ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10) and similar proteins; GALNT10 (EC 2.4.1.41), also called polypeptide GalNAc transferase 10, GalNAc-T10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, 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. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. GALNT10 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 1907080264 255 EPPAAAWGEIRNVGTGLCTDTKLGTLGSPLRLETCIRGRGEAAWNSMQVFTFTWREDIRPGDPQHTKKFCFDAVSHTSPV 334
Cdd:cd23476     1 EPPAAAWGEIRNVGTGLCADTKHGALGSPLRLEGCVKGRGEAAWNNGQVFTFGWREDIRPGDPQHTKKFCFDAISHNSPV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264 335 TLYDCHSMKGNQLWKYRKDKTLYHPVSGSCMDCSESDHRVFMNTCNPSSLTQQWLFEHTNSTVLENFNKN 404
Cdd:cd23476    81 TLYDCHGMKGNQLWRYRKDKTLYHPVSNSCMDCSESDHRIFMNTCNPSSPTQQWLFEHTNSTVLEKFNRN 150

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10) and similar proteins; GALNT10 (EC 2.4.1.41), also called polypeptide GalNAc transferase 10, GalNAc-T10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, 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. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. GALNT10 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 1907080264 255 EPPAAAWGEIRNVGTGLCTDTKLGTLGSPLRLETCIRGRGEAAWNSMQVFTFTWREDIRPGDPQHTKKFCFDAVSHTSPV 334
Cdd:cd23476     1 EPPAAAWGEIRNVGTGLCADTKHGALGSPLRLEGCVKGRGEAAWNNGQVFTFGWREDIRPGDPQHTKKFCFDAISHNSPV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264 335 TLYDCHSMKGNQLWKYRKDKTLYHPVSGSCMDCSESDHRVFMNTCNPSSLTQQWLFEHTNSTVLENFNKN 404
Cdd:cd23476    81 TLYDCHGMKGNQLWRYRKDKTLYHPVSNSCMDCSESDHRIFMNTCNPSSPTQQWLFEHTNSTVLEKFNRN 150

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264  264 IRNVGTGLCTDTKLGtlGSPLRLETCIRGrgeaawNSMQVFTFTWREDIRPGDPQhtkkFCFDAVSHT-SPVTLYDCHSM 342
Cdd:smart00458   1 IISGNTGKCLDVNGN--KNPVGLFDCHGT------GGNQLWKLTSDGAIRIKDTD----LCLTANGNTgSTVTLYSCDGT 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907080264  343 KGNQLWKYRKDKTLYHPVSGSCMDCSESDH--RVFMNTCNPSSlTQQWLFE 391
Cdd:smart00458  69 NDNQYWEVNKDGTIRNPDSGKCLDVKDGNTgtKVILWTCSGNP-NQKWIFE 118

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264   2 ALFPSVRILRTKKREGLIRTRMLGASAATGDVVTFLDSHCEANVNWLPPLLDRIARNRktivcpmIDVIDHDdfRYETQA 81
Cdd:COG0463    54 AKDPRIRVIRLERNRGKGAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGP-------ADLVYGS--RLIREG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264  82 GDAMRGAFDWEMYYKRIpippelqkadpsdPFESPVMAGGLFAVDRKWFWELgGYDPGLeiwgGEQYEIsFKVWMCGGRM 161
Cdd:COG0463   125 ESDLRRLGSRLFNLVRL-------------LTNLPDSTSGFRLFRREVLEEL-GFDEGF----LEDTEL-LRALRHGFRI 185

                  ....
gi 1907080264 162 EDIP 165
Cdd:COG0463   186 AEVP 189

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10) and similar proteins; GALNT10 (EC 2.4.1.41), also called polypeptide GalNAc transferase 10, GalNAc-T10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, 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. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. GALNT10 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 1907080264 255 EPPAAAWGEIRNVGTGLCTDTKLGTLGSPLRLETCIRGRGEAAWNSMQVFTFTWREDIRPGDPQHTKKFCFDAVSHTSPV 334
Cdd:cd23476     1 EPPAAAWGEIRNVGTGLCADTKHGALGSPLRLEGCVKGRGEAAWNNGQVFTFGWREDIRPGDPQHTKKFCFDAISHNSPV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264 335 TLYDCHSMKGNQLWKYRKDKTLYHPVSGSCMDCSESDHRVFMNTCNPSSLTQQWLFEHTNSTVLENFNKN 404
Cdd:cd23476    81 TLYDCHGMKGNQLWRYRKDKTLYHPVSNSCMDCSESDHRIFMNTCNPSSPTQQWLFEHTNSTVLEKFNRN 150

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 1907080264 260 AWGEIRNVGTGLCTDTKLGTLGSPLRLETCIRGRgeaaWNSMQVFTFTWREDIRPGDpqhtKKFCFDAVSHT--SPVTLY 337
Cdd:cd23439     1 ASGEIRNVGSGLCIDTKHGGENDEVRLSKCVKDG----GGGEQQFELTWHEDIRPKK----RKVCFDVSSHTpgAPVILY 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907080264 338 DCHSMKGNQLWKYR-KDKTLYHPVSGSCMDCSESDHRVFMNTCNPSSLTQQWLF 390
Cdd:cd23439    73 ACHGMKGNQLWKYRpNTKQLYHPVSGLCLDADPGSGKVFMNHCDESSDTQKWTW 126

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264 260 AWGEIRNVGTGLCTDTKLG-TLGSPLRLETCIRGRGEaawnsmQVFTFTWREDIRPGDPQhtkkFCFDAVSHT--SPVTL 336
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPGGsSAGGPVGLYPCHGSNGN------QLWTLTGDGTIRSVASD----LCLDVGSTAdgAKVVL 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907080264 337 YDCHSMKGNQLWKYRKD-KTLYHPVSGSCMDCSESDH---RVFMNTCNPSSLTQQW 388
Cdd:pfam00652  71 WPCHPGNGNQRWRYDEDgTQIRNPQSGKCLDVSGAGTsngKVILWTCDSGNPNQQW 126

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 1907080264 262 GEIRNVGTGLCTDTKLGTLGSPLRLETCiRGRGeaawnSMQVFTFTWREDIRPGDPqhtkkfCFDAVSHTSPVTLYDCHS 341
Cdd:cd23433     7 GEIRNVETNLCLDTMGRKAGEKVGLSSC-HGQG-----GNQVFSYTAKGEIRSDDL------CLDASRKGGPVKLEKCHG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907080264 342 MKGNQLWKYRKD-KTLYHPVSGSCMDCSESDH--RVFMNTCNPSSlTQQWLFE 391
Cdd:cd23433    75 MGGNQEWEYDKEtKQIRHVNSGLCLTAPNEDDpnEPVLRPCDGGP-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 1907080264   1 MALFPSVRILRTKKREGLIRTRMLGASAATGDVVTFLDSHCEANVNWLPPLLDRIARNRKTIVCPMIDVIDHDDFRYEtq 80
Cdd:pfam00535  49 AKKDPRVRVIRLPENRGKAGARNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR-- 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907080264  81 agdaMRGAFDWEMYYKRIpippELQKADPSDPFESPVMAGGLFAVDRK 128
Cdd:pfam00535 127 ----RASRITLSRLPFFL----GLRLLGLNLPFLIGGFALYRREALEE 166

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 1907080264 262 GEIRNVGTGLCTDTK--LGTLGSPLRLETCiRGRGEAawnsmQVFTFTWREDIRpgdpqHT--KKFCFDAVSHTsPVTLY 337
Cdd:cd23435     5 GALRNKGSELCLDVNnpNGQGGKPVIMYGC-HGLGGN-----QYFEYTSKGEIR-----HNigKELCLHASGSD-EVILQ 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907080264 338 DCHSMK----GNQLWKYRKDKTLYHPVSGSCMDCSESDhrVFMNTCNPSSLTQQWLFE 391
Cdd:cd23435    73 HCTSKGkdvpPEQKWLFTQDGTIRNPASGLCLHASGYK--VLLRTCNPSDDSQKWTFI 128

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1) and similar proteins; GALNT1 (EC 2.4.1.41), also called polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 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. It has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT1 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 is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264 262 GEIRNVGTGLCTDTKLGTLGSPLRLETCiRGRGeaawnSMQVFTFTWREDIRPGDpqhtkkFCFDAVSHTSPVTLYDCHS 341
Cdd:cd23466     7 GEIRNVETNQCLDNMARKENEKVGIFNC-HGMG-----GNQVFSYTANKEIRTDD------LCLDVSKLNGPVMMLKCHH 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907080264 342 MKGNQLWKYRKDK-TLYHPVSGSCMD-CSESDHRV-FMNTCNpSSLTQQWLFEH 392
Cdd:cd23466    75 LKGNQLWEYDPVKlTLLHVNSNQCLDkATEEDSQVpSIRDCN-GSRSQQWLLRN 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 1907080264 260 AWGEIRNVGTGLCTDT--KLGTLGSPLRLETCirgrGEAAWNSmQVFTFTWREDIRpgdpqhTKKFCFDAVSH-TSPVTL 336
Cdd:cd23459     6 AYGQVRNPGTNLCLDTlqRDEDKGYNLGLYPC----QGGLSSN-QLFSLSKKGELR------REESCADVQGTeESKVIL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907080264 337 YDCH-SMKGNQLWKYRKDKTLYHPVSGSCMDCSESDH--RVFMNTCNPSSLtQQWLFEH 392
Cdd:cd23459    75 ITCHgLEKFNQKWKHTKGGQIVHLASGKCLDAEGLKSgdDVTLAKCDGSLS-QKWTFEH 132

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 1907080264 261 WGEIRNVGTGLCTDT--KLGTLGSPLRLETCIRGRGEaawnsmQVFTFTWREDIRPGDPQhtkkFCFDaVSHTSpVTLYD 338
Cdd:cd23442     5 SGQLYNTGTGYCADYihGWRLAGGPVELSPCSGQNGN------QLFEYTSDKEIRFGSLQ----LCLD-VRQEQ-VVLQN 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907080264 339 CHSMKGNQLWKYRKDKTLYHPVSGSCMDCSESDHR--VFMNTCNPSSlTQQW 388
Cdd:cd23442    73 CTKEKTSQKWDFQETGRIVHILSGKCIEAVESENSklLFLSPCNGQR-NQMW 123

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264 260 AWGEIRNVG-TGLCTDTKLGTLGSPLRLETCIRGRGEAawNSMQVFTFTWREDIRPGdpqhTKKFCFDAVSHTspVTLYD 338
Cdd:cd23461     2 ASGVIQSVAfPNLCLDILGRSHGGPPVLAKCSSNKSMP--GTFQNFSLTFHRQIKHG----TSDDCLEVRGNN--VRLSR 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907080264 339 CHSMKGNQLWKYR-KDKTLYHPVSGS-CMDCSESDHRVFMNTCNPSSLTQQWLF 390
Cdd:cd23461    74 CHYQGGNQYWKYDyETHQLINGGQNNkCLEADVESLKITLSICDSDNVEQKWKW 127

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 1907080264 262 GEIRNvgTGLCTDTKLGTLGSPLRLETCIRGRGEAAWnsmqvfTFTWREDIRPGDpqhtkkFCFDAVSHT--SPVTLYDC 339
Cdd:cd23434     3 GSLKQ--GNLCLDTLGHKAGGTVGLYPCHGTGGNQEW------SFTKDGQIKHDD------LCLTVVDRApgSLVTLQPC 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907080264 340 HSMKGNQLWKYRK-DKTLYHPVSGSCMDCS-ESDHRVFMNTCNPSSLTQQWLF 390
Cdd:cd23434    69 REDDSNQKWEQIEnNSKLRHVGSNLCLDSRnAKSGGLTVETCDPSSGSQQWKF 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 1907080264 260 AWGEIRNVGTGLCTDTKLGTL--GSPLRLETCirgrgeaAWNSMQVFTFTWRED----IRpgdPQHTKKfCFDAVSHT-- 331
Cdd:cd00161     1 GTYRIVNAASGKCLDVAGGSTanGAPVQQWTC-------NGGANQQWTLTPVGDgyytIR---NVASGK-CLDVAGGSta 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907080264 332 --SPVTLYDCHSmKGNQLWKYRK----DKTLYHPVSGSCMDCSESDH----RVFMNTCNpSSLTQQW 388
Cdd:cd00161    70 ngANVQQWTCNG-GDNQQWRLEPvgdgYYRIVNKHSGKCLDVSGGSTangaNVQQWTCN-GGANQQW 134

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264   2 ALFPSVRILRTKKREGLIRTRMLGASAATGDVVTFLDSHCEANVNWLPPLLDRIARNRktivcpmIDVIDHDdfRYETQA 81
Cdd:COG0463    54 AKDPRIRVIRLERNRGKGAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGP-------ADLVYGS--RLIREG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264  82 GDAMRGAFDWEMYYKRIpippelqkadpsdPFESPVMAGGLFAVDRKWFWELgGYDPGLeiwgGEQYEIsFKVWMCGGRM 161
Cdd:COG0463   125 ESDLRRLGSRLFNLVRL-------------LTNLPDSTSGFRLFRREVLEEL-GFDEGF----LEDTEL-LRALRHGFRI 185

                  ....
gi 1907080264 162 EDIP 165
Cdd:COG0463   186 AEVP 189

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264 257 PAAAWGEIRNVGTGLCTDTKLG--TLGSPLRLETCIRGrgeaawnSMQVFTFTWREDIRpgdpqHTKKFCFDA----VSH 330
Cdd:cd23418     1 PGAGGGQIRGYGSGRCLDVPGGstTNGTRLILWDCHGG-------ANQQFTFTSAGELR-----VGGDKCLDAagggTTN 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907080264 331 TSPVTLYDCHSmKGNQLWKYRKDKTLYHPVSGSCMD 366
Cdd:cd23418    69 GTPVVIWPCNG-GANQKWRFNSDGTIRNVNSGLCLD 103

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 1907080264 261 WGEIRNVGTGLCTDTKLGTLG-SPLRLETCiRGRGeaawnSMQVFTFTWREDIRpgdpqHT--KKFCFDavSHTSPVTLY 337
Cdd:cd23470     4 YGAIKNEGTNQCLDVGENNRGgKPLIMYSC-HGMG-----GNQYFEYTTHKELR-----HNiaKQLCLR--VSKGPVQLG 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907080264 338 DCH------SMKGNQLWKYRKDKTLYHPVSGSCMdcSESDHRVFMNTCNPSSLTQQWLF 390
Cdd:cd23470    71 ECHykgknsQVPPDEEWELTQDHLIRNSGSNMCL--TARGKHPAMAPCNPADPHQLWSF 127

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 1907080264 256 PPAAAWGEIRNVGTGLCtdtkLGTLGSPLRLETCirgrgeAAWNSMQVFTFTWREDIRPGDpqhtkkFCFDAVSHTSPVT 335
Cdd:cd23436     1 PLVKASGLLVNVALRKC----IAIENTTLTLQDC------DLNNKSQHFNYTWLRLIRQGE------LCLAPVEAEGALT 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907080264 336 LYDCHSMKGNQLWKYRKDKTL-----------YHPVSgsCMDCSESDHRVFMNTCNPSSLTQQWLFEH 392
Cdd:cd23436    65 LHPCDNTNNGLRWLHKSLIAFpelmdhimlehQSQPT--CLEADPSQKILRLNACDSFKRYQKWRFGH 130

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264   4 FPSVRILRTKKREGLIRTRMLGASAATGDVVTFLDSHCEANVNWLPPLLDriarnrktivcpmidvidhddfryetqagd 83
Cdd:COG1216    55 FPRVRVIRNPENLGFAAARNLGLRAAGGDYLLFLDDDTVVEPDWLERLLA------------------------------ 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264  84 amrgafdwemyykripippelqkadpsdpfespvmAGGLFaVDRKWFWELGGYDPGLEIWGGEqYEISFKVWMCGGRMED 163
Cdd:COG1216   105 -----------------------------------AACLL-IRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVY 147

                         170
                  ....*....|..
gi 1907080264 164 IPCSRVGHIYRK 175
Cdd:COG1216   148 VPDAVVYHLGGA 159

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 1907080264 284 LRLETCIRGRGEAAWNsmQVFTFTWREDIRPGdpqhtkKFCFDAvsHT----SPVTLYDCHSMKGNQLWkyRKDKT-LYH 358
Cdd:cd23478    32 LSLSPCIKSKGVPAKS--QEWAYTYNQQIRQQ------QLCLSV--HTlfpgSPVVLVPCKEGDGKQRW--TKVGShIEH 99

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907080264 359 PVSGSCMDC------SESDHRVFMNTCNPSSLTQQW 388
Cdd:cd23478   100 MASRFCLDTemfgdgTESSKEIVINPCESSAMSQRW 135

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080264 264 IRNVGTGLCTDTKLGtlGSPLRLETCIRGrgeaawNSMQVFTFTWREDIRPgdpQHTKKfCFDA--VSHTSPVTLYDCHS 341
Cdd:cd23385     5 IYNEDLGKCLAARSS--SSKVSLSTCNPN------SPNQQWKWTSGHRLFN---VGTGK-CLGVssSSPSSPLRLFECDS 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907080264 342 MKGNQLWKYRKDkTLYHPVSGSCMDCS-ESDHRVFmnTCNPSSLTQQW 388
Cdd:cd23385    73 EDELQKWKCSKD-GLLLLKGLGLLLLYdKSGKNVV--VSKGSGLSSRW 117