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 225007540 460 KVLQRGRLRNLLADKCLVAQGRPSQKGGAVVVKDCDPQDPEQEWAYDEEHELVLAGLLCLDMSEIRsSDPPRLMKCHGSG 539
Cdd:cd23440    1 KVIRKGQLKHAGSGLCLVAEDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLLCLDSSETS-SDFPRLMKCHGSG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 225007540 540 GSQQWTLGKKNWLYQVSVGQCLAVGDPLSiKGYVSMAICDDSRSQQWQL 588
Cdd:cd23440   80 GSQQWRFKKDNRLYNPASGQCLAASKNGT-SGYVTMDICSDSPSQKWVF 127

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 225007540 460 KVLQRGRLRNLLADKCLVAQGRPSQKGGAVVVKDCDPQDPEQEWAYDEEHELVLAGLLCLDMSEIRsSDPPRLMKCHGSG 539
Cdd:cd23440    1 KVIRKGQLKHAGSGLCLVAEDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLLCLDSSETS-SDFPRLMKCHGSG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 225007540 540 GSQQWTLGKKNWLYQVSVGQCLAVGDPLSiKGYVSMAICDDSRSQQWQL 588
Cdd:cd23440   80 GSQQWRFKKDNRLYNPASGQCLAASKNGT-SGYVTMDICSDSPSQKWVF 127

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540  465 GRLRNLLADKCLVAQGRpSQKGGAVVVKDCDPQDPEQEWAYDEEHEL-VLAGLLCLDMSEIRSSDPPRLMKCHGSGGSQQ 543
Cdd:pfam00652   3 GRIRNRASGKCLDVPGG-SSAGGPVGLYPCHGSNGNQLWTLTGDGTIrSVASDLCLDVGSTADGAKVVLWPCHPGNGNQR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 225007540  544 WTLGKK-NWLYQVSVGQCLAVGDPLSIKGYVSMAICDD-SRSQQW 586
Cdd:pfam00652  82 WRYDEDgTQIRNPQSGKCLDVSGAGTSNGKVILWTCDSgNPNQQW 126

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540   473 DKCLVAQGRPSQkggaVVVKDCDPQDPEQEWAYDEEHELVLAGL-LCLDMSEiRSSDPPRLMKCHGSGGSQQWTLGKKNW 551
Cdd:smart00458   7 GKCLDVNGNKNP----VGLFDCHGTGGNQLWKLTSDGAIRIKDTdLCLTANG-NTGSTVTLYSCDGTNDNQYWEVNKDGT 81

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 225007540   552 LYQVSVGQCLAVGDPLSIKGyVSMAICDDSRSQQWQLE 589
Cdd:smart00458  82 IRNPDSGKCLDVKDGNTGTK-VILWTCSGNPNQKWIFE 118

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 225007540 460 KVLQRGRLRNLLADKCLVAQGRPSQKGGAVVVKDCDPQDPEQEWAYDEEHELVLAGLLCLDMSEIRsSDPPRLMKCHGSG 539
Cdd:cd23440    1 KVIRKGQLKHAGSGLCLVAEDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLLCLDSSETS-SDFPRLMKCHGSG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 225007540 540 GSQQWTLGKKNWLYQVSVGQCLAVGDPLSiKGYVSMAICDDSRSQQWQL 588
Cdd:cd23440   80 GSQQWRFKKDNRLYNPASGQCLAASKNGT-SGYVTMDICSDSPSQKWVF 127

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540  465 GRLRNLLADKCLVAQGRpSQKGGAVVVKDCDPQDPEQEWAYDEEHEL-VLAGLLCLDMSEIRSSDPPRLMKCHGSGGSQQ 543
Cdd:pfam00652   3 GRIRNRASGKCLDVPGG-SSAGGPVGLYPCHGSNGNQLWTLTGDGTIrSVASDLCLDVGSTADGAKVVLWPCHPGNGNQR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 225007540  544 WTLGKK-NWLYQVSVGQCLAVGDPLSIKGYVSMAICDD-SRSQQW 586
Cdd:pfam00652  82 WRYDEDgTQIRNPQSGKCLDVSGAGTSNGKVILWTCDSgNPNQQW 126

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 137 PTASIVICFFNEAfSALLRTVHSVLDRTpnYLLHEIILVDDHSElDDLKEdldsYVQQHLQKKVKVVRNEKREGLIRGRM 216
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQT--YPPFEVIVVDNGST-DGTAE----LLAALAFPRVRVIRNPENLGFAAARN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 217 IGASHATGEVLVFLDSHCEVNEAWLQPLLTpikenrktvvcpvidiisadtlvytpspivrggfnwglhfkwdpvpmsel 296
Cdd:COG1216   75 LGLRAAGGDYLLFLDDDTVVEPDWLERLLA-------------------------------------------------- 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 297 nspdgairsptmAGGLFaMDRNYFYELGQYDRGMDIWGGEnLEISFRIWMCGGQLLIVPCSRVGHIFRKRRpyGSPGGQD 376
Cdd:COG1216  105 ------------AACLL-IRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASS--GPLLRAY 168

                        250       260
                 ....*....|....*....|....*
gi 225007540 377 TMAHNSLRLAHVWMDDYKEQYFALR 401
Cdd:COG1216  169 YLGRNRLLFLRKHGPRPLLRLALLR 193

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 137 PTASIVICFFNEAfSALLRTVHSVLDRT-PNYllhEIILVDDHSElDDLKEDLDSYVQQHlqKKVKVVRNEKREGLIRGR 215
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTyPDF---EIIVVDDGST-DGTAEILRELAAKD--PRIRVIRLERNRGKGAAR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 216 MIGASHATGEVLVFLDSHCEVNEAWLQPLLTPIKENRktvvcpvIDIISADTLVYTPSPIVRGGFNWGLHFKWDPVPMse 295
Cdd:COG0463   75 NAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGP-------ADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNL-- 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 296 lnspdgairsPTMAGGLFAMDRNYFYELGqYDRGMdiwgGENLEIsFRIWMCGGQLLIVP 355
Cdd:COG0463  146 ----------PDSTSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVP 189

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 225007540 465 GRLRNLLADKCLVAQGRpsQKGGAVVVKDCDPQDPEQEWAYDEEHELVlAGLLCLDMSeiRSSDPPRLMKCHGSGGSQQW 544
Cdd:cd23433    7 GEIRNVETNLCLDTMGR--KAGEKVGLSSCHGQGGNQVFSYTAKGEIR-SDDLCLDAS--RKGGPVKLEKCHGMGGNQEW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 225007540 545 TLGKK-NWLYQVSVGQCLAVGDPlSIKGYVSMAICDDSRSQQWQLEG 590
Cdd:cd23433   82 EYDKEtKQIRHVNSGLCLTAPNE-DDPNEPVLRPCDGGPSQKWELEG 127

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 141 IVICFFNEAFSaLLRTVHSVLDRTPNYLLHEIILVDDHSEldDLKEDLDSYVQQHLQKKVKVVRNekREGLIRGR----M 216
Cdd:cd04192    1 VVIAARNEAEN-LPRLLQSLSALDYPKEKFEVILVDDHST--DGTVQILEFAAAKPNFQLKILNN--SRVSISGKknalT 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 225007540 217 IGASHATGEVLVFLDSHCEVNEAWLQPLLTPI-KENRKTVVCPVI 260
Cdd:cd04192   76 TAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIqKEQIGLVAGPVI 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 225007540 465 GRLRNLLADKCLVAQGRPSQKGgaVVVKDC--DPQDPEQEWAYDEEHELVLAGL-LCLDMSEIRSSDPPRLMKCHGSGGS 541
Cdd:cd23439    3 GEIRNVGSGLCIDTKHGGENDE--VRLSKCvkDGGGGEQQFELTWHEDIRPKKRkVCFDVSSHTPGAPVILYACHGMKGN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 225007540 542 QQWTL--GKKNwLYQVSVGQCLavgDPLSIKGYVSMAICD-DSRSQQW 586
Cdd:cd23439   81 QLWKYrpNTKQ-LYHPVSGLCL---DADPGSGKVFMNHCDeSSDTQKW 124

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 225007540 460 KVLQRGRLRNLLADKCLVAQGRpsQKGGAVVVKDCDPQDPEQEWAYDEEHELVLaGLLCLDMSeiRSSDPPRLMKCHGsG 539
Cdd:cd23437    1 KNLAWGEIRNLGTGLCLDTMGH--QNGGPVGLYPCHGMGGNQLFRLNEAGQLAV-GEQCLTAS--GSGGKVKLRKCNL-G 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 225007540 540 GSQQWTLGKKN-WLYQVSVGQCLAVGdplSIKGYVSMAICD-DSRSQQWQ 587
Cdd:cd23437   75 ETGKWEYDEATgQIRHKGTGKCLDLN---EGTNKLILQPCDsSSPSQKWE 121

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 225007540 463 QRGRLRNLLADKCLVAQGRPSQKGGAVVVKDCDPQDpEQEW----AYDEEHELVLAGL-LCLDMSEIRSSD--PPRLMKC 535
Cdd:cd00161    1 GTYRIVNAASGKCLDVAGGSTANGAPVQQWTCNGGA-NQQWtltpVGDGYYTIRNVASgKCLDVAGGSTANgaNVQQWTC 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 225007540 536 HGsGGSQQWTLGKKN----WLYQVSVGQCLAVGDPLSIKG-YVSMAICDDSRSQQW 586
Cdd:cd00161   80 NG-GDNQQWRLEPVGdgyyRIVNKHSGKCLDVSGGSTANGaNVQQWTCNGGANQQW 134

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 141 IVICFFNEAfSALLRTVHSVLDRTpnYLLHEIILVDDHSElDDLKEDLdsyvqQHLQKKVKVVRNEKREGLIRGRMIGAS 220
Cdd:cd04186    1 IIIVNYNSL-EYLKACLDSLLAQT--YPDFEVIVVDNAST-DGSVELL-----RELFPEVRLIRNGENLGFGAGNNQGIR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 221 HATGEVLVFLDSHCEVNEAWLQPLLTPIKENrktvvcpvidiisadtlvytpspivrggfnwglhfkwdpvpmselnsPD 300
Cdd:cd04186   72 EAKGDYVLLLNPDTVVEPGALLELLDAAEQD-----------------------------------------------PD 104

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225007540 301 GAIRSPTMAGGLFAMDRNYFYELGQYDRGMDIWgGENLEISFRIWMCGGQLLIVPCSRVGH 361
Cdd:cd04186  105 VGIVGPKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYH 164

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 466 RLRNLLADKCLVAQGrpsqkGGAVVVKDCDPqDPEQEWAY--DEEHELVLAGL---LCLDMSeirSSDPPRLMKChGSGG 540
Cdd:cd23415    4 RLRNVATGRCLDSNA-----GGNVYTGPCNG-GPYQRWTWsgVGDGTVTLRNAatgRCLDSN---GNGGVYTLPC-NGGS 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225007540 541 SQQWTLGKKNW----LYQVSVGQCLAVGDplsiKGYVSMAICDDSRSQQWQ 587
Cdd:cd23415   74 YQRWRVTSTSGggvtLRNVATGRCLDSNG----SGGVYTRPCNGGSYQRWR 120

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540   463 QRGRLRNLLADKCLVAqgrPSQKGGAVVVKDCDPQDPEQEWAYDEEHELVLAGL-LCLDMSEIRSSDPPRLMKCHGSgGS 541
Cdd:smart00458  37 SDGAIRIKDTDLCLTA---NGNTGSTVTLYSCDGTNDNQYWEVNKDGTIRNPDSgKCLDVKDGNTGTKVILWTCSGN-PN 112

                   ....*
gi 225007540   542 QQWTL 546
Cdd:smart00458 113 QKWIF 117

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; 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. In higher eukaryotes,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. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 141 IVICFFNEAfsallRTVHSVLDRTPNYLL----HEIILVDDHSElDDLKEDLDSYVQQHlqKKVKVVRNEKREGLIRGRM 216
Cdd:cd04179    1 VVIPAYNEE-----ENIPELVERLLAVLEegydYEIIVVDDGST-DGTAEIARELAARV--PRVRVIRLSRNFGKGAAVR 72

                         90
                 ....*....|....*.
gi 225007540 217 IGASHATGEVLVFLDS 232
Cdd:cd04179   73 AGFKAARGDIVVTMDA 88

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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 467 LRNLLADKCLVAQGRpsqkGGAVVVKDCDPQDPEQEWAYDEEHELVLAG-LLCLDMSEIRSSDPPRLMKCHGSGGSQQWT 545
Cdd:cd23385    5 IYNEDLGKCLAARSS----SSKVSLSTCNPNSPNQQWKWTSGHRLFNVGtGKCLGVSSSSPSSPLRLFECDSEDELQKWK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 225007540 546 LGKKNwLYQVSVGQCLAVGDPLSIKGYVSmaiCDDSRSQQWQ 587
Cdd:cd23385   81 CSKDG-LLLLKGLGLLLLYDKSGKNVVVS---KGSGLSSRWK 118

CESA_like is the cellulose synthase superfamily; The cellulose synthase (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 include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 141 IVICFFNEAfSALLRTVHSVLDRtpNYLLHEIILVDDHSElDDLKEDLDSYVQQHLQKKVKVVRNE---KREGLIRgrmi 217
Cdd:cd06423    1 IIVPAYNEE-AVIERTIESLLAL--DYPKLEVIVVDDGST-DDTLEILEELAALYIRRVLVVRDKEnggKAGALNA---- 72

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                 ....*....|....*....|....*....|....*....|
gi 225007540 218 GASHATGEVLVFLDSHCEVNEAWLQPLLTPIKENRKTVVC 257
Cdd:cd06423   73 GLRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAV 112

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). 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. Pgant8 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 both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. 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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 465 GRLRNLLAD-KCLVAQGRPsqKGGAVVVKDCDPQD----PEQEWAYDEEHELVLAGL-LCLDMSEIRSsdppRLMKCHGS 538
Cdd:cd23461    4 GVIQSVAFPnLCLDILGRS--HGGPPVLAKCSSNKsmpgTFQNFSLTFHRQIKHGTSdDCLEVRGNNV----RLSRCHYQ 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225007540 539 GGSQQWTLG-KKNWLYQ-VSVGQCLAVGDPlsiKGYVSMAICD-DSRSQQW 586
Cdd:cd23461   78 GGNQYWKYDyETHQLINgGQNNKCLEADVE---SLKITLSICDsDNVEQKW 125

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007540 141 IVICFFNEA--FSALLRTVHSVLDRTPNYLlHEIILVDDHSElDDLKEDLDSYVQQHlQKKVKVVRNEKREGliRGR--M 216
Cdd:cd04188    1 VVIPAYNEEkrLPPTLEEAVEYLEERPSFS-YEIIVVDDGSK-DGTAEVARKLARKN-PALIRVLTLPKNRG--KGGavR 75

                         90
                 ....*....|....*
gi 225007540 217 IGASHATGEVLVFLD 231
Cdd:cd04188   76 AGMLAARGDYILFAD 90