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 442625712 493 PSYAAGIIQNVANPvYCLDNMG--KSTEEAVGMFSCADnrthPQPNQFWELSIFRDLRMkgfDSVCLDVHEGppNATVWM 570
Cdd:cd23462    1 EALAYGEIRNLAGK-LCLDAPGrkKELNKPVGLYPCHG----QGGNQYWMLTKDGEIRR---DDLCLDYAGG--SGDVTL 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442625712 571 WSCHSQGGNQFWYYDRQTQRLVHGeNNKRCLEgfVENGIAKVVANSCENGNDRQRWEFG 629
Cdd:cd23462   71 YPCHGMKGNQFWIYDEETKQIVHG-TSKKCLE--LSDDSSKLVMEPCNGSSPRQQWEFE 126

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 442625712 493 PSYAAGIIQNVANPvYCLDNMG--KSTEEAVGMFSCADnrthPQPNQFWELSIFRDLRMkgfDSVCLDVHEGppNATVWM 570
Cdd:cd23462    1 EALAYGEIRNLAGK-LCLDAPGrkKELNKPVGLYPCHG----QGGNQYWMLTKDGEIRR---DDLCLDYAGG--SGDVTL 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442625712 571 WSCHSQGGNQFWYYDRQTQRLVHGeNNKRCLEgfVENGIAKVVANSCENGNDRQRWEFG 629
Cdd:cd23462   71 YPCHGMKGNQFWIYDEETKQIVHG-TSKKCLE--LSDDSSKLVMEPCNGSSPRQQWEFE 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 442625712  181 SVIFIFFNEhFNTLLRSIYSVINRTPPELlkQIVLVDDGSEwDVLKQPLDDYVQQhfPHLVTIVRNPERQGLIGARIAGA 260
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGST-DGTVEIAEEYAKK--DPRVRVIRLPENRGKAGARNAGL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625712  261 KVAVGQVMVFFDSHIEVNYNWLPPLIEPIAINPKISTCPMVDTISHEDFSYfsgnkdgarggfdWKMLYKQLPVLPEDAL 340
Cdd:pfam00535  75 RAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY-------------RRASRITLSRLPFFLG 141

                         170       180
                  ....*....|....*....|....*
gi 442625712  341 DKSMPYRSPVMMGGLFAINTDFFWD 365
Cdd:pfam00535 142 LRLLGLNLPFLIGGFALYRREALEE 166

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625712 178 PNISVIFIFFNEHfNTLLRSIYSVINRTPPELlkQIVLVDDGSE---WDVLKQplddYVQQHfpHLVTIVRNPERQGLIG 254
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTdgtAEILRE----LAAKD--PRIRVIRLERNRGKGA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625712 255 ARIAGAKVAVGQVMVFFDSHIEVNYNWLPPLIEPIAINPkistcpmvdtishEDFSYfsGNKDGARGGFDWKMLYKQLPV 334
Cdd:COG0463   73 ARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGP-------------ADLVY--GSRLIREGESDLRRLGSRLFN 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625712 335 LpedaldKSMPYRSPVMMGGLFAINTDFFWDLgGYDDQLdiwgGEQYELsFKIWMCGGMLLDVPCSRVAH 404
Cdd:COG0463  138 L------VRLLTNLPDSTSGFRLFRREVLEEL-GFDEGF----LEDTEL-LRALRHGFRIAEVPVRYRAG 195

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 442625712 493 PSYAAGIIQNVANPvYCLDNMG--KSTEEAVGMFSCADnrthPQPNQFWELSIFRDLRMkgfDSVCLDVHEGppNATVWM 570
Cdd:cd23462    1 EALAYGEIRNLAGK-LCLDAPGrkKELNKPVGLYPCHG----QGGNQYWMLTKDGEIRR---DDLCLDYAGG--SGDVTL 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442625712 571 WSCHSQGGNQFWYYDRQTQRLVHGeNNKRCLEgfVENGIAKVVANSCENGNDRQRWEFG 629
Cdd:cd23462   71 YPCHGMKGNQFWIYDEETKQIVHG-TSKKCLE--LSDDSSKLVMEPCNGSSPRQQWEFE 126

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625712  496 AAGIIQNVANPvYCLDNMGKSTE-EAVGMFSCADNRThpqpNQFWELSIFRDLRMKGfDSVCLDVHEGPPNATVWMWSCH 574
Cdd:pfam00652   1 ATGRIRNRASG-KCLDVPGGSSAgGPVGLYPCHGSNG----NQLWTLTGDGTIRSVA-SDLCLDVGSTADGAKVVLWPCH 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442625712  575 SQGGNQFWYYDRQTQRLVHGENNKrCLEGFVENGIA-KVVANSCENGNDRQRW 626
Cdd:pfam00652  75 PGNGNQRWRYDEDGTQIRNPQSGK-CLDVSGAGTSNgKVILWTCDSGNPNQQW 126

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 442625712 496 AAGIIQNVAnPVYCLDNMGKSTEEAVGMFSCADNRThpQPNQFWELSIFRDLRMKGfDSVCLDVHEGPPNATVWMWSCHS 575
Cdd:cd23439    1 ASGEIRNVG-SGLCIDTKHGGENDEVRLSKCVKDGG--GGEQQFELTWHEDIRPKK-RKVCFDVSSHTPGAPVILYACHG 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442625712 576 QGGNQFWYYDRQTQRLVHGENNKrCLEGFVENGiaKVVANSCENGNDRQRWEF 628
Cdd:cd23439   77 MKGNQLWKYRPNTKQLYHPVSGL-CLDADPGSG--KVFMNHCDESSDTQKWTW 126

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625712   509 CLDNMGKSTEeaVGMFSCadnrTHPQPNQFWELSIFRDLRMKGFDsVCLDVhEGPPNATVWMWSCHSQGGNQFWYYDrQT 588
Cdd:smart00458   9 CLDVNGNKNP--VGLFDC----HGTGGNQLWKLTSDGAIRIKDTD-LCLTA-NGNTGSTVTLYSCDGTNDNQYWEVN-KD 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 442625712   589 QRLVHGENNKrCLEGFVENGIAKVVANSCeNGNDRQRWEF 628
Cdd:smart00458  80 GTIRNPDSGK-CLDVKDGNTGTKVILWTC-SGNPNQKWIF 117

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625712  552 FDSVCLDVHEG-PPNATVWMWSCHSQGGNQFWYYDRQtqRLVHGENNKRCLEGFVENGIAKVVANSCENGNDRQRWEFGf 630
Cdd:pfam00652   9 ASGKCLDVPGGsSAGGPVGLYPCHGSNGNQLWTLTGD--GTIRSVASDLCLDVGSTADGAKVVLWPCHPGNGNQRWRYD- 85

                  ....*.
gi 442625712  631 VNHTML 636
Cdd:pfam00652  86 EDGTQI 91

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 442625712 495 YAAGIIQNVANPvYCLDNMGKSTEEAVGMFSCadnrtHPQP-NQFWELSIFRDLRMkgfDSVCLDVHEgpPNATVWMWSC 573
Cdd:cd23466    4 FSLGEIRNVETN-QCLDNMARKENEKVGIFNC-----HGMGgNQVFSYTANKEIRT---DDLCLDVSK--LNGPVMMLKC 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442625712 574 HSQGGNQFWYYDRQTQRLVHgENNKRCLEGFVENGIAKVVANSCeNGNDRQRW 626
Cdd:cd23466   73 HHLKGNQLWEYDPVKLTLLH-VNSNQCLDKATEEDSQVPSIRDC-NGSRSQQW 123

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 442625712 495 YAAGIIQNVANPvYCLDNMGKSTEEAVGMFSCadnrtHPQP-NQFWELSIFRDLRMkgfDSVCLDVHEgpPNATVWMWSC 573
Cdd:cd23467    4 YSLGEIRNVETN-QCLDNMGRKENEKVGIFNC-----HGMGgNQVFSYTADKEIRT---DDLCLDVSR--LNGPVVMLKC 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442625712 574 HSQGGNQFWYYDRQTQRLVHgENNKRCLEGFVENGIAKVVANSCeNGNDRQRW 626
Cdd:cd23467   73 HHMRGNQLWEYDAERLTLRH-VNSNQCLDEPSEEDKMVPTMKDC-SGSRSQQW 123

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625712 178 PNISVIFIFFNEHfNTLLRSIYSVINRTPPELlkQIVLVDDGSE---WDVLKQplddYVQQHfpHLVTIVRNPERQGLIG 254
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTdgtAEILRE----LAAKD--PRIRVIRLERNRGKGA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625712 255 ARIAGAKVAVGQVMVFFDSHIEVNYNWLPPLIEPIAINPkistcpmvdtishEDFSYfsGNKDGARGGFDWKMLYKQLPV 334
Cdd:COG0463   73 ARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGP-------------ADLVY--GSRLIREGESDLRRLGSRLFN 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625712 335 LpedaldKSMPYRSPVMMGGLFAINTDFFWDLgGYDDQLdiwgGEQYELsFKIWMCGGMLLDVPCSRVAH 404
Cdd:COG0463  138 L------VRLLTNLPDSTSGFRLFRREVLEEL-GFDEGF----LEDTEL-LRALRHGFRIAEVPVRYRAG 195

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 442625712 182 VIFIFFNEhFNTLLRSIYSVINRTPPELlkQIVLVDDGSEwDVLKQPLDDYVQQHFPhlVTIVRNPERQGLIGARIAGAK 261
Cdd:cd00761    1 VIIPAYNE-EPYLERCLESLLAQTYPNF--EVIVVDDGST-DGTLEILEEYAKKDPR--VIRVINEENQGLAAARNAGLK 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442625712 262 VAVGQVMVFFDSHIEVNYNWLPPLIEPIAINPK--ISTCPMVDTISHEDFSYFSGNKDGARGGFDWKMLYKQL 332
Cdd:cd00761   75 AARGEYILFLDADDLLLPDWLERLVAELLADPEadAVGGPGNLLFRRELLEEIGGFDEALLSGEEDDDFLLRL 147

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625712 496 AAGIIQNvanPVYCLDNMGKST--EEAVGMFSCADNrthpQPNQFWELSIFRDLRMKGFdsvCLDVHEGPPNATVWMWSC 573
Cdd:cd23441    4 AYGQIKQ---GNLCLDSDEQLFqgPALLILAPCSNS----SDSQEWSFTKDGQLQTQGL---CLTVDSSSKDLPVVLETC 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442625712 574 hSQGGNQFWyyDRQTQRLVHGENNKrCLEGFVEngiAKVVANSCENGNDRQRWEF 628
Cdd:cd23441   74 -SDDPKQKW--TRTGRQLVHSESGL-CLDSRKK---KGLVVSPCRSGAPSQKWDF 121

ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar proteins; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cytolysis by forming heptameric pores in target host membranes. After binding to target membranes, the protein assembles into a heptameric pre-pore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation. Hemolysin may be called "cytolysin" or "cytolytic toxin", according to a specific action for certain cells. For example, this subfamily includes Vibrio vulnificus cytolysin that attack blood cell membranes and cause cell rupture, thereby liberating hemoglobins. Members of this subfamily contain 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 may harbor a putative sugar-binding pocket.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442625712 551 GFDSVCLDVhegPPNATVWMWSCHSQGGNQFWYYDrQTQRLVHGENNKRCLEGfveNGIAKVVANSCENgNDRQRWE 627
Cdd:cd23423   11 SFNNRCLTV---DNNGRVTLESCDSGDRNQSWILD-SEGRYRSRVAPDLCLDA---DDDGLLTLEQCSL-SLTQKWE 79

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 442625712 498 GIIQNVANPvYCLD------NMGKSteeaVGMFSCadnrtHPQP-NQFWELSIFRDLRMKGFDSVCLDVhegPPNATVWM 570
Cdd:cd23435    5 GALRNKGSE-LCLDvnnpngQGGKP----VIMYGC-----HGLGgNQYFEYTSKGEIRHNIGKELCLHA---SGSDEVIL 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442625712 571 WSCHSQG----GNQFWYYdRQTQRLVHGENNKrCLEGfvenGIAKVVANSCENGNDRQRWEFG 629
Cdd:cd23435   72 QHCTSKGkdvpPEQKWLF-TQDGTIRNPASGL-CLHA----SGYKVLLRTCNPSDDSQKWTFI 128

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 442625712 182 VIFIFFNeHFNTLLRSIYSVINRTPPELlkQIVLVDDGSEWDVLkqpldDYVQQHFPHlVTIVRNPERQGLIGARIAGAK 261
Cdd:cd04186    1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVDNASTDGSV-----ELLRELFPE-VRLIRNGENLGFGAGNNQGIR 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 442625712 262 VAVGQVMVFFDSHIEVNYNWLPPLIEPIAINPKI 295
Cdd:cd04186   72 EAKGDYVLLLNPDTVVEPGALLELLDAAEQDPDV 105

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 442625712 556 CLDVHEG--PPNATVWMWSCHSqGGNQFWYYDRQTQ---RLVHGENNKrCLE---GFVENGiAKVVANSCeNGNDRQRWE 627
Cdd:cd00161   13 CLDVAGGstANGAPVQQWTCNG-GANQQWTLTPVGDgyyTIRNVASGK-CLDvagGSTANG-ANVQQWTC-NGGDNQQWR 88

                 .
gi 442625712 628 F 628
Cdd:cd00161   89 L 89

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625712 556 CLDVHEG--PPNATVWMWSCHSqGGNQFWYYDRqTQRLVHGENnkRCL---EGFVENGiAKVVANSCeNGNDRQRWEFG 629
Cdd:cd23418   16 CLDVPGGstTNGTRLILWDCHG-GANQQFTFTS-AGELRVGGD--KCLdaaGGGTTNG-TPVVIWPC-NGGANQKWRFN 88

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 442625712 197 SIYSVINRTPPELLK----QIVLVDDGSE---WDVLKQplddyVQQHFPHlVTIVRNPERQGLIGARIAGAKVAVGQVMV 269
Cdd:cd04179   11 NIPELVERLLAVLEEgydyEIIVVDDGSTdgtAEIARE-----LAARVPR-VRVIRLSRNFGKGAAVRAGFKAARGDIVV 84

                         90       100
                 ....*....|....*....|....*
gi 442625712 270 FFDS----HIEVnynwLPPLIEPIA 290
Cdd:cd04179   85 TMDAdlqhPPED----IPKLLEKLL 105

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442625712 556 CLDVHegpPNATVWMWSCHSqGGNQFWYY--DRQTQRLVHGENNKRCLEGfveNGIAKVVANSCeNGNDRQRWEFG 629
Cdd:cd23415   13 CLDSN---AGGNVYTGPCNG-GPYQRWTWsgVGDGTVTLRNAATGRCLDS---NGNGGVYTLPC-NGGSYQRWRVT 80

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625712 180 ISVIFIFFNEHfNTLLRSIYSVINRTPPELLKQIVLVDDGSE---WDVLKQplddyVQQHFPHlVTIVRNPERQgLIGAR 256
Cdd:cd02525    2 VSIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTdgtREIVQE-----YAAKDPR-IRLIDNPKRI-QSAGL 73