ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 9 (GALNT9) and similar proteins; GALNT9 (EC 2.4.1.41), also called polypeptide GalNAc transferase 9, GalNAc-T9, pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9, 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. GALNT9 does not glycosylate apomucin or SDC3. GALNT9 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 169790926 456 MRVYNNTLTYGEVRNSKASAYCLDQGAEDGDRAILYPCHGMSSQLVRYSADGLLQLGPLGSTAFLPDSKCLVDDGTGRMP 535
Cdd:cd23473    1 MRIYNNTITYGEVRNSKASGYCLDQGSEEDDKAILYPCHGMSSQLVRYSTEGLLQLGPLGSTAFLPDTKCLVDDGRGRTP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169790926 536 TLKKCEDVARPTQRLWDFTQSGPIVSRATGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIKH 600
Cdd:cd23473   81 TLKKCEDVARPAQRLWDFTQNGPIISRDTGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIKH 145

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 9 (GALNT9) and similar proteins; GALNT9 (EC 2.4.1.41), also called polypeptide GalNAc transferase 9, GalNAc-T9, pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9, 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. GALNT9 does not glycosylate apomucin or SDC3. GALNT9 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 169790926 456 MRVYNNTLTYGEVRNSKASAYCLDQGAEDGDRAILYPCHGMSSQLVRYSADGLLQLGPLGSTAFLPDSKCLVDDGTGRMP 535
Cdd:cd23473    1 MRIYNNTITYGEVRNSKASGYCLDQGSEEDDKAILYPCHGMSSQLVRYSTEGLLQLGPLGSTAFLPDTKCLVDDGRGRTP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169790926 536 TLKKCEDVARPTQRLWDFTQSGPIVSRATGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIKH 600
Cdd:cd23473   81 TLKKCEDVARPAQRLWDFTQNGPIISRDTGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIKH 145

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790926  464 TYGEVRNsKASAYCLD--QGAEDGDRAILYPCHGM-SSQLVRYSADGLLQLGPlgstaflpDSKCL--VDDGTGRMPTLK 538
Cdd:pfam00652   1 ATGRIRN-RASGKCLDvpGGSSAGGPVGLYPCHGSnGNQLWTLTGDGTIRSVA--------SDLCLdvGSTADGAKVVLW 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 169790926  539 KCeDVARPTQRlWDFTQSG-PIVSRATGRCLEVEMSKDANFglRLVVQRC----SGQKW 592
Cdd:pfam00652  72 PC-HPGNGNQR-WRYDEDGtQIRNPQSGKCLDVSGAGTSNG--KVILWTCdsgnPNQQW 126

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790926   471 SKASAYCLDQGAEDGdRAILYPCHGMSS-QLVRYSADGLLQlgplgstaFLPDSKCL-VDDGTGRMPTLKKCEDVArPTQ 548
Cdd:smart00458   3 SGNTGKCLDVNGNKN-PVGLFDCHGTGGnQLWKLTSDGAIR--------IKDTDLCLtANGNTGSTVTLYSCDGTN-DNQ 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 169790926   549 RlWDFTQSGPIVSRATGRCLEVemsKDANFGLRLVVQRCSG---QKW 592
Cdd:smart00458  73 Y-WEVNKDGTIRNPDSGKCLDV---KDGNTGTKVILWTCSGnpnQKW 115

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 9 (GALNT9) and similar proteins; GALNT9 (EC 2.4.1.41), also called polypeptide GalNAc transferase 9, GalNAc-T9, pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9, 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. GALNT9 does not glycosylate apomucin or SDC3. GALNT9 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 169790926 456 MRVYNNTLTYGEVRNSKASAYCLDQGAEDGDRAILYPCHGMSSQLVRYSADGLLQLGPLGSTAFLPDSKCLVDDGTGRMP 535
Cdd:cd23473    1 MRIYNNTITYGEVRNSKASGYCLDQGSEEDDKAILYPCHGMSSQLVRYSTEGLLQLGPLGSTAFLPDTKCLVDDGRGRTP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169790926 536 TLKKCEDVARPTQRLWDFTQSGPIVSRATGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIKH 600
Cdd:cd23473   81 TLKKCEDVARPAQRLWDFTQNGPIISRDTGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIKH 145

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 17 (GALNT17) and similar proteins; GALNT17 (EC 2.4.1.41), also called polypeptide GalNAc transferase-like protein 3, GalNAc-T-like protein 3, pp-GaNTase-like protein 3, protein-UDP acetylgalactosaminyltransferase-like protein 3, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3, or Williams-Beuren syndrome chromosomal region 17 protein, may 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. GALNT17 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 169790926 456 MRVYNNTLTYGEVRNSKASAYCLDQGAEDGDRAILYPCHGMSSQLVRYSADGLLQLGPLGSTAFLPDSKCLVDDGTGRMP 535
Cdd:cd23474    1 MRRYNNTVAYGELRNNKAKDVCLDQGPPENHTAILYPCHGWGPQLARYTKEGYLHLGALGTTTLLPDTRCLVDNKKSRFP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169790926 536 TLKKCEDVARPTQRLWDFTQSGPIVSRATGRCLEVEMSKdaNFGLRLVVQRCSGQKWMIRNWIK 599
Cdd:cd23474   81 QLLDCDKVKSILHKRWNFIQNGAIMNLGTGRCLEVENRG--NFGIDLILRSCTGQRWTIKNFIK 142

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8) and similar proteins; GALNT8 (EC 2.4.1.41), also called polypeptide GalNAc transferase 8, GalNAc-T8, pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8, may 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. GALNT8 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 169790926 453 YPEMRVYNNTLTYGEVRNSKASAYCLDQGAEDGDRAILYPCHGMSSQLVRYSADGLLQLGPLGSTAFLPDsKCLVDDGTG 532
Cdd:cd23472    1 YPVLMPIQTIVGYGTMKNSLNENICIDQGPVPGNTPIMYGCHGYSPQFVYYHLTGELYVGGLKADIYASD-RCLTDPGEG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169790926 533 RMPTLKKCEDVARPTQRL-WDFTQSGPIVSRATGRCLEVEMSKDANFGLrLVVQRCSGQKWMIRNWIK 599
Cdd:cd23472   80 WKPELVSCQDATLKGLNMyWDFKQGTAIINRKTKRCLEISLDKTPSYYT-LILQTCTGQKWEIQHVLM 146

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790926  464 TYGEVRNsKASAYCLD--QGAEDGDRAILYPCHGM-SSQLVRYSADGLLQLGPlgstaflpDSKCL--VDDGTGRMPTLK 538
Cdd:pfam00652   1 ATGRIRN-RASGKCLDvpGGSSAGGPVGLYPCHGSnGNQLWTLTGDGTIRSVA--------SDLCLdvGSTADGAKVVLW 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 169790926  539 KCeDVARPTQRlWDFTQSG-PIVSRATGRCLEVEMSKDANFglRLVVQRC----SGQKW 592
Cdd:pfam00652  72 PC-HPGNGNQR-WRYDEDGtQIRNPQSGKCLDVSGAGTSNG--KVILWTCdsgnPNQQW 126

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790926 151 PQVSVVFIFVNEAlSVILRSVHSVVNHTPSQLlkEVILVDDNSDNVELkfnldQYVNKRYPGLVKIVRNSRREGLIRARL 230
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTA-----ELLAALAFPRVRVIRNPENLGFAAARN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790926 231 QGWKAATAPVVGFFDAHVEFNTGWAEPALSRiredrrrivlpaidnikystfevqqyanaahgynwglwcmyiippqdwl 310
Cdd:COG1216   75 LGLRAAGGDYLLFLDDDTVVEPDWLERLLAA------------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790926 311 drgdesapirtpamigCSFVVDREYFGDIGLLDPGMEVYGGEnVELGMRVWQCGGSMEVLPCSRVAHIER-TRKPYNNdi 389
Cdd:COG1216  106 ----------------ACLLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGaSSGPLLR-- 166

                        250
                 ....*....|....*..
gi 169790926 390 DYYAKRNALRAAEVWMD 406
Cdd:COG1216  167 AYYLGRNRLLFLRKHGP 183

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 3 (Pgant3) and similar proteins; Pgant3, also called pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant3 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers EA2 as a substrate and has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Pgant3 plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. It may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Together with Pgant35A, Pgant3 regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790926 465 YGEVRNsKASAYCLD-QGAEDGDRAI-LYPCHG-MSSQLVRYSADGLLQlgplgstaflPDSKCLVDDgTGRMPTLKKCE 541
Cdd:cd23460    2 LGQIKH-TESGLCLDwAGESNGDKTVaLKPCHGgGGNQFWMYTGDGQIR----------QDHLCLTAD-EGNKVTLRECA 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169790926 542 DVaRPTQRlWDFTQS-GPIVSRATGRCLEVEMSKDanfglRLVVQRCSG----QKWMIR 595
Cdd:cd23460   70 DQ-LPSQE-WSYDEKtGTIRHRSTGLCLTLDANND-----VVILKECDSnslwQKWIFQ 121

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 169790926 466 GEVRNSKaSAYCLDQ-GAEDGDRAILYPCHGM-SSQLVRYSADGLLQlgplgstaflPDSKCLvDDGTGRMP-TLKKCeD 542
Cdd:cd23433    7 GEIRNVE-TNLCLDTmGRKAGEKVGLSSCHGQgGNQVFSYTAKGEIR----------SDDLCL-DASRKGGPvKLEKC-H 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 169790926 543 VARPTQrLWDF-TQSGPIVSRATGRCLEVEMSKDANfglRLVVQRCSG---QKWMIRN 596
Cdd:cd23433   74 GMGGNQ-EWEYdKETKQIRHVNSGLCLTAPNEDDPN---EPVLRPCDGgpsQKWELEG 127

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 169790926 461 NTLTYGEVRNSKaSAYCLD--QGAEDGDRAI-LYPCHGM--SSQLVRYSADGLLQlgplgstaflPDSKCL-VDDGTGRM 534
Cdd:cd23459    3 DVLAYGQVRNPG-TNLCLDtlQRDEDKGYNLgLYPCQGGlsSNQLFSLSKKGELR----------REESCAdVQGTEESK 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169790926 535 PTLKKCEDVARPTQRlWDFTQSGPIVSRATGRCLEVEMSKDanfGLRLVVQRCSG---QKW 592
Cdd:cd23459   72 VILITCHGLEKFNQK-WKHTKGGQIVHLASGKCLDAEGLKS---GDDVTLAKCDGslsQKW 128

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 169790926 464 TYGEVRNsKASAYCLD---QGAEDGDRAILYPCHGMSSQL--VRYSADGLLQLGPLGStaflpdSKCL-VDDGT---GRM 534
Cdd:cd00161    1 GTYRIVN-AASGKCLDvagGSTANGAPVQQWTCNGGANQQwtLTPVGDGYYTIRNVAS------GKCLdVAGGStanGAN 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169790926 535 PTLKKCEDvaRPTQRlWDFTQSGP----IVSRATGRCLEVEMSKDANfGLRLVVQRCSG---QKW 592
Cdd:cd00161   74 VQQWTCNG--GDNQQ-WRLEPVGDgyyrIVNKHSGKCLDVSGGSTAN-GANVQQWTCNGganQQW 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 169790926 155 VVFIFVNEAlSVILRSVHSVVNHTPSQLlkEVILVDDNS-DNVELKfnLDQYVNKRYPglVKIVRNSRREGLIRARLQGW 233
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGStDGTLEI--LEEYAKKDPR--VIRVINEENQGLAAARNAGL 73

                         90       100       110
                 ....*....|....*....|....*....|...
gi 169790926 234 KAATAPVVGFFDAHVEFNTGWAEPALSRIREDR 266
Cdd:cd00761   74 KAARGEYILFLDADDLLLPDWLERLVAELLADP 106

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 169790926 158 IFVN-EALSVILRSVHSVVNHTPSQLlkEVILVDDNSDnvelkfnlDQYVN--KRYPGLVKIVRNSRREGLIRARLQGWK 234
Cdd:cd04186    2 IIVNyNSLEYLKACLDSLLAQTYPDF--EVIVVDNAST--------DGSVEllRELFPEVRLIRNGENLGFGAGNNQGIR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790926 235 AATAPVVGFFDAHVEFNTGWAEPALSRIREDRrrivlpaidnikystfevqqyanaahgyNWGLWCmyiippqdwldrgd 314
Cdd:cd04186   72 EAKGDYVLLLNPDTVVEPGALLELLDAAEQDP----------------------------DVGIVG-------------- 109

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169790926 315 esapirtPAMIGCSFVVDREYFGDIGLLDPGMEVYgGENVELGMRVWQCGGSMEVLPCSRVAHIE 379
Cdd:cd04186  110 -------PKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYHHG 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 169790926 477 CLDQ-GAEDGDRAILYPCHGM-SSQLVRYSADGLLQlgplgstaflPDSKCL-VDDGTGRMP-TLKKCEDVARPTQrlWD 552
Cdd:cd23434   11 CLDTlGHKAGGTVGLYPCHGTgGNQEWSFTKDGQIK----------HDDLCLtVVDRAPGSLvTLQPCREDDSNQK--WE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 169790926 553 FTQSGP-IVSRATGRCLEvemSKDANfGLRLVVQRCSG----QKW 592
Cdd:cd23434   79 QIENNSkLRHVGSNLCLD---SRNAK-SGGLTVETCDPssgsQQW 119

ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine protease I (RPI) and similar proteins; RPI, also called serine protease 1, is a major serine protease exhibiting lytic activity toward living yeast cells. It has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI. RPI contains a C-terminal 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 bears a potential sugar binding site.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790926 467 EVRNSKASaycldqgaeDGDRAILYPCHGMSSQLVRYSADGLLQLGplgstaflpdSKCL------VDDGTGRMptLKKC 540
Cdd:cd23452   15 DVPNSSTT---------DGAPLQLWDCNGTNAQKWTFASDGTLRAL----------GKCLdvawggTDNGTAVQ--LWTC 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169790926 541 EdvARPTQRlWDFTQSGPIVSRATGRCLEVEMSKDANfGLRLVVQRCSG---QKW 592
Cdd:cd23452   74 S--GNPAQQ-FVLSGAGDLVNPQANKCVDVSGGNSGN-GTRLQLWECSGnanQKW 124

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 169790926 161 NEALSvILRSVHSVVNHTPSQLLKEVILVDDNS-DN-VELkfnLDQYVnKRYPGlVKIVRNSRREGLIRARLQGWKAATA 238
Cdd:cd04179    7 NEEEN-IPELVERLLAVLEEGYDYEIIVVDDGStDGtAEI---ARELA-ARVPR-VRVIRLSRNFGKGAAVRAGFKAARG 80

                 ....*...
gi 169790926 239 PVVGFFDA 246
Cdd:cd04179   81 DIVVTMDA 88

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 169790926 466 GEVRNSKasaYCLDqGAEDGDRAILYPCHGMS-SQLVRYSA-DGLLQLGPLGstaflpdsKCL-VDDGTGRMpTLKKCED 542
Cdd:cd23462   50 GEIRRDD---LCLD-YAGGSGDVTLYPCHGMKgNQFWIYDEeTKQIVHGTSK--------KCLeLSDDSSKL-VMEPCNG 116

                         90
                 ....*....|.
gi 169790926 543 VArPTQRlWDF 553
Cdd:cd23462  117 SS-PRQQ-WEF 125

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 12 (GALNT12) and similar proteins; GALNT12 (EC 2.4.1.41), also called polypeptide GalNAc transferase 12, GalNAc-T12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12, 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. 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. GALNT12 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 169790926 465 YGEVRNSKASAYCLDQGAED-----GDRAILYPCHGM-SSQLVRYSAdgllqLGPLGSTAFLPDSKCLVDDGTGRMpTLK 538
Cdd:cd23471    4 FGMLKNKGMTNYCFDYNPPDehqiaGHQVILYQCHGMgQNQFFEYTS-----QNEIRYNTRQPEGCAAVDAGTDFL-TMH 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790926 539 KCED--VARPTQRLWDFTQSGPIVSRATGRCLE-VEMSKDANFGlrLVVQRCSG---QKW 592
Cdd:cd23471   78 LCREnrQAVPENQKFIFREDGSLFHVQTQKCVQaVRNESSGSPA--PVLRPCTDsdhQKW 135

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 169790926 464 TYGEVRNSKASAyCLDQ-GAEDGDRAILYPCHGM-SSQLVRYSADGLLQlgplgstaflPDSKCLVDDGTGRMPTLKKCE 541
Cdd:cd23467    5 SLGEIRNVETNQ-CLDNmGRKENEKVGIFNCHGMgGNQVFSYTADKEIR----------TDDLCLDVSRLNGPVVMLKCH 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169790926 542 DVaRPTQrLWDFTQSGPIVSRA-TGRCLEVEMSKDAnfgLRLVVQRCSG---QKWMIRN 596
Cdd:cd23467   74 HM-RGNQ-LWEYDAERLTLRHVnSNQCLDEPSEEDK---MVPTMKDCSGsrsQQWLLRN 127