-------------R 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 665401163   81 WNGHFDWINLPEREKQRQRreckqeREICPAYSPTMAGGLFAIDRR 126
Cdd:pfam00535 127 RASRITLSRLPFFLGLRLL------GLNLPFLIGGFALYRREALEE 166

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 665401163 250 PTKDVQGWGKVHA-VNSNICLDdlLQNNEKPYN-AGLYPCGKvlQKSQLFSFTNTNVLRNELSCATV-QHSESPPYRVVM 326
Cdd:NF035930 110 PGQGGGGWGGREIrGKGGLCLD--VSGGLRPGNgLIVYNCNG--GENQRFTWGRGGELRVGDLCLDVaDGNTRDGARVIA 185

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665401163 327 VPCmeNDEFNEQWRYEHQHIIHSNTGMCLDhqglksLDDAQVAPCDP-------HSESQRW 380
Cdd:NF035930 186 WSC--SGGPNQRWRWRGGQIRSRLSGKCLD------IEGGRARPGQPvivwscnGGPNQRW 238

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 665401163 251 TKDVQGWGKVHAVNSNICLDDLLQNNEKPYNAGLYPCGKVLQKSQLFSFTNTNVLRNELSCATVQHSEspPYRVVMVPCM 330
Cdd:cd23459    1 DEDVLAYGQVRNPGTNLCLDTLQRDEDKGYNLGLYPCQGGLSSNQLFSLSKKGELRREESCADVQGTE--ESKVILITCH 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665401163 331 ENDEFNEQWRYE-HQHIIHSNTGMCLDHQGLKSLDDAQVAPCDPhSESQRWTIEH 384
Cdd:cd23459   79 GLEKFNQKWKHTkGGQIVHLASGKCLDAEGLKSGDDVTLAKCDG-SLSQKWTFEH 132

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 665401163 253 DVQGWGkvHAVNSNICLDDLLQNNEKPYNAGLYPCGKVlQKSQLFSFTNTNVLRNELSCATVqHSESPPYRVVMVPCmeN 332
Cdd:cd23441    1 NELAYG--QIKQGNLCLDSDEQLFQGPALLILAPCSNS-SDSQEWSFTKDGQLQTQGLCLTV-DSSSKDLPVVLETC--S 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 665401163 333 DEFNEQWRYEHQHIIHSNTGMCLDHQGLKSLddaQVAPCDPHSESQRWTIE 383
Cdd:cd23441   75 DDPKQKWTRTGRQLVHSESGLCLDSRKKKGL---VVSPCRSGAPSQKWDFT 122

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 665401163 258 GKVHAVNSNICLDDL-LQNNEKPynaGLYPCGKvLQKSQLFSFTNTNVLRNELSCATVQHSESPpyrVVMVPCMENDEfN 336
Cdd:cd23433    7 GEIRNVETNLCLDTMgRKAGEKV---GLSSCHG-QGGNQVFSYTAKGEIRSDDLCLDASRKGGP---VKLEKCHGMGG-N 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 665401163 337 EQWRYEHQ--HIIHSNTGMCLDHQGLKSLDDAQVAPCDPHSeSQRWTIE 383
Cdd:cd23433   79 QEWEYDKEtkQIRHVNSGLCLTAPNEDDPNEPVLRPCDGGP-SQKWELE 126

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401163    1 MPCRLGLIRARLAGARIATGDVLIFLDAHCEGNIGWCEPLLQRIKESRTSVLVPIIDVIDANDFQYstngyksfqvggfQ 80
Cdd:pfam00535  60 LPENRGKAGARNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY-------------R 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 665401163   81 WNGHFDWINLPEREKQRQRreckqeREICPAYSPTMAGGLFAIDRR 126
Cdd:pfam00535 127 RASRITLSRLPFFLGLRLL------GLNLPFLIGGFALYRREALEE 166

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 665401163 266 NICLDDL-LQNNEKPynaGLYPC----GkvlqkSQLFSFTNTNVLRNELSCATVQhSESPPYRVVMVPCMENDEfNEQWR 340
Cdd:cd23434    9 NLCLDTLgHKAGGTV---GLYPChgtgG-----NQEWSFTKDGQIKHDDLCLTVV-DRAPGSLVTLQPCREDDS-NQKWE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 665401163 341 YEH--QHIIHSNTGMCLD--HQGLKSLddaQVAPCDPHSESQRWTI 382
Cdd:cd23434   79 QIEnnSKLRHVGSNLCLDsrNAKSGGL---TVETCDPSSGSQQWKF 121

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 665401163 268 CLDDLLQNNEKPYNAGLYPCGK---VLQKSQLFSFTNTNVLRNELSCATVqHSESPPYRVVMVPCMENDEfNEQWRYEHQ 344
Cdd:cd23478   18 CLESRRVEGQELPNLSLSPCIKskgVPAKSQEWAYTYNQQIRQQQLCLSV-HTLFPGSPVVLVPCKEGDG-KQRWTKVGS 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 665401163 345 HIIHSNTGMCLDHQ----GLKSLDDAQVAPCDPHSESQRW 380
Cdd:cd23478   96 HIEHMASRFCLDTEmfgdGTESSKEIVINPCESSAMSQRW 135

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 665401163 258 GKVHAVNSNICLDDLLQNNEKPYNAGLYPCgKVLQKSQLFSFTNTNVLRN----ELsCATVQHSESppyrVVMVPCMEND 333
Cdd:cd23435    5 GALRNKGSELCLDVNNPNGQGGKPVIMYGC-HGLGGNQYFEYTSKGEIRHnigkEL-CLHASGSDE----VILQHCTSKG 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665401163 334 EF---NEQWRYEH-QHIIHSNTGMCLDHQGLKslddAQVAPCDPHSESQRWTIE 383
Cdd:cd23435   79 KDvppEQKWLFTQdGTIRNPASGLCLHASGYK----VLLRTCNPSDDSQKWTFI 128

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 665401163 311 CATVQHSESppyRVVMVPCMENDEFNeQWR-YEHQHIIHSNTGMCLDHQGLKSLDDAQVAPCDPHSESQRWT 381
Cdd:cd23385   13 CLAARSSSS---KVSLSTCNPNSPNQ-QWKwTSGHRLFNVGTGKCLGVSSSSPSSPLRLFECDSEDELQKWK 80

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 665401163 268 CLDDLLQNNEKPYNAGLYPCgKVLQKSQLFS---FTNTNVLRNELSCATVQhSESPPYRVVMVPCMENDEfNEQWRYEHQ 344
Cdd:cd23479   16 CLESQGQDTTGDTLLGLGEC-RGTASNLPASqewVLSDPLIRQQDKCLAIT-SFSPGSKVILELCNQKDG-RQKWKLKGS 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 665401163 345 HIIHSNTGMCLDHQGlkslDDAQVAPCDPHSESQRWTI 382
Cdd:cd23479   93 FIQHQVSGLCLDSQS----GRVVINQCQADLASQQWEL 126

ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa galactose-binding lectin (EW29) and similar proteins; EW29 is a galactose-binding lectin from the earthworm Lumbricus terrestris. It contains two ricin B-type lectin domains 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 second ricin B-type lectin domain may harbor two sugar-binding pockets in subdomains alpha and gamma. EW29 uses these two sugar-binding sites for its function as a single domain-type hemagglutinin.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401163 271 DLLQNNEKPYNA-GLYPCGKVLQKSQLFSF-TNTNVLRNELS--CATVQHSESppyrVVMVPCmENDEFNEQWRYEHQHI 346
Cdd:cd23449   15 DVEGANAKPGAKvIMWEKKGGAEDNQLWYEdEVTGTIRSKLNdfCLDASGDKG----LILNPY-DPSNPKQQWKISGNKI 89

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 665401163 347 IH-SNTGMCLDHQGLKSLDDAQVAPCDPHSE-SQRWTIE 383
Cdd:cd23449   90 QNrSNPDNVLDIKGGSKDDGARLCAWEYNGGpNQLWDFE 128

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 5 (GALNT5) and similar proteins; GALNT5 (EC 2.4.1.41), also called polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, protein-UDP acetylgalactosaminyltransferase 5, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, 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. GALNT5 has activity toward EA2 peptide substrate but has a weak activity toward Muc2 or Muc1b substrates. GALNT5 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 665401163 293 KSQLFSFTNTNVLRNELSCATVQHSESppyRVVMVPCmENDEFNEQWRYEHQ--------HII--HSNTGMCLD-HQGLK 361
Cdd:cd23436   35 KSQHFNYTWLRLIRQGELCLAPVEAEG---ALTLHPC-DNTNNGLRWLHKSLiafpelmdHIMleHQSQPTCLEaDPSQK 110

                         90       100
                 ....*....|....*....|...
gi 665401163 362 SLddaQVAPCDPHSESQRWTIEH 384
Cdd:cd23436  111 IL---RLNACDSFKRYQKWRFGH 130

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 665401163 315 QHSESPPYRVVMVPCMENDEFNEQWRYEHQHIIHSNTGMCLDHQGLKSLDDAQVAPC----DPHSESQRWTIEH 384
Cdd:cd23454   18 HGSLKSGAKVVLAPLKTKDYESQLWRYDDGYLVNKASGLVLDIQGGVVKSGTRLVQSpkkpSKDANNQRWGLTA 91

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

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665401163   311 CATVQHSESPpyrVVMVPCMENDEfNEQWRYEHQHII-HSNTGMCLDHQGLKSlDDAQVAPCDPHSESQRWTIEH 384
Cdd:smart00458   9 CLDVNGNKNP---VGLFDCHGTGG-NQLWKLTSDGAIrIKDTDLCLTANGNTG-STVTLYSCDGTNDNQYWEVNK 78

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401163   2 PCRLGLIRARLAGARIATGDVLIFLDAHCEGNIGWCEPLLQRIKESRTSVlvpiidVIDANDFQYSTNGYKSFQVGGFQW 81
Cdd:COG0463   65 ERNRGKGAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADL------VYGSRLIREGESDLRRLGSRLFNL 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401163  82 NGHFDWInlperekqrqrreckqereicpaysPTMAGGLFAIDRRYFWEVGsYDEQMdgwgGENLEMsFRIWQCGGTIET 161
Cdd:COG0463  139 VRLLTNL-------------------------PDSTSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAE 187

                 ..
gi 665401163 162 IP 163
Cdd:COG0463  188 VP 189

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 665401163 121 FAIDRRYFWEVGSYDEQMDGWGGEnLEMSFRIWQCGGTIETIPCSRVGH 169
Cdd:COG1216  108 LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYH 155

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 665401163 257 WGKVHAVNSNICLDDLLQNNEKPYNAGLYPCGKVLQkSQLFSFTNTNVLR--NELSCATVQHSEsppyrVVMVPCmENDE 334
Cdd:cd23442    5 SGQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNG-NQLFEYTSDKEIRfgSLQLCLDVRQEQ-----VVLQNC-TKEK 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 665401163 335 FNEQWRY-EHQHIIHSNTGMCLDHQGLKSLDDAQVAPCDPHSEsQRWT 381
Cdd:cd23442   78 TSQKWDFqETGRIVHILSGKCIEAVESENSKLLFLSPCNGQRN-QMWK 124

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 665401163 257 WGKVHAVNSNICLDdLLQNNEKPYNAGLYPCGKvLQKSQLFSFTNTNVLRNELSCATVQHSESPPY---------RVVMV 327
Cdd:cd23470    4 YGAIKNEGTNQCLD-VGENNRGGKPLIMYSCHG-MGGNQYFEYTTHKELRHNIAKQLCLRVSKGPVqlgechykgKNSQV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665401163 328 PCmendefNEQWRYEHQHII-HSNTGMCLDHQGLKSlddaQVAPCDPHSESQRW 380
Cdd:cd23470   82 PP------DEEWELTQDHLIrNSGSNMCLTARGKHP----AMAPCNPADPHQLW 125