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Conserved domains on  [gi|767981136|ref|XP_011535308|]
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polypeptide N-acetylgalactosaminyltransferase 16 isoform X1 [Homo sapiens]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase( domain architecture ID 11551826)

polypeptide N-acetylgalactosaminyltransferase 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

CAZY:  GT2
EC:  2.4.1.41
Gene Ontology:  GO:0004653|GO:0030246|GO:0046872
PubMed:  12634319|12691742|9445404|8844840
SCOP:  3000077|3000678

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 ...
 126-420 0e+00

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: 512.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 126 SVIITFHNEARSTLLRTVKSVLNRTPANLIQEIILVDDFSSDPEDCLLL-----TRIPKVKCLRNDRREGLIRSRVRGAD 200
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 201 VAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKmTR 280
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 281 TDPTRPIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFR-KRHPYNFPEGN 359
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767981136 360 AlTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMNCKSFRWYLENVY 420
Cdd:cd02510  240 G-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT16 cd23479
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 426-557 9.33e-64

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 16 (GALNT16) and similar proteins; GALNT16 (EC 2.4.1.41), also called polypeptide GalNAc transferase 16, GalNAc-T16, polypeptide GalNAc transferase-like protein 1, GalNAc-T-like protein 1, pp-GaNTase-like protein 1, polypeptide N-acetylgalactosaminyltransferase-like protein 1, protein-UDP acetylgalactosaminyltransferase-like protein 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. GALNT16 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: 467357  Cd Length: 129  Bit Score: 204.66  E-value: 9.33e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 426 PVKEALPGIIKQGVNCLESQGQNTAGDFLLGMGICRGSAKNPQPAQAWLFSDHLIQQQGKCLAATSTlmsSPGSPVILQM 505
Cdd:cd23479    1 PEKEAIPGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASQEWVLSDPLIRQQDKCLAITSF---SPGSKVILEL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767981136 506 CNPREGKQKWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLLPH 557
Cdd:cd23479   78 CNQKDGRQKWKLKGSFIQHQVSGLCLDSQSGRVVINQCQADLASQQWELLQV 129
 
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 ...
 126-420 0e+00

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: 512.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 126 SVIITFHNEARSTLLRTVKSVLNRTPANLIQEIILVDDFSSDPEDCLLL-----TRIPKVKCLRNDRREGLIRSRVRGAD 200
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 201 VAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKmTR 280
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 281 TDPTRPIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFR-KRHPYNFPEGN 359
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767981136 360 AlTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMNCKSFRWYLENVY 420
Cdd:cd02510  240 G-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT16 cd23479
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 426-557 9.33e-64

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 16 (GALNT16) and similar proteins; GALNT16 (EC 2.4.1.41), also called polypeptide GalNAc transferase 16, GalNAc-T16, polypeptide GalNAc transferase-like protein 1, GalNAc-T-like protein 1, pp-GaNTase-like protein 1, polypeptide N-acetylgalactosaminyltransferase-like protein 1, protein-UDP acetylgalactosaminyltransferase-like protein 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. GALNT16 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: 467357  Cd Length: 129  Bit Score: 204.66  E-value: 9.33e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 426 PVKEALPGIIKQGVNCLESQGQNTAGDFLLGMGICRGSAKNPQPAQAWLFSDHLIQQQGKCLAATSTlmsSPGSPVILQM 505
Cdd:cd23479    1 PEKEAIPGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASQEWVLSDPLIRQQDKCLAITSF---SPGSKVILEL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767981136 506 CNPREGKQKWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLLPH 557
Cdd:cd23479   78 CNQKDGRQKWKLKGSFIQHQVSGLCLDSQSGRVVINQCQADLASQQWELLQV 129
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 126-306 4.86e-28

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: 110.18  E-value: 4.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136  126 SVIITFHNEArSTLLRTVKSVLNRTPANLiqEIILVDDFSSD--PEDCL-LLTRIPKVKCLRNDRREGLIRSRVRGADVA 202
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGSTDgtVEIAEeYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136  203 AATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPIIDVISLDNFAYlaasadlrggfdWSLHFKWEQIPleqKMTRTD 282
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY------------RRASRITLSRL---PFFLGL 142

                         170       180
                  ....*....|....*....|....
gi 767981136  283 PTRPIRTPVIAGGIFVIDKSWFNH 306
Cdd:pfam00535 143 RLLGLNLPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
441-543 1.92e-17

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 78.73  E-value: 1.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136  441 CLESQGQNTAGdFLLGMGICRGSAKNpqpaQAWLFS-DHLIQQ--QGKCLAATSTlmsSPGSPVILQMCNPREGKQKWR- 516
Cdd:pfam00652  13 CLDVPGGSSAG-GPVGLYPCHGSNGN----QLWTLTgDGTIRSvaSDLCLDVGST---ADGAKVVLWPCHPGNGNQRWRy 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767981136  517 -RKGSFIQHSVSGLCLETKPA-----QLVTSKC 543
Cdd:pfam00652  85 dEDGTQIRNPQSGKCLDVSGAgtsngKVILWTC 117
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 126-236 4.67e-16

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 77.05  E-value: 4.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 126 SVIITFHNEARsTLLRTVKSVLNRTPANLiqEIILVDDFSSDP-EDCL--LLTRIPKVKCLRNDRREGLIRSRVRGADVA 202
Cdd:COG0463    5 SVVIPTYNEEE-YLEEALESLLAQTYPDF--EIIVVDDGSTDGtAEILreLAAKDPRIRVIRLERNRGKGAARNAGLAAA 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767981136 203 AATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVV 236
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 441-543 1.32e-07

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 50.20  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136   441 CLESQGQNTAgdflLGMGICRGSAKNpqpaQAWLF-SDHLIQQQ--GKCLAATStlmsSPGSPVILQMCNPREGKQKWR- 516
Cdd:smart00458   9 CLDVNGNKNP----VGLFDCHGTGGN----QLWKLtSDGAIRIKdtDLCLTANG----NTGSTVTLYSCDGTNDNQYWEv 76

                           90       100       110
                   ....*....|....*....|....*....|.
gi 767981136   517 RKGSFIQHSVSGLCLE----TKPAQLVTSKC 543
Cdd:smart00458  77 NKDGTIRNPDSGKCLDvkdgNTGTKVILWTC 107
 
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 ...
 126-420 0e+00

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: 512.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 126 SVIITFHNEARSTLLRTVKSVLNRTPANLIQEIILVDDFSSDPEDCLLL-----TRIPKVKCLRNDRREGLIRSRVRGAD 200
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 201 VAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKmTR 280
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 281 TDPTRPIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFR-KRHPYNFPEGN 359
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767981136 360 AlTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMNCKSFRWYLENVY 420
Cdd:cd02510  240 G-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT16 cd23479
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 426-557 9.33e-64

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 16 (GALNT16) and similar proteins; GALNT16 (EC 2.4.1.41), also called polypeptide GalNAc transferase 16, GalNAc-T16, polypeptide GalNAc transferase-like protein 1, GalNAc-T-like protein 1, pp-GaNTase-like protein 1, polypeptide N-acetylgalactosaminyltransferase-like protein 1, protein-UDP acetylgalactosaminyltransferase-like protein 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. GALNT16 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: 467357  Cd Length: 129  Bit Score: 204.66  E-value: 9.33e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 426 PVKEALPGIIKQGVNCLESQGQNTAGDFLLGMGICRGSAKNPQPAQAWLFSDHLIQQQGKCLAATSTlmsSPGSPVILQM 505
Cdd:cd23479    1 PEKEAIPGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASQEWVLSDPLIRQQDKCLAITSF---SPGSKVILEL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767981136 506 CNPREGKQKWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLLPH 557
Cdd:cd23479   78 CNQKDGRQKWKLKGSFIQHQVSGLCLDSQSGRVVINQCQADLASQQWELLQV 129
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 429-543 8.41e-35

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: 127.13  E-value: 8.41e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 429 EALPGIIKQGVNCLESQGQNTAGDFLLGMGICRgsakNPQPAQAWLFS-DHLIQQQGKCLAATSTlmsSPGSPVILQMCN 507
Cdd:cd23441    2 ELAYGQIKQGNLCLDSDEQLFQGPALLILAPCS----NSSDSQEWSFTkDGQLQTQGLCLTVDSS---SKDLPVVLETCS 74

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767981136 508 PrEGKQKWRRKGSFIQHSVSGLCLET-KPAQLVTSKC 543
Cdd:cd23441   75 D-DPKQKWTRTGRQLVHSESGLCLDSrKKKGLVVSPC 110
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 126-306 4.86e-28

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: 110.18  E-value: 4.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136  126 SVIITFHNEArSTLLRTVKSVLNRTPANLiqEIILVDDFSSD--PEDCL-LLTRIPKVKCLRNDRREGLIRSRVRGADVA 202
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGSTDgtVEIAEeYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136  203 AATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPIIDVISLDNFAYlaasadlrggfdWSLHFKWEQIPleqKMTRTD 282
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY------------RRASRITLSRL---PFFLGL 142

                         170       180
                  ....*....|....*....|....
gi 767981136  283 PTRPIRTPVIAGGIFVIDKSWFNH 306
Cdd:pfam00535 143 RLLGLNLPFLIGGFALYRREALEE 166
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 433-533 7.76e-20

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14) and similar proteins; GALNT14 (EC 2.4.1.41), also called polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, protein-UDP acetylgalactosaminyltransferase 14, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. GALNT14 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467356  Cd Length: 140  Bit Score: 86.08  E-value: 7.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 433 GIIKQGVNCLESQGQNTAGDFLLGMGICRGSAKNPQPAQAWLF-SDHLIQQQGKCLAATSTLmssPGSPVILQMCNPREG 511
Cdd:cd23478   10 GVIRQRQNCLESRRVEGQELPNLSLSPCIKSKGVPAKSQEWAYtYNQQIRQQQLCLSVHTLF---PGSPVVLVPCKEGDG 86

                         90       100
                 ....*....|....*....|..
gi 767981136 512 KQKWRRKGSFIQHSVSGLCLET 533
Cdd:cd23478   87 KQRWTKVGSHIEHMASRFCLDT 108
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
441-543 1.92e-17

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 78.73  E-value: 1.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136  441 CLESQGQNTAGdFLLGMGICRGSAKNpqpaQAWLFS-DHLIQQ--QGKCLAATSTlmsSPGSPVILQMCNPREGKQKWR- 516
Cdd:pfam00652  13 CLDVPGGSSAG-GPVGLYPCHGSNGN----QLWTLTgDGTIRSvaSDLCLDVGST---ADGAKVVLWPCHPGNGNQRWRy 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767981136  517 -RKGSFIQHSVSGLCLETKPA-----QLVTSKC 543
Cdd:pfam00652  85 dEDGTQIRNPQSGKCLDVSGAgtsngKVILWTC 117
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 126-236 4.67e-16

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 77.05  E-value: 4.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 126 SVIITFHNEARsTLLRTVKSVLNRTPANLiqEIILVDDFSSDP-EDCL--LLTRIPKVKCLRNDRREGLIRSRVRGADVA 202
Cdd:COG0463    5 SVVIPTYNEEE-YLEEALESLLAQTYPDF--EIIVVDDGSTDGtAEILreLAAKDPRIRVIRLERNRGKGAARNAGLAAA 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767981136 203 AATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVV 236
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 127-270 1.28e-14

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: 71.38  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 127 VIITFHNEARsTLLRTVKSVLNRTPANLiqEIILVDDFSSD--PEDCL-LLTRIPKVKCLRNDRREGLIRSRVRGADVAA 203
Cdd:cd00761    1 VIIPAYNEEP-YLERCLESLLAQTYPNF--EVIVVDDGSTDgtLEILEeYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767981136 204 ATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVspiidVISLDNFAYLAASADLRGGFDWSLHFKWE 270
Cdd:cd00761   78 GEYILFLDADDLLLPDWLERLVAELLADPEADA-----VGGPGNLLFRRELLEEIGGFDEALLSGEE 139
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
123-376 2.09e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 71.95  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 123 PATSVIITFHNEArSTLLRTVKSVLNRTPANLiqEIILVDDFSSDPE-DCLLLTRIPKVKCLRNDRREGLIRSRVRGADV 201
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTaELLAALAFPRVRVIRNPENLGFAAARNLGLRA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 202 AAATVLTFLDSHCEVNTEWLPPMlqrvkedhtrvvspiidvisldnfayLAASAdlrggfdwslhfkweqipleqkmtrt 281
Cdd:COG1216   80 AGGDYLLFLDDDTVVEPDWLERL--------------------------LAAAC-------------------------- 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 282 dptrpirtpviaggiFVIDKSWFNHLGKYDAQMDIWGGEnFELSFRVWMCGGSLEIVPCSRVGHVFRKRHpynFPEGNAL 361
Cdd:COG1216  108 ---------------LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASS---GPLLRAY 168

                        250
                 ....*....|....*
gi 767981136 362 TYIRNTKRTAEVWMD 376
Cdd:COG1216  169 YLGRNRLLFLRKHGP 183
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 433-543 8.21e-14

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: 68.12  E-value: 8.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 433 GIIKQGVNCLESQGqNTAGDfLLGMGICRGSAKNpqpaQAWLFS-DHLIQQQGKCLAATStlmSSPGSPVILQMCNPREG 511
Cdd:cd23434    3 GSLKQGNLCLDTLG-HKAGG-TVGLYPCHGTGGN----QEWSFTkDGQIKHDDLCLTVVD---RAPGSLVTLQPCREDDS 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767981136 512 KQKWRR--KGSFIQHSVSGLCLETKPAQ---LVTSKC 543
Cdd:cd23434   74 NQKWEQieNNSKLRHVGSNLCLDSRNAKsggLTVETC 110
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 119-236 2.96e-11

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: 64.76  E-value: 2.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 119 SSDLPATSVIITFHNEARsTLLRTVKSVLNRTPANLIQEIILVDDFSSDPEDCLLLT---RIPKVKCLRNDRREGLIRSR 195
Cdd:COG1215   25 PADLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIARElaaEYPRVRVIERPENGGKAAAL 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767981136 196 VRGADVAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVV 236
Cdd:COG1215  104 NAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS 144
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 441-543 6.08e-09

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: 54.24  E-value: 6.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 441 CLESQGQNTAGDflLGMGICRGSAKNpqpaQAWLFSDHL-IQQQGKCLAAtstlmSSPGSPVILQMCNPREGKQKWR--R 517
Cdd:cd23433   17 CLDTMGRKAGEK--VGLSSCHGQGGN----QVFSYTAKGeIRSDDLCLDA-----SRKGGPVKLEKCHGMGGNQEWEydK 85

                         90       100       110
                 ....*....|....*....|....*....|
gi 767981136 518 KGSFIQHSVSGLCL----ETKPAQLVTSKC 543
Cdd:cd23433   86 ETKQIRHVNSGLCLtapnEDDPNEPVLRPC 115
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 441-543 1.32e-07

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 50.20  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136   441 CLESQGQNTAgdflLGMGICRGSAKNpqpaQAWLF-SDHLIQQQ--GKCLAATStlmsSPGSPVILQMCNPREGKQKWR- 516
Cdd:smart00458   9 CLDVNGNKNP----VGLFDCHGTGGN----QLWKLtSDGAIRIKdtDLCLTANG----NTGSTVTLYSCDGTNDNQYWEv 76

                           90       100       110
                   ....*....|....*....|....*....|.
gi 767981136   517 RKGSFIQHSVSGLCLE----TKPAQLVTSKC 543
Cdd:smart00458  77 NKDGTIRNPDSGKCLDvkdgNTGTKVILWTC 107
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 127-236 2.52e-07

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: 51.03  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 127 VIITFHNEARsTLLRTVKSVLNRTPANLIQEIILVDDFSSDpeDCL-----LLTRIPKVKCLRNDRREGLIRSRVRGADV 201
Cdd:cd04179    1 VVIPAYNEEE-NIPELVERLLAVLEEGYDYEIIVVDDGSTD--GTAeiareLAARVPRVRVIRLSRNFGKGAAVRAGFKA 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767981136 202 AAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVV 236
Cdd:cd04179   78 ARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVV 112
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 441-543 2.91e-07

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: 49.67  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 441 CLESQGQNTAGDFLLGMGICRGsaknPQPAQAWLFS-DHLIQQQGKCLAATStlmssPGSPVILQMCNPREGKQKWR--R 517
Cdd:cd23462   16 CLDAPGRKKELNKPVGLYPCHG----QGGNQYWMLTkDGEIRRDDLCLDYAG-----GSGDVTLYPCHGMKGNQFWIydE 86

                         90       100
                 ....*....|....*....|....*...
gi 767981136 518 KGSFIQHSVSGLCLETKPA--QLVTSKC 543
Cdd:cd23462   87 ETKQIVHGTSKKCLELSDDssKLVMEPC 114
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 127-267 1.32e-06

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: 49.59  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 127 VIITFHNEARsTLLRTVKSVLNRT-PANLIqEIILVDDFSSDpEDCLLLT-----RIPKVKCLRNDRREGLIRSRV--RG 198
Cdd:cd04192    1 VVIAARNEAE-NLPRLLQSLSALDyPKEKF-EVILVDDHSTD-GTVQILEfaaakPNFQLKILNNSRVSISGKKNAltTA 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767981136 199 ADVAAATVLTFLDSHCEVNTEWLPPMLQ-RVKEDHTRVVSPII---------DVISLDnFAYLAASAdlRGGFDWSLHF 267
Cdd:cd04192   78 IKAAKGDWIVTTDADCVVPSNWLLTFVAfIQKEQIGLVAGPVIyfkgksllaKFQRLD-WLSLLGLI--AGSFGLGKPF 153
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 126-388 1.67e-06

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: 49.97  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136  126 SVIITFHN-EARSTLLRTVKSVLNRTPANLiqEIILVDDFSSDPedclLLTRIPKVKCLR--------NDRREGLIRSRV 196
Cdd:pfam10111   1 SVVIPVYNgEKTHWIQERILNQTFQYDPEF--ELIIINDGSTDK----TLEEVSSIKDHNlqvyypnaPDTTYSLAASRN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136  197 RGADVAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTR------VVSPIIDVISldnfaylAASADLRGGFDWSlhfkWE 270
Cdd:pfam10111  75 RGTSHAIGEYISFIDGDCLWSPDKFEKQLKIATSLALQeniqaaVVLPVTDLND-------ESSNFLRRGGDLT----AS 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136  271 QIPLEQKMTRTDPTRPIRTPviAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPcsrVGHVFRKR 350
Cdd:pfam10111 144 GDVLRDLLVFYSPLAIFFAP--NSSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRLAARYPFVAVMP---PQLLYRLS 218

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767981136  351 HPYNFPEGNALTYIRNTKRTAEVWMDEYKQYYYEARPS 388
Cdd:pfam10111 219 AKSMSPYSGFRRFLGDLARQAAACGKVLKHAYHDAPPS 256
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 434-543 2.10e-06

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: 47.05  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 434 IIKQGVN-CLESQGQnTAGDFLLGMGICRGSAKNpqpaQAWLFS-DHLIQQQGKCLAATStlmsspGSPVILQMCNPREG 511
Cdd:cd23460    5 IKHTESGlCLDWAGE-SNGDKTVALKPCHGGGGN----QFWMYTgDGQIRQDHLCLTADE------GNKVTLRECADQLP 73

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767981136 512 KQKW--RRKGSFIQHSVSGLCLETKPA--QLVTSKC 543
Cdd:cd23460   74 SQEWsyDEKTGTIRHRSTGLCLTLDANndVVILKEC 109
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 441-543 7.82e-06

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: 45.36  E-value: 7.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 441 CLESQGQNTAGdfLLGMGICRGSAKNpqpaQAW-LFSDHLIQQQGKCLAAtstlmSSPGSPVILQMCNPREgKQKWR--R 517
Cdd:cd23437   16 CLDTMGHQNGG--PVGLYPCHGMGGN----QLFrLNEAGQLAVGEQCLTA-----SGSGGKVKLRKCNLGE-TGKWEydE 83

                         90       100
                 ....*....|....*....|....*...
gi 767981136 518 KGSFIQHSVSGLCLE--TKPAQLVTSKC 543
Cdd:cd23437   84 ATGQIRHKGTGKCLDlnEGTNKLILQPC 111
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 441-516 8.60e-06

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: 45.40  E-value: 8.60e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767981136 441 CLESQGQNTagdflLGMGICRGSAKNPQPAQAWLFS-DHLIQQ--QGKCLAATstlmsspGSPVILQMCNPREGKQKWR 516
Cdd:cd23435   60 CLHASGSDE-----VILQHCTSKGKDVPPEQKWLFTqDGTIRNpaSGLCLHAS-------GYKVLLRTCNPSDDSQKWT 126
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 126-348 1.11e-05

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: 47.23  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 126 SVIITFHNEARsTLLRTVKSVLN-RTPANLIqEIILVDDFSSD-PEDCL--LLTRIPKVKCLRNDRReglIRS--RVRGA 199
Cdd:cd02525    3 SIIIPVRNEEK-YIEELLESLLNqSYPKDLI-EIIVVDGGSTDgTREIVqeYAAKDPRIRLIDNPKR---IQSagLNIGI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 200 DVAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPIIDVISLDNF----AYLAASADLRGGfdwSLHfkweqiple 275
Cdd:cd02525   78 RNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFqkaiAVAQSSPLGSGG---SAY--------- 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767981136 276 qkmtRTDPTRPIRTPVIAGGIFviDKSWFNHLGKYDAQMDIwgGENFELSFRVWMCGGSLEIVPCSRVGHVFR 348
Cdd:cd02525  146 ----RGGAVKIGYVDTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPR 210
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 292-352 1.37e-05

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: 43.37  E-value: 1.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767981136  292 IAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCsRVGHVFRKRHP 352
Cdd:pfam02709  19 YFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG-DIGRYYMLYHK 78
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 424-532 2.70e-05

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: 43.86  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 424 TVPVKEALPGiikqgvNCLESQGQNTAGDFLLGMGICRGSAknpqpAQAWLF-SDHLIQQQGKCLAATSTLMSSpGSPVI 502
Cdd:cd23451    2 TGPVRLANAG------KCLDVPGSSTADGNPVQIYTCNGTA-----AQKWTLgTDGTLRVLGKCLDVSGGGTAN-GTLVQ 69

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767981136 503 LQMCNPrEGKQKWR-RKGSFIQHSVSGLCLE 532
Cdd:cd23451   70 LWDCNG-TGAQKWVpRADGTLYNPQSGKCLD 99
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 127-345 2.87e-05

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: 44.47  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 127 VIITFHNEARsTLLRTVKSVLNRTPANLiqEIILVDDFSSDPEDCLLLTRIPKVKCLRNDRREGLIRSRVRGADVAAATV 206
Cdd:cd04186    1 IIIVNYNSLE-YLKACLDSLLAQTYPDF--EVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 207 LTFLDSHCEVNTEWLPPMLQRVKEDhtrvvsPIIDVIsldnfaylaasadlrggfdwslhfkweqipleqkmtrtdptrp 286
Cdd:cd04186   78 VLLLNPDTVVEPGALLELLDAAEQD------PDVGIV------------------------------------------- 108

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767981136 287 irTPVIAGGIFVIDKSWFNHLGKYDAQMDIWgGENFELSFRVWMCGGSLEIVPCSRVGH 345
Cdd:cd04186  109 --GPKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYH 164
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 123-349 3.14e-05

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 45.44  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136  123 PATSVIITFHNEArSTLLRTVKSVLNRTPANLiqEIILVDDFSSD--PEDCLLLTRIP---KVKCLRNDRREGL---IRS 194
Cdd:pfam13641   2 PDVSVVVPAFNED-SVLGRVLEAILAQPYPPV--EVVVVVNPSDAetLDVAEEIAARFpdvRLRVIRNARLLGPtgkSRG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136  195 RVRGADVAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPIIDVislDNFAYLAASADlrggfdwSLHFKWEQIPL 274
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFS---LNRSTMLSALG-------ALEFALRHLRM 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767981136  275 EQkMTRTdptrpIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWggENFELSFRVWMCGGSLEIVPCSRVGHVFRK 349
Cdd:pfam13641 149 MS-LRLA-----LGVLPLSGAGSAIRREVLKELGLFDPFFLLG--DDKSLGRRLRRHGWRVAYAPDAAVRTVFPT 215
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 440-543 4.30e-05

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: 43.47  E-value: 4.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 440 NCLESQGQNTAGDFLLGMGICRGSAKNpqpaQAW-LFSDHLI---QQQGKCLAAtstlmsSPGSPVILQMCNP----REG 511
Cdd:cd23435   14 LCLDVNNPNGQGGKPVIMYGCHGLGGN----QYFeYTSKGEIrhnIGKELCLHA------SGSDEVILQHCTSkgkdVPP 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767981136 512 KQKWR-RKGSFIQHSVSGLCLETKPAQLVTSKC 543
Cdd:cd23435   84 EQKWLfTQDGTIRNPASGLCLHASGYKVLLRTC 116
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 441-532 4.63e-05

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: 43.11  E-value: 4.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 441 CLESQGQNTAGDFLLGMGICRGSAKnpqpaQAWLFSDH--LIQQQGKCLAATSTlMSSPGSPVILQMCNPREGkQKWR-R 517
Cdd:cd23418   16 CLDVPGGSTTNGTRLILWDCHGGAN-----QQFTFTSAgeLRVGGDKCLDAAGG-GTTNGTPVVIWPCNGGAN-QKWRfN 88

                         90
                 ....*....|....*
gi 767981136 518 KGSFIQHSVSGLCLE 532
Cdd:cd23418   89 SDGTIRNVNSGLCLD 103
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 127-187 1.27e-04

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: 42.85  E-value: 1.27e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767981136 127 VIITFHNEARS--TLLRTVKSVLNRTPANLiqEIILVDDFSSDpeDCL-----LLTRIPKVKCLRNDR 187
Cdd:cd04187    1 IVVPVYNEEENlpELYERLKAVLESLGYDY--EIIFVDDGSTD--RTLeilreLAARDPRVKVIRLSR 64
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 441-543 2.28e-04

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: 41.15  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 441 CLESQGQNTAGDFLLGMGICRGSAKNPQpaqawLFS---DHLIQQQGKCLAATSTlmssPGSPVILQMC--NPREGkQKW 515
Cdd:cd23459   18 CLDTLQRDEDKGYNLGLYPCQGGLSSNQ-----LFSlskKGELRREESCADVQGT----EESKVILITChgLEKFN-QKW 87

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767981136 516 R-RKGSFIQHSVSGLCLETKPAQ----LVTSKC 543
Cdd:cd23459   88 KhTKGGQIVHLASGKCLDAEGLKsgddVTLAKC 120
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 433-516 4.37e-04

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: 40.36  E-value: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 433 GIIKQGVNCLESQGQNTAgdflLGMGICRGSaknpqPAQAWLF--SDHLIQ--QQGKCLAATStlmssPGSPVILQMCNP 508
Cdd:cd23437   48 GQLAVGEQCLTASGSGGK----VKLRKCNLG-----ETGKWEYdeATGQIRhkGTGKCLDLNE-----GTNKLILQPCDS 113


                 ....*...
gi 767981136 509 REGKQKWR 516
Cdd:cd23437  114 SSPSQKWE 121
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 494-543 8.79e-04

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: 39.63  E-value: 8.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767981136 494 MSSPGSPVILQMCNPREGKQKW--RRKGSFIQHSVSGLCLETKPAQ--LVTSKC 543
Cdd:cd23439   62 SHTPGAPVILYACHGMKGNQLWkyRPNTKQLYHPVSGLCLDADPGSgkVFMNHC 115
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 127-167 1.36e-03

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 40.35  E-value: 1.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 767981136 127 VIITFhNEARsTLLRTVKSVlnrtpANLIQEIILVDDFSSD 167
Cdd:cd02511    5 VIITK-NEER-NIERCLESV-----KWAVDEIIVVDSGSTD 38
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 479-548 2.77e-03

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


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 37.96  E-value: 2.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767981136 479 LIQ--QQGKCLAAtstlmSSPGSPVILQMCNPREGKQKWRR-KGSFIQHSVSGLCL----ETKPAQLVTSKCQADAQ 548
Cdd:cd23385    4 LIYneDLGKCLAA-----RSSSSKVSLSTCNPNSPNQQWKWtSGHRLFNVGTGKCLgvssSSPSSPLRLFECDSEDE 75
beta-trefoil_Ricin_RIPs_II_rpt1 cd23443
first ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ...
 465-536 3.83e-03

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: 37.66  E-value: 3.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767981136 465 KNPQPAQAWLF-SDHLIQQQGKCLAATStlmSSPGSPVILQMCN--PREGKqKWRRK--GSFIqHSVSGLCLETKPA 536
Cdd:cd23443   32 KSQDANQLWTFkRDGTIRSNGKCLTTNG---YSPGSYVVIYDCStaVAEAT-KWEVSddGTII-NPASGLVLTADSG 103
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 441-542 5.72e-03

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


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 37.19  E-value: 5.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 441 CLesqgQNTAGDFLLGMGICRGSAknpqPAQAWL-FSDHLIQQQG--KCLAATStlmSSPGSPVILQMCNPREGKQKWR- 516
Cdd:cd23385   13 CL----AARSSSSKVSLSTCNPNS----PNQQWKwTSGHRLFNVGtgKCLGVSS---SSPSSPLRLFECDSEDELQKWKc 81

                         90       100
                 ....*....|....*....|....*...
gi 767981136 517 --RKGSFIQHSVSGLCLETKPAQLVTSK 542
Cdd:cd23385   82 skDGLLLLKGLGLLLLYDKSGKNVVVSK 109
beta-trefoil_Ricin_AglA cd23425
ricin B-type lectin domain, beta-trefoil fold, found in alpha-galactosidase A (AglA) and ...
 440-542 8.68e-03

ricin B-type lectin domain, beta-trefoil fold, found in alpha-galactosidase A (AglA) and similar proteins; AglA (EC 3.2.1.22), also called melibiase A, hydrolyzes a variety of simple alpha-D-galactosides as well as more complex molecules such as oligosaccharides and polysaccharides. It belongs to the glycosyl hydrolase 27 (GH27) family. AglA contains an N-terminal GH27 catalytic domain, an alpha galactosidase C-terminal beta sandwich domain in the middle region, and a carbohydrate-binding domain at the C-terminus. The carbohydrate-binding domain is also known as a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.


Pssm-ID: 467303 [Multi-domain]  Cd Length: 116  Bit Score: 36.27  E-value: 8.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767981136 440 NCLESQGQNtagdflLGMGICRGSAKnpqpaQAW-LFSDHLIQ---QQGKCLAATstlmsspGSPVILQMCNPREGkQKW 515
Cdd:cd23425   14 NCLTADAAE------VKFQTCDGSDS-----QIWqVRKSGILRnlsNTGQCLTAD-------GANVSLSPCDTSTS-QNW 74

                         90       100
                 ....*....|....*....|....*...
gi 767981136 516 R-RKGSFIQHSVSGLCLETKPAQLVTSK 542
Cdd:cd23425   75 SyEISGNLVNKKTGLCLTEGNDAQVTVT 102
 
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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