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Conserved domains on  [gi|51315979|sp|Q8BGT9|]
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RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 12; AltName: Full=Polypeptide GalNAc transferase 12; Short=GalNAc-T12; Short=pp-GaNTase 12; AltName: Full=Protein-UDP acetylgalactosaminyltransferase 12; AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 134-428 2.27e-162

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


:

Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 464.76  E-value: 2.27e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 134 SVVIAFYNEAWSTLLRTVYSVLETSPDILLEEVILVDDYSDREHLKERLANE-LSQLPKVRLIRASRREGLVRARLLGAS 212
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYyKKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 213 AARGEVLTFLDCHCECHEGWLEPLLQRIHEKESAVVCPVIDVIDWNTFEYLGnSGEPQIGGFDWRLVFTWHVVPQRERQS 292
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRG-SSGDARGGFDWSLHFKWLPLPEEERRR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 293 MrSPIDVIRSPTMAGGLFAVSKRYFDYLGSYDTGMEVWGGENLEFSFRIWQCGGTLETHPCSHVGHVFP-KQAPYS---- 367
Cdd:cd02510 160 E-SPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTfpgg 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51315979 368 RSKALANSVRAAEVWMDEFKELYYHRNPQARLEPFGDVTERKKLRAKLQCKDFKWFLDTVY 428
Cdd:cd02510 239 SGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 438-574 1.26e-79

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.


The actual alignment was detected with superfamily member cd23471:

Pssm-ID: 483949  Cd Length: 140  Bit Score: 246.63  E-value: 1.26e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 438 PGFFGMLQNRGLRGYCLDYNPPNENHVEGHQVLLYLCHGMGQNQFFEYTTRKEIRYNTRQPEACITVEDGKDTLVMDLCR 517
Cdd:cd23471   1 PGFFGMLKNKGMTNYCFDYNPPDEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTRQPEGCAAVDAGTDFLTMHLCR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 518 ET---VPENQEFILQEDGTLVHKHSRKCVEATEKVLDNGFAPYLRDCTNSDNQRWFFKER 574
Cdd:cd23471  81 ENrqaVPENQKFIFREDGSLFHVQTQKCVQAVRNESSGSPAPVLRPCTDSDHQKWFFKER 140
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 134-428 2.27e-162

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 464.76  E-value: 2.27e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 134 SVVIAFYNEAWSTLLRTVYSVLETSPDILLEEVILVDDYSDREHLKERLANE-LSQLPKVRLIRASRREGLVRARLLGAS 212
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYyKKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 213 AARGEVLTFLDCHCECHEGWLEPLLQRIHEKESAVVCPVIDVIDWNTFEYLGnSGEPQIGGFDWRLVFTWHVVPQRERQS 292
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRG-SSGDARGGFDWSLHFKWLPLPEEERRR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 293 MrSPIDVIRSPTMAGGLFAVSKRYFDYLGSYDTGMEVWGGENLEFSFRIWQCGGTLETHPCSHVGHVFP-KQAPYS---- 367
Cdd:cd02510 160 E-SPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTfpgg 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51315979 368 RSKALANSVRAAEVWMDEFKELYYHRNPQARLEPFGDVTERKKLRAKLQCKDFKWFLDTVY 428
Cdd:cd02510 239 SGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 438-574 1.26e-79

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.


Pssm-ID: 467349  Cd Length: 140  Bit Score: 246.63  E-value: 1.26e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 438 PGFFGMLQNRGLRGYCLDYNPPNENHVEGHQVLLYLCHGMGQNQFFEYTTRKEIRYNTRQPEACITVEDGKDTLVMDLCR 517
Cdd:cd23471   1 PGFFGMLKNKGMTNYCFDYNPPDEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTRQPEGCAAVDAGTDFLTMHLCR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 518 ET---VPENQEFILQEDGTLVHKHSRKCVEATEKVLDNGFAPYLRDCTNSDNQRWFFKER 574
Cdd:cd23471  81 ENrqaVPENQKFIFREDGSLFHVQTQKCVQAVRNESSGSPAPVLRPCTDSDHQKWFFKER 140
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 134-315 7.43e-35

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.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 129.05  E-value: 7.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979   134 SVVIAFYNEaWSTLLRTVYSVLETSPDILleEVILVDDYSdREHLKERLANELSQLPKVRLIRASRREGLVRARLLGASA 213
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979   214 ARGEVLTFLDCHCECHEGWLEPLLQRIHEKESAVVCPVIDVIDWNTFEYLgnsgepqiggfdWRLVFTWHVVPQRERQSM 293
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR------------RASRITLSRLPFFLGLRL 144

                         170       180
                  ....*....|....*....|..
gi 51315979   294 RSPIDVIRSPTMAGGLFAVSKR 315
Cdd:pfam00535 145 LGLNLPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
440-569 5.39e-25

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 100.30  E-value: 5.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979   440 FFGMLQNRGlRGYCLDYNPPNENhveGHQVLLYLCHGMGQNQFFEYTTRKEIRynTRQPEACITVEDGKD--TLVMDLCR 517
Cdd:pfam00652   1 ATGRIRNRA-SGKCLDVPGGSSA---GGPVGLYPCHGSNGNQLWTLTGDGTIR--SVASDLCLDVGSTADgaKVVLWPCH 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 51315979   518 ETVPeNQEFILQEDGT-LVHKHSRKCVEATEKVLDNGfAPYLRDC-TNSDNQRW 569
Cdd:pfam00652  75 PGNG-NQRWRYDEDGTqIRNPQSGKCLDVSGAGTSNG-KVILWTCdSGNPNQQW 126
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 131-249 1.38e-19

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 87.45  E-value: 1.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 131 PKTSVVIAFYNEAwSTLLRTVYSVLE-TSPDIlleEVILVDDYSD---REHLKERLAnelsQLPKVRLIRASRREGLVRA 206
Cdd:COG0463   2 PLVSVVIPTYNEE-EYLEEALESLLAqTYPDF---EIIVVDDGSTdgtAEILRELAA----KDPRIRVIRLERNRGKGAA 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 51315979 207 RLLGASAARGEVLTFLDCHCECHEGWLEPLLQRIHEKESAVVC 249
Cdd:COG0463  74 RNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY 116
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 447-572 1.57e-16

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 75.63  E-value: 1.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979    447 RGLRGYCLDYNPPNENHVeghqvlLYLCHGMGQNQFFEYTTRKEIRynTRQPEACITVEDGKDTLVMDL-CrETVPENQE 525
Cdd:smart00458   3 SGNTGKCLDVNGNKNPVG------LFDCHGTGGNQLWKLTSDGAIR--IKDTDLCLTANGNTGSTVTLYsC-DGTNDNQY 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 51315979    526 FILQEDGTLVHKHSRKCVEATEKvlDNGFAPYLRDCTNSDNQRWFFK 572
Cdd:smart00458  74 WEVNKDGTIRNPDSGKCLDVKDG--NTGTKVILWTCSGNPNQKWIFE 118
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 131-223 6.34e-04

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 42.34  E-value: 6.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979  131 PKTSVVIAFYNeAWSTLLRTVYSVLETSPDILleEVILVDDYSDrEHLKERLANELSQLPKVRLIrASRREGLVRARLLG 210
Cdd:PRK10073   6 PKLSIIIPLYN-AGKDFRAFMESLIAQTWTAL--EIIIVNDGST-DNSVEIAKHYAENYPHVRLL-HQANAGVSVARNTG 80

                         90
                 ....*....|...
gi 51315979  211 ASAARGEVLTFLD 223
Cdd:PRK10073  81 LAVATGKYVAFPD 93
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 134-428 2.27e-162

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 464.76  E-value: 2.27e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 134 SVVIAFYNEAWSTLLRTVYSVLETSPDILLEEVILVDDYSDREHLKERLANE-LSQLPKVRLIRASRREGLVRARLLGAS 212
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYyKKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 213 AARGEVLTFLDCHCECHEGWLEPLLQRIHEKESAVVCPVIDVIDWNTFEYLGnSGEPQIGGFDWRLVFTWHVVPQRERQS 292
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRG-SSGDARGGFDWSLHFKWLPLPEEERRR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 293 MrSPIDVIRSPTMAGGLFAVSKRYFDYLGSYDTGMEVWGGENLEFSFRIWQCGGTLETHPCSHVGHVFP-KQAPYS---- 367
Cdd:cd02510 160 E-SPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTfpgg 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51315979 368 RSKALANSVRAAEVWMDEFKELYYHRNPQARLEPFGDVTERKKLRAKLQCKDFKWFLDTVY 428
Cdd:cd02510 239 SGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 438-574 1.26e-79

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.


Pssm-ID: 467349  Cd Length: 140  Bit Score: 246.63  E-value: 1.26e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 438 PGFFGMLQNRGLRGYCLDYNPPNENHVEGHQVLLYLCHGMGQNQFFEYTTRKEIRYNTRQPEACITVEDGKDTLVMDLCR 517
Cdd:cd23471   1 PGFFGMLKNKGMTNYCFDYNPPDEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTRQPEGCAAVDAGTDFLTMHLCR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 518 ET---VPENQEFILQEDGTLVHKHSRKCVEATEKVLDNGFAPYLRDCTNSDNQRWFFKER 574
Cdd:cd23471  81 ENrqaVPENQKFIFREDGSLFHVQTQKCVQAVRNESSGSPAPVLRPCTDSDHQKWFFKER 140
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 438-572 4.22e-43

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.


Pssm-ID: 467313 [Multi-domain]  Cd Length: 128  Bit Score: 150.17  E-value: 4.22e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 438 PGFFGMLQNRGlRGYCLDYNPPNENhvEGHQVLLYLCHGMGQNQFFEYTTRKEIRYNTrQPEACITVeDGKDTLVMDLCR 517
Cdd:cd23435   1 PGYYGALRNKG-SELCLDVNNPNGQ--GGKPVIMYGCHGLGGNQYFEYTSKGEIRHNI-GKELCLHA-SGSDEVILQHCT 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 51315979 518 ET---VPENQEFILQEDGTLVHKHSRKCVEAtekvldNGFAPYLRDCTNSD-NQRWFFK 572
Cdd:cd23435  76 SKgkdVPPEQKWLFTQDGTIRNPASGLCLHA------SGYKVLLRTCNPSDdSQKWTFI 128
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 134-315 7.43e-35

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.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 129.05  E-value: 7.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979   134 SVVIAFYNEaWSTLLRTVYSVLETSPDILleEVILVDDYSdREHLKERLANELSQLPKVRLIRASRREGLVRARLLGASA 213
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979   214 ARGEVLTFLDCHCECHEGWLEPLLQRIHEKESAVVCPVIDVIDWNTFEYLgnsgepqiggfdWRLVFTWHVVPQRERQSM 293
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR------------RASRITLSRLPFFLGLRL 144

                         170       180
                  ....*....|....*....|..
gi 51315979   294 RSPIDVIRSPTMAGGLFAVSKR 315
Cdd:pfam00535 145 LGLNLPFLIGGFALYRREALEE 166
beta-trefoil_Ricin_GALNT4 cd23469
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 438-572 2.85e-27

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 4 (GALNT4) and similar proteins; GALNT4 (EC 2.4.1.41), also called polypeptide GalNAc transferase 4, GalNAc-T4, pp-GaNTase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4, 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. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT4 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.


Pssm-ID: 467347  Cd Length: 136  Bit Score: 106.91  E-value: 2.85e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 438 PGFFGMLQNRGLRGYCLDYNPPNENHVEGHqVLLYLCHGMGQNQFFEYTTRKEIRYNTRQpEACITVEDGKDTLVMDLCR 517
Cdd:cd23469   1 PGWHGAVRSMGISSECLDYNSPEHNPTGAH-LSLFGCHGQGGNQFFEYTSNKEIRFNSVT-ELCAEVPDQKNYIGMKHCP 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 518 E---TVPENQEFILQEDGTLVHKHSRKCVEATEKvlDNGFAPY-LRDCTNSD-NQRWFFK 572
Cdd:cd23469  79 KdgsPVPANIIWHFKEDGTIYHPHSGMCISAYRT--PEGRADVqMRTCDAGDkNQLWSFE 136
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
440-569 5.39e-25

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 100.30  E-value: 5.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979   440 FFGMLQNRGlRGYCLDYNPPNENhveGHQVLLYLCHGMGQNQFFEYTTRKEIRynTRQPEACITVEDGKD--TLVMDLCR 517
Cdd:pfam00652   1 ATGRIRNRA-SGKCLDVPGGSSA---GGPVGLYPCHGSNGNQLWTLTGDGTIR--SVASDLCLDVGSTADgaKVVLWPCH 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 51315979   518 ETVPeNQEFILQEDGT-LVHKHSRKCVEATEKVLDNGfAPYLRDC-TNSDNQRW 569
Cdd:pfam00652  75 PGNG-NQRWRYDEDGTqIRNPQSGKCLDVSGAGTSNG-KVILWTCdSGNPNQQW 126
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 451-572 2.54e-21

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.


Pssm-ID: 467340 [Multi-domain]  Cd Length: 126  Bit Score: 89.73  E-value: 2.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 451 GYCLDynPPNENHVEGHQVLLYLCHGMGQNQFFEYTTRKEIRYNtrqpEACITVEDGKDTLVMDLCRETvPENQEFIL-Q 529
Cdd:cd23462  14 KLCLD--APGRKKELNKPVGLYPCHGQGGNQYWMLTKDGEIRRD----DLCLDYAGGSGDVTLYPCHGM-KGNQFWIYdE 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 51315979 530 EDGTLVHKHSRKCVEatekVLDNGFAPYLRDCT-NSDNQRWFFK 572
Cdd:cd23462  87 ETKQIVHGTSKKCLE----LSDDSSKLVMEPCNgSSPRQQWEFE 126
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 437-570 8.83e-21

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.


Pssm-ID: 467320 [Multi-domain]  Cd Length: 124  Bit Score: 88.27  E-value: 8.83e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 437 RPGFFGMLQNRGLrGYCLDYNPpnENHVEGHQVLLYLCHGMGQNQFFEYTTRKEIRYNTRQpeACITVEDGKdtLVMDLC 516
Cdd:cd23442   1 APYFSGQLYNTGT-GYCADYIH--GWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSLQ--LCLDVRQEQ--VVLQNC 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 51315979 517 RETVpENQEFILQEDGTLVHKHSRKCVEATEKVlDNGFApYLRDCTNSDNQRWF 570
Cdd:cd23442  74 TKEK-TSQKWDFQETGRIVHILSGKCIEAVESE-NSKLL-FLSPCNGQRNQMWK 124
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 451-573 1.26e-20

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467315 [Multi-domain]  Cd Length: 124  Bit Score: 87.74  E-value: 1.26e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 451 GYCLDYNppneNHVEGHQVLLYLCHGMGQNQFFEYTTRKEIRYNtrqpEACITVEDGKDTLVMDLCRetVPENQEFILQE 530
Cdd:cd23437  14 GLCLDTM----GHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVG----EQCLTASGSGGKVKLRKCN--LGETGKWEYDE 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 51315979 531 -DGTLVHKHSRKCVEATEkvlDNGFApYLRDCTN-SDNQRWFFKE 573
Cdd:cd23437  84 aTGQIRHKGTGKCLDLNE---GTNKL-ILQPCDSsSPSQKWEFNE 124
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 453-572 2.47e-20

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.


Pssm-ID: 467311 [Multi-domain]  Cd Length: 127  Bit Score: 86.98  E-value: 2.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 453 CLDYNPPNEnhveGHQVLLYLCHGMGQNQFFEYTTRKEIryntRQPEACITVEDGKDTLVMDLCRETvPENQEFIL-QED 531
Cdd:cd23433  17 CLDTMGRKA----GEKVGLSSCHGQGGNQVFSYTAKGEI----RSDDLCLDASRKGGPVKLEKCHGM-GGNQEWEYdKET 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 51315979 532 GTLVHKHSRKCVEATEKVLDNGfaPYLRDCTNSDNQRWFFK 572
Cdd:cd23433  88 KQIRHVNSGLCLTAPNEDDPNE--PVLRPCDGGPSQKWELE 126
beta-trefoil_Ricin_GALNT3 cd23468
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 438-571 3.67e-20

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) and similar proteins; GALNT3 (EC 2.4.1.41), also called polypeptide GalNAc transferase 3, GalNAc-T3, pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, 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. 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. GALNT3 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.


Pssm-ID: 467346  Cd Length: 129  Bit Score: 86.40  E-value: 3.67e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 438 PGFFGMLQNRGlRGYCLDYNppnENHVEGHQVLLYLCHGMGQNQFFEYTTRKEIRYNTrQPEACITVEDGkdTLVMDLC- 516
Cdd:cd23468   2 PLIFGAIKNVG-KELCLDVG---ENNHGGKPLIMYNCHGLGGNQYFEYSTHHEIRHNI-QKELCLHGSQG--SVQLKECt 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 517 ---RET-VPENQEFILQEDGTLVHKHSRKCVEAtekvldNGFAPYLRDCTNSDN-QRWFF 571
Cdd:cd23468  75 ykgRNTaVLPEEKWELQKDQLLYNPALNMCLSA------NGENPSLVPCNPSDPfQQWIF 128
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 131-249 1.38e-19

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 87.45  E-value: 1.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 131 PKTSVVIAFYNEAwSTLLRTVYSVLE-TSPDIlleEVILVDDYSD---REHLKERLAnelsQLPKVRLIRASRREGLVRA 206
Cdd:COG0463   2 PLVSVVIPTYNEE-EYLEEALESLLAqTYPDF---EIIVVDDGSTdgtAEILRELAA----KDPRIRVIRLERNRGKGAA 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 51315979 207 RLLGASAARGEVLTFLDCHCECHEGWLEPLLQRIHEKESAVVC 249
Cdd:COG0463  74 RNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY 116
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 135-249 1.56e-18

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.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 82.94  E-value: 1.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 135 VVIAFYNEAwSTLLRTVYSVLETSPDILleEVILVDDYSDREHLkERLANELSQLPKVRLIRASRREGLVRARLLGASAA 214
Cdd:cd00761   1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTL-EILEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 51315979 215 RGEVLTFLDCHCECHEGWLEPLLQRIHEKESAVVC 249
Cdd:cd00761  77 RGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 124-294 4.98e-18

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 84.79  E-value: 4.98e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 124 KYDYDNLPKTSVVIAFYNEAwSTLLRTVYSVLETSPDILLEEVILVDDYSDREhLKERLANELSQLPKVRLIRASRREGL 203
Cdd:COG1215  22 RRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGSTDE-TAEIARELAAEYPRVRVIERPENGGK 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 204 VRARLLGASAARGEVLTFLDCHCECHEGWLEPLLQRIHEKESAVVCPVIdVIDWNTFEylgnsgepQIGGFD-------- 275
Cdd:COG1215 100 AAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGANL-AFRREALE--------EVGGFDedtlgedl 170

                       170       180       190
                ....*....|....*....|....*....|....
gi 51315979 276 ----------WRLVF-----TWHVVPQRERQSMR 294
Cdd:COG1215 171 dlslrllragYRIVYvpdavVYEEAPETLRALFR 204
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 438-571 1.48e-17

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.


Pssm-ID: 467337 [Multi-domain]  Cd Length: 132  Bit Score: 79.29  E-value: 1.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 438 PGFFGMLQNRGlRGYCLDYnpPNENHVEGHQVLLYLCHGMGQ-NQFFEYTTRKEIRyntRQpEACITVEDG-KDTLVMDL 515
Cdd:cd23459   4 VLAYGQVRNPG-TNLCLDT--LQRDEDKGYNLGLYPCQGGLSsNQLFSLSKKGELR---RE-ESCADVQGTeESKVILIT 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 51315979 516 CRETVPENQEFILQEDGTLVHKHSRKCVEATEkvLDNGFAPYLRDCTNSDNQRWFF 571
Cdd:cd23459  77 CHGLEKFNQKWKHTKGGQIVHLASGKCLDAEG--LKSGDDVTLAKCDGSLSQKWTF 130
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 447-572 1.57e-16

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 75.63  E-value: 1.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979    447 RGLRGYCLDYNPPNENHVeghqvlLYLCHGMGQNQFFEYTTRKEIRynTRQPEACITVEDGKDTLVMDL-CrETVPENQE 525
Cdd:smart00458   3 SGNTGKCLDVNGNKNPVG------LFDCHGTGGNQLWKLTSDGAIR--IKDTDLCLTANGNTGSTVTLYsC-DGTNDNQY 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 51315979    526 FILQEDGTLVHKHSRKCVEATEKvlDNGFAPYLRDCTNSDNQRWFFK 572
Cdd:smart00458  74 WEVNKDGTIRNPDSGKCLDVKDG--NTGTKVILWTCSGNPNQKWIFE 118
beta-trefoil_Ricin_GALNT6 cd23470
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 438-571 2.67e-16

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.


Pssm-ID: 467348  Cd Length: 128  Bit Score: 75.68  E-value: 2.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 438 PGFFGMLQNRGLRGyCLDYNppnENHVEGHQVLLYLCHGMGQNQFFEYTTRKEIRYNTRQpEACITVEDGKdtLVMDLCR 517
Cdd:cd23470   1 PTFYGAIKNEGTNQ-CLDVG---ENNRGGKPLIMYSCHGMGGNQYFEYTTHKELRHNIAK-QLCLRVSKGP--VQLGECH 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 518 -----ETVPENQEFILQEDGTLVHKHSRKCVEATEKvldngfAPYLRDCTNSD-NQRWFF 571
Cdd:cd23470  74 ykgknSQVPPDEEWELTQDHLIRNSGSNMCLTARGK------HPAMAPCNPADpHQLWSF 127
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
131-278 2.00e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 75.03  E-value: 2.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 131 PKTSVVIAFYNEaWSTLLRTVYSVLETSPDILleEVILVDDYSD---REHLKERlanelsQLPKVRLIRASRREGLVRAR 207
Cdd:COG1216   3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGSTdgtAELLAAL------AFPRVRVIRNPENLGFAAAR 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51315979 208 LLGASAARGEVLTFLDCHCECHEGWLEPLLQRihekeSAVVCPViDVIDwntfeylgnsgepQIGGFDWRL 278
Cdd:COG1216  74 NLGLRAAGGDYLLFLDDDTVVEPDWLERLLAA-----ACLLIRR-EVFE-------------EVGGFDERF 125
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 442-571 1.96e-14

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.


Pssm-ID: 467297 [Multi-domain]  Cd Length: 130  Bit Score: 70.07  E-value: 1.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 442 GMLQNRglrgyCLDYnpPNENHVEGHQVLLYLCHGmGQNQFFEYTTRKEIRYNTRQpeaCITVEDGK----DTLVMDLCR 517
Cdd:cd23418  10 GYGSGR-----CLDV--PGGSTTNGTRLILWDCHG-GANQQFTFTSAGELRVGGDK---CLDAAGGGttngTPVVIWPCN 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 51315979 518 ETvpENQEFILQEDGTLVHKHSRKCVEATEKVLDNGFAPYLRDCTNSDNQRWFF 571
Cdd:cd23418  79 GG--ANQKWRFNSDGTIRNVNSGLCLDVAGGGTANGTRLILWSCNGGSNQRWRR 130
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 440-572 1.43e-13

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.


Pssm-ID: 467338 [Multi-domain]  Cd Length: 121  Bit Score: 67.47  E-value: 1.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 440 FFGMLQNRGlRGYCLDynpPNENHVEGHQVLLYLCHGMGQNQFFEYTTRKEIryntRQPEACITVEDGKDtLVMDLCrET 519
Cdd:cd23460   1 GLGQIKHTE-SGLCLD---WAGESNGDKTVALKPCHGGGGNQFWMYTGDGQI----RQDHLCLTADEGNK-VTLREC-AD 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 51315979 520 VPENQEFILQE-DGTLVHKHSRKCVEatekVLDNGFAPYLRDCTNSDN-QRWFFK 572
Cdd:cd23460  71 QLPSQEWSYDEkTGTIRHRSTGLCLT----LDANNDVVILKECDSNSLwQKWIFQ 121
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 450-529 1.04e-12

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.


Pssm-ID: 467340 [Multi-domain]  Cd Length: 126  Bit Score: 65.08  E-value: 1.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 450 RGYCLDYNppnenhVEGHQVLLYLCHGMGQNQFFEYT-TRKEIRYNTRQpeACITVEDGKDTLVMDLCRETVPeNQEFIL 528
Cdd:cd23462  55 DDLCLDYA------GGSGDVTLYPCHGMKGNQFWIYDeETKQIVHGTSK--KCLELSDDSSKLVMEPCNGSSP-RQQWEF 125


                .
gi 51315979 529 Q 529
Cdd:cd23462 126 E 126
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 453-572 1.57e-12

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.


Pssm-ID: 467344  Cd Length: 127  Bit Score: 64.68  E-value: 1.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 453 CLDynppNENHVEGHQVLLYLCHGMGQNQFFEYTTRKEIRYNtrqpEACITVEDGKDTLVMDLCREtVPENQefILQEDG 532
Cdd:cd23466  17 CLD----NMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTD----DLCLDVSKLNGPVMMLKCHH-LKGNQ--LWEYDP 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 51315979 533 ---TLVHKHSRKCVE-ATEkvlDNGFAPYLRDCTNSDNQRWFFK 572
Cdd:cd23466  86 vklTLLHVNSNQCLDkATE---EDSQVPSIRDCNGSRSQQWLLR 126
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 453-572 2.52e-11

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.


Pssm-ID: 467345  Cd Length: 127  Bit Score: 61.20  E-value: 2.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 453 CLDynppNENHVEGHQVLLYLCHGMGQNQFFEYTTRKEIRYNtrqpEACITVEDGKDTLVMDLCREtVPENQEFILQ-ED 531
Cdd:cd23467  17 CLD----NMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTD----DLCLDVSRLNGPVVMLKCHH-MRGNQLWEYDaER 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 51315979 532 GTLVHKHSRKCVEATEKvlDNGFAPYLRDCTNSDNQRWFFK 572
Cdd:cd23467  88 LTLRHVNSNQCLDEPSE--EDKMVPTMKDCSGSRSQQWLLR 126
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 441-571 3.59e-11

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.


Pssm-ID: 467312 [Multi-domain]  Cd Length: 121  Bit Score: 60.41  E-value: 3.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 441 FGMLQNRGLrgyCLDynppNENHVEGHQVLLYLCHGMGQNQFFEYTTRKEIryntRQPEACITVEDGK-DTLV-MDLCRE 518
Cdd:cd23434   2 FGSLKQGNL---CLD----TLGHKAGGTVGLYPCHGTGGNQEWSFTKDGQI----KHDDLCLTVVDRApGSLVtLQPCRE 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 51315979 519 TvPENQEFILQE-DGTLVHKHSRKCVEATEkVLDNGfaPYLRDCTN-SDNQRWFF 571
Cdd:cd23434  71 D-DSNQKWEQIEnNSKLRHVGSNLCLDSRN-AKSGG--LTVETCDPsSGSQQWKF 121
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 441-569 2.21e-10

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.


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 58.54  E-value: 2.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 441 FGMLQNRGlRGYCLDynPPNENHVEGHQVLLYLCHGmGQNQFFEYTTRKEIRYN--TRQPEACITVEDGKDT----LVMD 514
Cdd:cd00161   2 TYRIVNAA-SGKCLD--VAGGSTANGAPVQQWTCNG-GANQQWTLTPVGDGYYTirNVASGKCLDVAGGSTAnganVQQW 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 51315979 515 LCRETvpENQEFILQEDG----TLVHKHSRKCVEATEKVLDNGFAPYLRDCTNSDNQRW 569
Cdd:cd00161  78 TCNGG--DNQQWRLEPVGdgyyRIVNKHSGKCLDVSGGSTANGANVQQWTCNGGANQQW 134
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 135-332 2.32e-09

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.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 57.20  E-value: 2.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 135 VVIAFYNEAwSTLLRTVYSVLETSPDILLEEVILVDDYS-DR--EHLKERLAnelsQLPKVRLIRASRREGLVRARLLGA 211
Cdd:cd04179   1 VVIPAYNEE-ENIPELVERLLAVLEEGYDYEIIVVDDGStDGtaEIARELAA----RVPRVRVIRLSRNFGKGAAVRAGF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 212 SAARGEVLTFLDCHCECHEGWLEPLLQRIHEKESAVVCPV----IDVIDWNTFEYLGNsgepqiGGFDW--RLVFTWHVv 285
Cdd:cd04179  76 KAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSrfvrGGGAGMPLLRRLGS------RLFNFliRLLLGVRI- 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 51315979 286 pqrerqsmrspidvirsPTMAGGLFAVSKRYFDYLGSYDT------GMEVWGG 332
Cdd:cd04179 149 -----------------SDTQSGFRLFRREVLEALLSLLEsngfefGLELLVG 184
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 131-224 4.54e-08

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 53.75  E-value: 4.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 131 PKTSVVIAFYNEAWSTLLRTVYSVLE-TSPDIlleEVILVDDYSDREHLKERLANELSQLPKVRLIRASRREGLVRARLL 209
Cdd:cd04184   1 PLISIVMPVYNTPEKYLREAIESVRAqTYPNW---ELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNS 77

                        90
                ....*....|....*
gi 51315979 210 GASAARGEVLTFLDC 224
Cdd:cd04184  78 ALELATGEFVALLDH 92
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 451-569 4.81e-08

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts 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.


Pssm-ID: 467336 [Multi-domain]  Cd Length: 135  Bit Score: 51.94  E-value: 4.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 451 GYCLDYNPPNENhvEGHQVLLYLCHGmGQNQFFEY--TTRKEIRYNTRQPEACITV-----EDGKDTLVMDlCRETVpeN 523
Cdd:cd23458  11 GKCIDVAGGSTA--NGANIQQWDCGS-GSNQQWTLveIDNGYYRIKASHSGKCLDVaggstANGANIQQWD-CVGGA--N 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 51315979 524 QEFILQEDG----TLVHKHSRKCVEATEKVLDNGFAPYLRDCTNSDNQRW 569
Cdd:cd23458  85 QQWKLQDLGngyfELKARHSGKCLDVAGGSTANGASIQQWTCNGNDNQRF 134
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 135-358 6.55e-08

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.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 52.56  E-value: 6.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 135 VVIAFYNeAWSTLLRTVYSVLETSPDILleEVILVDDYS---DREHLKErlanelsQLPKVRLIRASRREGLVRARLLGA 211
Cdd:cd04186   1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVDNAStdgSVELLRE-------LFPEVRLIRNGENLGFGAGNNQGI 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 212 SAARGEVLTFLDCHCECHEGWLEPLLQRIHE-KESAVVCPVID----VIDWNTFEylgnsgepQIGGFDwrlvftwhvvp 286
Cdd:cd04186  71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQdPDVGIVGPKVSgaflLVRREVFE--------EVGGFD----------- 131

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51315979 287 qrerqsmrspidvirsptmagglfavsKRYFDYlgsydtgmevwgGENLEFSFRIWQCGGTLETHPCSHVGH 358
Cdd:cd04186 132 ---------------------------EDFFLY------------YEDVDLCLRARLAGYRVLYVPQAVIYH 164
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 451-569 1.97e-07

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal 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 bears a potential sugar binding site.


Pssm-ID: 467329 [Multi-domain]  Cd Length: 125  Bit Score: 50.02  E-value: 1.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 451 GYCLDyNPPNENhVEGHQVLLYLCHGMGqNQFFEYTTRKEIRYNTRqpeaCITV-----EDGKDTLVMDlCRETVpeNQE 525
Cdd:cd23451  11 GKCLD-VPGSST-ADGNPVQIYTCNGTA-AQKWTLGTDGTLRVLGK----CLDVsgggtANGTLVQLWD-CNGTG--AQK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 51315979 526 FILQEDGTLVHKHSRKCVEATEKVLDNGFAPYLRDCTNSDNQRW 569
Cdd:cd23451  81 WVPRADGTLYNPQSGKCLDAPGGSTTDGTQLQLYTCNGTAAQQW 124
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 135-276 2.42e-07

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.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 51.91  E-value: 2.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 135 VVIAFYNEAwSTLLRTVYSVLETS-PDILLEeVILVDDYS-DREH-LKERLANElsQLPKVRLIRASRREGLVRARLL-- 209
Cdd:cd04192   1 VVIAARNEA-ENLPRLLQSLSALDyPKEKFE-VILVDDHStDGTVqILEFAAAK--PNFQLKILNNSRVSISGKKNALtt 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51315979 210 GASAARGEVLTFLDCHCECHEGWLEPLLQRIHEKESAVVC-PVIDVIDWNTFEYLGNsgepqiggFDW 276
Cdd:cd04192  77 AIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAgPVIYFKGKSLLAKFQR--------LDW 136
beta-trefoil_Ricin_GALNT8-like cd23438
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 440-572 4.82e-07

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8)-like subfamily; The GALNT8-like subfamily includes GALNT8, GALNT9, GALNT17 and GALNT18. 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. GALNT9 does not glycosylate apomucin or SDC3. 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 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.


Pssm-ID: 467316  Cd Length: 134  Bit Score: 48.97  E-value: 4.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 440 FFGMLQNRGLRGYCLDYNPpnenhVEGHQVLLYLCHGMGQnQFFEYTTRKEIRY----NTRQPEACITVEDGKDTLVMDL 515
Cdd:cd23438   4 AYGEMRNSLVTDLCLDQGP-----KENHTAILYPCHGWSP-QLVRYTKDGQLYLgqlgSTASPDTRCLVDDGKSDKPQLL 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 51315979 516 CRETVPENQE--FILQEDGTLVHKHSRKCVEATEKVLDNGFAPYLRDCTnsdNQRWFFK 572
Cdd:cd23438  78 DCSKVKNRLQkyWDFSQGGAIQNRATGRCLEVEEDKLNFGHRLVLQTCS---GQKWNIK 133
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 134-396 6.04e-07

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 51.12  E-value: 6.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979   134 SVVIAFYN-EAWSTLLRTVysVLETSPDILLEEVILVDDYSdrehlKERLANELSQLPKVRLIRASRRE-----GLVRAR 207
Cdd:pfam10111   1 SVVIPVYNgEKTHWIQERI--LNQTFQYDPEFELIIINDGS-----TDKTLEEVSSIKDHNLQVYYPNApdttySLAASR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979   208 LLGASAARGEVLTFLDCHCECHEGWLEPLLQRIHEK------ESAVVCPVIDVIDWNTfEYLGNSGEpqiggfdwrlvFT 281
Cdd:pfam10111  74 NRGTSHAIGEYISFIDGDCLWSPDKFEKQLKIATSLalqeniQAAVVLPVTDLNDESS-NFLRRGGD-----------LT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979   282 WHVVPQRERQSMRSPIDVIRSPTmaGGLFAVSKRYFDYLGSYDTGMEVWGGENLEFSFRIWQCGGTLETHPCS-----HV 356
Cdd:pfam10111 142 ASGDVLRDLLVFYSPLAIFFAPN--SSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRLAARYPFVAVMPPQllyrlSA 219

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 51315979   357 GHVFPKQAPYSRSKALAnsvRAAEVWMDEFKELYYHRNPQ 396
Cdd:pfam10111 220 KSMSPYSGFRRFLGDLA---RQAAACGKVLKHAYHDAPPS 256
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 135-224 8.59e-07

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic 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. 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. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 49.40  E-value: 8.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 135 VVIAFYNEAWS--TLLRTVYSVLETSPDILleEVILVDDYS-DREHlkERLANELSQLPKVRLIRASRREGLVRARLLGA 211
Cdd:cd04187   1 IVVPVYNEEENlpELYERLKAVLESLGYDY--EIIFVDDGStDRTL--EILRELAARDPRVKVIRLSRNFGQQAALLAGL 76

                        90
                ....*....|...
gi 51315979 212 SAARGEVLTFLDC 224
Cdd:cd04187  77 DHARGDAVITMDA 89
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 134-352 1.14e-06

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.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 49.92  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 134 SVVIAFYNEAwSTLLRTVYSVLETSPDILLEEVILVDDYSD---REHLKERLANElsqlPKVRLI-RASRREGlvRARLL 209
Cdd:cd02525   3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTdgtREIVQEYAAKD----PRIRLIdNPKRIQS--AGLNI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 210 GASAARGEVLTFLDCHCECHEGWLEPLLQRIHEKESAVVCPVIDVIDWNTFE---------YLGNSGEPQiggfdwrlvf 280
Cdd:cd02525  76 GIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQkaiavaqssPLGSGGSAY---------- 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51315979 281 twhvvpqreRQSMRSPIDVirsPTMAGGLFavSKRYFDYLGSYDTGMEVwgGENLEFSFRIWQCGGTLETHP 352
Cdd:cd02525 146 ---------RGGAVKIGYV---DTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSP 201
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
 448-569 1.37e-06

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.


Pssm-ID: 467330 [Multi-domain]  Cd Length: 125  Bit Score: 47.51  E-value: 1.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 448 GLRGYCLDynPPNENHVEGHQVLLYLCHGMGQnQFFEYTTRKEIRYNTRqpeaCITV-----EDGKDTLVMDlCRETVpe 522
Cdd:cd23452   8 GLANKCID--VPNSSTTDGAPLQLWDCNGTNA-QKWTFASDGTLRALGK----CLDVawggtDNGTAVQLWT-CSGNP-- 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 51315979 523 NQEFILQEDGTLVHKHSRKCVEATEKVLDNGFAPYLRDCTNSDNQRW 569
Cdd:cd23452  78 AQQFVLSGAGDLVNPQANKCVDVSGGNSGNGTRLQLWECSGNANQKW 124
beta-trefoil_Ricin_GALNT18 cd23475
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 441-569 2.03e-06

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 18 (GALNT18) and similar proteins; GALNT18 (EC 2.4.1.41), also called polypeptide GalNAc transferase 18, GalNAc-T18, polypeptide GalNAc transferase-like protein 4, GalNAc-T-like protein 4, pp-GaNTase-like protein 4, polypeptide N-acetylgalactosaminyltransferase-like protein 4, protein-UDP acetylgalactosaminyltransferase-like protein 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4, 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. GALNT18 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.


Pssm-ID: 467353  Cd Length: 142  Bit Score: 47.61  E-value: 2.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 441 FGMLQNRGLRGYCLDYNPPNENhveghQVLLYLCHGMG-QNQFfeYTTRKEIRYNTRQPeaciTVEDGKDTLVMDL---- 515
Cdd:cd23475  10 YGVLQNSLKTDLCLDQGPDTDN-----IPIMYICHGMTpQNVY--YTSNQQLHVGILSP----TIDDDDNRCLVDVnsrp 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51315979 516 ----CRETVPENQEFILQ--EDGTLVHKHSRKCVEATEKV-LDNGFAPYLRDCTnsdNQRW 569
Cdd:cd23475  79 rlieCSYAKAKRMKLYWLftQGGSIQNKKSKRCLELQENAdNEFGYQLVLQKCS---GQRW 136
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 135-249 7.63e-06

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


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 47.18  E-value: 7.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 135 VVIAFYNEAwSTLLRTVYSVLETSPDILLE--EVILVDDYSDREHLK--ERLANELSQLpkVRLIRASRREGLVRARLLG 210
Cdd:cd04188   1 VVIPAYNEE-KRLPPTLEEAVEYLEERPSFsyEIIVVDDGSKDGTAEvaRKLARKNPAL--IRVLTLPKNRGKGGAVRAG 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 51315979 211 ASAARGEVLTFLD-------CHcechegwLEPLLQRIHEKESAVVC 249
Cdd:cd04188  78 MLAARGDYILFADadlatpfEE-------LEKLEEALKTSGYDIAI 116
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 453-521 1.20e-05

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.


Pssm-ID: 467317 [Multi-domain]  Cd Length: 126  Bit Score: 45.03  E-value: 1.20e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51315979 453 CLDYNppneNHVEGHQVLLYLCHGMGQNQFFEYttrkeiRYNTRQ-----PEACITVEDGKDTLVMDLCRETVP 521
Cdd:cd23439  57 CFDVS----SHTPGAPVILYACHGMKGNQLWKY------RPNTKQlyhpvSGLCLDADPGSGKVFMNHCDESSD 120
beta-trefoil_Ricin_GALNT17 cd23474
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 441-572 1.23e-05

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.


Pssm-ID: 467352  Cd Length: 142  Bit Score: 45.27  E-value: 1.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 441 FGMLQNRGLRGYCLDYNPPnenhvEGHQVLLYLCHGMGQnQFFEYTTRKEIRY-----NTRQPEACITVEDGKDTL--VM 513
Cdd:cd23474  10 YGELRNNKAKDVCLDQGPP-----ENHTAILYPCHGWGP-QLARYTKEGYLHLgalgtTTLLPDTRCLVDNKKSRFpqLL 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51315979 514 DlC---RETVPENQEFIlqEDGTLVHKHSRKCVEaTEKVLDNGFAPYLRDCTnsdNQRWFFK 572
Cdd:cd23474  84 D-CdkvKSILHKRWNFI--QNGAIMNLGTGRCLE-VENRGNFGIDLILRSCT---GQRWTIK 138
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 135-327 1.76e-05

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


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 45.68  E-value: 1.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 135 VVIAFYNEAwSTLLRTVYSVLE-TSPDIlleEVILVDDYSDREHLKERLANELSQLPKVRLIRASRREGLVRARLLGASA 213
Cdd:cd06423   1 IIVPAYNEE-AVIERTIESLLAlDYPKL---EVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRH 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 214 ARGEVLTFLDCHCECHEGWLEPLLQRIHEKESAV-VCPVIDVIDWNTfeylgnsgepqigGFDWRLVFTWHVVPQRERQS 292
Cdd:cd06423  77 AKGDIVVVLDADTILEPDALKRLVVPFFADPKVGaVQGRVRVRNGSE-------------NLLTRLQAIEYLSIFRLGRR 143

                       170       180       190
                ....*....|....*....|....*....|....*
gi 51315979 293 MRSPIDVIrsPTMAGGLFAVSKRYFDYLGSYDTGM 327
Cdd:cd06423 144 AQSALGGV--LVLSGAFGAFRREALREVGGWDEDT 176
beta-trefoil_Ricin_GALNT9 cd23473
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 441-572 4.21e-05

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.


Pssm-ID: 467351  Cd Length: 145  Bit Score: 43.80  E-value: 4.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 441 FGMLQNRGLRGYCLDynppnENHVEGHQVLLYLCHGMgQNQFFEYTTRKEIRYN-----TRQPEACITVEDGKD-TLVMD 514
Cdd:cd23473  10 YGEVRNSKASGYCLD-----QGSEEDDKAILYPCHGM-SSQLVRYSTEGLLQLGplgstAFLPDTKCLVDDGRGrTPTLK 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51315979 515 LCRETVPENQEFI-LQEDGTLVHKHSRKCVEaTEKVLDNGFAPYL--RDCTnsdNQRWFFK 572
Cdd:cd23473  84 KCEDVARPAQRLWdFTQNGPIISRDTGRCLE-VEMSKDANFGLRLvvQRCS---GQKWMIR 140
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 126-223 5.78e-05

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 44.88  E-value: 5.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 126 DYDNLPKTSVVIAFYNEAwSTLLRTVYSVLETS-PDILLeEVILVDDYSD-------REHLKERlanelsqlpkVRLIRA 197
Cdd:cd06439  24 DPAYLPTVTIIIPAYNEE-AVIEAKLENLLALDyPRDRL-EIIVVSDGSTdgtaeiaREYADKG----------VKLLRF 91

                        90       100
                ....*....|....*....|....*.
gi 51315979 198 SRREGLVRARLLGASAARGEVLTFLD 223
Cdd:cd06439  92 PERRGKAAALNRALALATGEIVVFTD 117
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 135-248 8.41e-05

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; 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. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 44.06  E-value: 8.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 135 VVIAFYNEAwSTLLRTVYSVLETSPDILLEeVILVDDYS-DRehlKERLANELS-QLPKVRLIRASRREGLVRARLLGAS 212
Cdd:cd06442   1 IIIPTYNER-ENIPELIERLDAALKGIDYE-IIVVDDNSpDG---TAEIVRELAkEYPRVRLIVRPGKRGLGSAYIEGFK 75

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 51315979 213 AARGEVLTFLDC---HcecHEGWLEPLLQRIHEKESAVV 248
Cdd:cd06442  76 AARGDVIVVMDAdlsH---PPEYIPELLEAQLEGGADLV 111
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 532-571 2.69e-04

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.


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 41.20  E-value: 2.69e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 51315979 532 GTLVHKHSRKCVEATEKVLDNGFAPYLRDCTNSDNQRWFF 571
Cdd:cd00161   3 YRIVNAASGKCLDVAGGSTANGAPVQQWTCNGGANQQWTL 42
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 134-222 4.51e-04

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily 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.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 41.79  E-value: 4.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 134 SVVIAFYNEAwSTLLRTVYSVLETSPDILleEVILVDDYSDREHLkerlanELSQLPKVRLIRASRreGlvRARLL--GA 211
Cdd:cd02522   2 SIIIPTLNEA-ENLPRLLASLRRLNPLPL--EIIVVDGGSTDGTV------AIARSAGVVVISSPK--G--RARQMnaGA 68

                        90
                ....*....|.
gi 51315979 212 SAARGEVLTFL 222
Cdd:cd02522  69 AAARGDWLLFL 79
beta-trefoil_Ricin_SGSL_rpt2 cd23489
second ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes ...
 499-571 4.53e-04

second ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes anguina) seed lectin (SGSL) and similar proteins; Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. SGSL is a non-toxic three-chain type II RIPs consisting of Aalpha, Abeta and B chains with Abeta and B being disulfide-linked. The Aalpha and Abeta chains constitute the rRNA glycosidase domain and the B chain contains two ricin B-type carbohydrate-binding lectin domains. SGSL may have no glycosidase activity due to small changes in both the nucleotide binding and carbohydrate binding capabilities. It binds galactose and derivatives with a preference for the beta-anomeric forms. It also binds prophyrins. SGSL has hemagglutinating activity towards rabbit and human erythrocytes. The ricin B-type lectin domain shows 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 model corresponds to the second ricin B-type lectin domain.


Pssm-ID: 467367  Cd Length: 128  Bit Score: 40.45  E-value: 4.53e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51315979 499 EACITVEDGKDTLVMDLCretVPENQE--FILQEDGTLVHKHSRK-CVEATEKVLDNGFAPYLRDCTNSDNQRWFF 571
Cdd:cd23489  11 DMCLEATDGNTNMWLEEC---VPNQREqsWALYSDGTIRVDDNRElCVTASSSTYDNWKVITILNCDGSNNQRWVF 83
beta-trefoil_Ricin_GALNT8 cd23472
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 428-569 5.61e-04

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.


Pssm-ID: 467350  Cd Length: 146  Bit Score: 40.57  E-value: 5.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 428 YPELhVPEDRPGFFGMLQNRGLRGYCLDYNPpnenhVEGHQVLLYLCHGMGQnQFFEYTTRKEI--------RYNTrqpE 499
Cdd:cd23472   1 YPVL-MPIQTIVGYGTMKNSLNENICIDQGP-----VPGNTPIMYGCHGYSP-QFVYYHLTGELyvgglkadIYAS---D 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51315979 500 ACITVEDGKDTLVMDLCRETVPE--NQEFILQEDGTLVHKHSRKCVEATEKVLDNGFAPYLRDCTnsdNQRW 569
Cdd:cd23472  71 RCLTDPGEGWKPELVSCQDATLKglNMYWDFKQGTAIINRKTKRCLEISLDKTPSYYTLILQTCT---GQKW 139
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 131-223 6.34e-04

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 42.34  E-value: 6.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979  131 PKTSVVIAFYNeAWSTLLRTVYSVLETSPDILleEVILVDDYSDrEHLKERLANELSQLPKVRLIrASRREGLVRARLLG 210
Cdd:PRK10073   6 PKLSIIIPLYN-AGKDFRAFMESLIAQTWTAL--EIIIVNDGST-DNSVEIAKHYAENYPHVRLL-HQANAGVSVARNTG 80

                         90
                 ....*....|...
gi 51315979  211 ASAARGEVLTFLD 223
Cdd:PRK10073  81 LAVATGKYVAFPD 93
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 442-571 8.22e-04

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 11 (GALNT11) and similar proteins; GALNT11 (EC 2.4.1.41), also called polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes its activation, modulating the balance between motile and immotile (sensory) cilia at the left-right organizer (LRO). GALNT11 displays the same enzyme activity toward MUC1, MUC4, and EA2 as GALNT1. It is not involved in glycosylation of erythropoietin (EPO). GALNT11 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467318 [Multi-domain]  Cd Length: 127  Bit Score: 39.67  E-value: 8.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 442 GMLQNRGLrGYCLDynPPNENHVEGHQVLLYLCHGMGQNQFFEYTTRKEIRYNTRqpeACI-TVEDGKDTLVMDLCRETV 520
Cdd:cd23440   6 GQLKHAGS-GLCLV--AEDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANL---LCLdSSETSSDFPRLMKCHGSG 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 51315979 521 pENQEFILQEDGTLVHKHSRKCVEATekvlDNGFAPY--LRDCTNSDNQRWFF 571
Cdd:cd23440  80 -GSQQWRFKKDNRLYNPASGQCLAAS----KNGTSGYvtMDICSDSPSQKWVF 127
beta-trefoil_Ricin_RIPs_II_rpt1 cd23443
first ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ...
 448-539 9.92e-04

first ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating proteins (RIPs); Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. They consist of a catalytic A-chain which has rRNA N-glycosidase activity and a lectin B-chain containing two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The lectin chain facilitates the internalization of the catalytic chain on binding to the cell surface. The two chains are connected by a disulfide bridge. This model corresponds to the first ricin B-type lectin domain. Members of this subfamily includes Ricinus communis ricin, bitter gourd (Momordica charantia) seed lectin (BGSL), snake gourd (Trichosanthes anguina) seed lectin (SGSL), Sambucus ebulus ebulin I, Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf, Abrus precatorius abrin (ABR) and agglutinin-I (AAG), and Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs).


Pssm-ID: 467321 [Multi-domain]  Cd Length: 123  Bit Score: 39.20  E-value: 9.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 448 GLRGYCLDYNPPNENhvEGHQVLLYLCHGMGQNQFFEYTTRKEIRYNTRqpeaCITVED---GKDTLVMDlCRETVPENQ 524
Cdd:cd23443   7 GRDGLCVDVKDGYYS--DGNPVILWPCKSQDANQLWTFKRDGTIRSNGK----CLTTNGyspGSYVVIYD-CSTAVAEAT 79

                        90
                ....*....|....*
gi 51315979 525 EFILQEDGTLVHKHS 539
Cdd:cd23443  80 KWEVSDDGTIINPAS 94
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 501-571 1.21e-03

ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its 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 may harbor a sugar-binding pocket.


Pssm-ID: 467334 [Multi-domain]  Cd Length: 122  Bit Score: 38.88  E-value: 1.21e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51315979 501 CITVEDGKD---TLVMDLCRETvpENQEFILQEDGTLVHK-HSRKCVEATEKVLDNGFApYLRDCTNSDNQRWFF 571
Cdd:cd23456  13 CLDVSGGATngaNVVVYDCNNS--NSQKWYYDATGRLHSKaNPGKCLDAGGENSNGANV-VLWACNDSANQRWDF 84
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
523-573 1.41e-03

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 38.13  E-value: 1.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 51315979   523 NQEFILQEDG-----TLVHKHSRKCVEATEKVLDNGFAPYLRDCTNSDNQRWFFKE 573
Cdd:pfam14200   2 NQQWRFGGTVgdgyyTIVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVD 57
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 442-571 2.63e-03

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.


Pssm-ID: 467339  Cd Length: 128  Bit Score: 38.15  E-value: 2.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315979 442 GMLQNRGLRGYCLDYNppneNHVEGHQVLLYLCHG----MGQNQFFEYTTRKEIRYNTRqpEACITVEDgkDTLVMDLCR 517
Cdd:cd23461   4 GVIQSVAFPNLCLDIL----GRSHGGPPVLAKCSSnksmPGTFQNFSLTFHRQIKHGTS--DDCLEVRG--NNVRLSRCH 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 51315979 518 EtVPENQEFILQ-EDGTLVH-KHSRKCVEATekvlDNGFAPYLRDCtNSDN--QRWFF 571
Cdd:cd23461  76 Y-QGGNQYWKYDyETHQLINgGQNNKCLEAD----VESLKITLSIC-DSDNveQKWKW 127
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 301-353 3.65e-03

N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 36.44  E-value: 3.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 51315979   301 RSPTMAGGLFAVSKRYFDYLGSYDTGMEVWGGENLEFSFRIWQCGGTLETHPC 353
Cdd:pfam02709  15 PYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG 67
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 496-569 4.64e-03

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.


Pssm-ID: 467319 [Multi-domain]  Cd Length: 122  Bit Score: 37.38  E-value: 4.64e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51315979 496 RQPEACI----TVEDGKDTLVMDLCRETVPEnQEFILQEDGTLvhKHSRKCVEATEKvlDNGFAPYLRDCTNSDNQRW 569
Cdd:cd23441   9 KQGNLCLdsdeQLFQGPALLILAPCSNSSDS-QEWSFTKDGQL--QTQGLCLTVDSS--SKDLPVVLETCSDDPKQKW 81
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 522-571 5.28e-03

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts 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.


Pssm-ID: 467336 [Multi-domain]  Cd Length: 135  Bit Score: 37.30  E-value: 5.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 51315979 522 ENQEFILQEDGT----LVHKHSRKCVEATEKVLDNGFAPYLRDCTNSDNQRWFF 571
Cdd:cd23458  36 SNQQWTLVEIDNgyyrIKASHSGKCLDVAGGSTANGANIQQWDCVGGANQQWKL 89
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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