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Conserved domains on  [gi|269784709|ref|NP_001161453|]
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N-acetylgalactosaminyltransferase 7 isoform 2 [Mus musculus]

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 ...
 210-518 5.92e-167

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: 479.39  E-value: 5.92e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 210 SVVIVFHNEGWSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKVFRNERREGLIQARSIGAQ 289
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 290 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRATCTVPLIDYIDGNDYSIEPQqggdeDGFARGAWDWSMLWKRIPLSH 369
Cdd:cd02510   81 AAT-GDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGS-----SGDARGGFDWSLHFKWLPLPE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 370 KEKaKRKHKTEPYRSPAMAGGLFAIEKDFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLLFVPCSRVGHIYRLegwQG 449
Cdd:cd02510  155 EER-RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRR---KR 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784709 450 NPPPLYVGSSPTLKNYVRVVEVWWDEYKDYFYASRPESKALPYGDISELKKFREDHNCKSFKWFMEEIA 518
Cdd:cd02510  231 KPYTFPGGSGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 530-653 9.00e-65

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: 209.07  E-value: 9.00e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNLNEFKEWQ 609
Cdd:cd23437    1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 269784709 610 YFKSLHRFTHITSGKCLDRSEVLHQVFISTCDSSKMTQKWEMNN 653
Cdd:cd23437   81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124
 
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 ...
 210-518 5.92e-167

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: 479.39  E-value: 5.92e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 210 SVVIVFHNEGWSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKVFRNERREGLIQARSIGAQ 289
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 290 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRATCTVPLIDYIDGNDYSIEPQqggdeDGFARGAWDWSMLWKRIPLSH 369
Cdd:cd02510   81 AAT-GDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGS-----SGDARGGFDWSLHFKWLPLPE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 370 KEKaKRKHKTEPYRSPAMAGGLFAIEKDFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLLFVPCSRVGHIYRLegwQG 449
Cdd:cd02510  155 EER-RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRR---KR 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784709 450 NPPPLYVGSSPTLKNYVRVVEVWWDEYKDYFYASRPESKALPYGDISELKKFREDHNCKSFKWFMEEIA 518
Cdd:cd02510  231 KPYTFPGGSGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 530-653 9.00e-65

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: 209.07  E-value: 9.00e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNLNEFKEWQ 609
Cdd:cd23437    1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 269784709 610 YFKSLHRFTHITSGKCLDRSEVLHQVFISTCDSSKMTQKWEMNN 653
Cdd:cd23437   81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 210-397 7.83e-29

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: 112.87  E-value: 7.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709  210 SVVIVFHNEgWSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLDEYIKLwNGLVKVFRNERREGLIQARSIGAQ 289
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKK-DPRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709  290 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRATCTVPLIDYIDGNDYSiepqqggdedgfargaWDWSMLWKRIPLSH 369
Cdd:pfam00535  76 AAT-GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGE----------------YRRASRITLSRLPF 138

                         170       180
                  ....*....|....*....|....*...
gi 269784709  370 KEKAKRKHKTEPYRSPAMAGGLFAIEKD 397
Cdd:pfam00535 139 FLGLRLLGLNLPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
534-649 1.00e-25

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 102.61  E-value: 1.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709  534 WGEIRGLETAYCIDSMG-KTNGGFVELGPCHRMGGNQLFRINEANQLMQY--DQCLTKG--PDGSKVMITHCNLNEFKE- 607
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGgSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVasDLCLDVGstADGAKVVLWPCHPGNGNQr 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 269784709  608 WQYFKSLHRFTHITSGKCLDRSEVLH---QVFISTCDSSKMTQKW 649
Cdd:pfam00652  82 WRYDEDGTQIRNPQSGKCLDVSGAGTsngKVILWTCDSGNPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 537-649 9.76e-17

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 76.40  E-value: 9.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709   537 IRGLETAYCIDSMGktNGGFVELGPCHRMGGNQLFRINEANQLM--QYDQCLT-KGPDGSKVMITHC-NLNEFKEWQYFK 612
Cdd:smart00458   1 IISGNTGKCLDVNG--NKNPVGLFDCHGTGGNQLWKLTSDGAIRikDTDLCLTaNGNTGSTVTLYSCdGTNDNQYWEVNK 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 269784709   613 SlHRFTHITSGKCLDRSEVLH--QVFISTCDSSKmTQKW 649
Cdd:smart00458  79 D-GTIRNPDSGKCLDVKDGNTgtKVILWTCSGNP-NQKW 115
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 210-434 3.31e-12

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 66.26  E-value: 3.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 210 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLDEYIKLWNGlVKVFRNERREGLIQARSIGAQ 289
Cdd:COG0463    5 SVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGS-TDGTAEILRELAAKDPR-IRVIRLERNRGKGAARNAGLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 290 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRAtctvpliDYIDGNDYSiepqQGGDEDGFARGAWDWSMLWKRIPLSH 369
Cdd:COG0463   80 AAR-GDYIAFLDADDQLDPEKLEELVAALEEGPA-------DLVYGSRLI----REGESDLRRLGSRLFNLVRLLTNLPD 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784709 370 kekakrkhktepyrspaMAGGLFAIEKDFFFELGlYDPGLqiwgGENFEIsYKIWQCGGKLLFVP 434
Cdd:COG0463  148 -----------------STSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVP 189
 
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 ...
 210-518 5.92e-167

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: 479.39  E-value: 5.92e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 210 SVVIVFHNEGWSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKVFRNERREGLIQARSIGAQ 289
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 290 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRATCTVPLIDYIDGNDYSIEPQqggdeDGFARGAWDWSMLWKRIPLSH 369
Cdd:cd02510   81 AAT-GDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGS-----SGDARGGFDWSLHFKWLPLPE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 370 KEKaKRKHKTEPYRSPAMAGGLFAIEKDFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLLFVPCSRVGHIYRLegwQG 449
Cdd:cd02510  155 EER-RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRR---KR 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784709 450 NPPPLYVGSSPTLKNYVRVVEVWWDEYKDYFYASRPESKALPYGDISELKKFREDHNCKSFKWFMEEIA 518
Cdd:cd02510  231 KPYTFPGGSGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 530-653 9.00e-65

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: 209.07  E-value: 9.00e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNLNEFKEWQ 609
Cdd:cd23437    1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 269784709 610 YFKSLHRFTHITSGKCLDRSEVLHQVFISTCDSSKMTQKWEMNN 653
Cdd:cd23437   81 YDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEFNE 124
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 210-397 7.83e-29

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: 112.87  E-value: 7.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709  210 SVVIVFHNEgWSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLDEYIKLwNGLVKVFRNERREGLIQARSIGAQ 289
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKK-DPRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709  290 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRATCTVPLIDYIDGNDYSiepqqggdedgfargaWDWSMLWKRIPLSH 369
Cdd:pfam00535  76 AAT-GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGE----------------YRRASRITLSRLPF 138

                         170       180
                  ....*....|....*....|....*...
gi 269784709  370 KEKAKRKHKTEPYRSPAMAGGLFAIEKD 397
Cdd:pfam00535 139 FLGLRLLGLNLPFLIGGFALYRREALEE 166
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 535-653 1.27e-28

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: 110.86  E-value: 1.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 535 GEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCN-LNEFKEWQYFKS 613
Cdd:cd23433    7 GEIRNVETNLCLDTMGRKAGEKVGLSSCHGQGGNQVFSYTAKGEIRSDDLCLDASRKGGPVKLEKCHgMGGNQEWEYDKE 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 269784709 614 LHRFTHITSGKCLDRSEVLH--QVFISTCDSSKmTQKWEMNN 653
Cdd:cd23433   87 TKQIRHVNSGLCLTAPNEDDpnEPVLRPCDGGP-SQKWELEG 127
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
534-649 1.00e-25

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 102.61  E-value: 1.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709  534 WGEIRGLETAYCIDSMG-KTNGGFVELGPCHRMGGNQLFRINEANQLMQY--DQCLTKG--PDGSKVMITHCNLNEFKE- 607
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGgSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVasDLCLDVGstADGAKVVLWPCHPGNGNQr 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 269784709  608 WQYFKSLHRFTHITSGKCLDRSEVLH---QVFISTCDSSKMTQKW 649
Cdd:pfam00652  82 WRYDEDGTQIRNPQSGKCLDVSGAGTsngKVILWTCDSGNPNQQW 126
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 535-652 1.13e-25

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: 102.14  E-value: 1.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 535 GEIRGLETAYCIDSMGKTNGGF-VELGPCHRMGGNQLFRINEANQLMQYDQCLTkGPDGSKVMITHCNLNEFKE-WQYFK 612
Cdd:cd23460    3 GQIKHTESGLCLDWAGESNGDKtVALKPCHGGGGNQFWMYTGDGQIRQDHLCLT-ADEGNKVTLRECADQLPSQeWSYDE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 269784709 613 SLHRFTHITSGKCLDRSEVLHQVFISTCDSSKMTQKWEMN 652
Cdd:cd23460   82 KTGTIRHRSTGLCLTLDANNDVVILKECDSNSLWQKWIFQ 121
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 545-649 5.94e-21

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: 88.53  E-value: 5.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 545 CIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLT--KGPDGSKVMITHC-NLNEFKEWQYFKSLHRFTHIT 621
Cdd:cd23434   11 CLDTLGHKAGGTVGLYPCHGTGGNQEWSFTKDGQIKHDDLCLTvvDRAPGSLVTLQPCrEDDSNQKWEQIENNSKLRHVG 90

                         90       100
                 ....*....|....*....|....*....
gi 269784709 622 SGKCLD-RSEVLHQVFISTCDSSKMTQKW 649
Cdd:cd23434   91 SNLCLDsRNAKSGGLTVETCDPSSGSQQW 119
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 530-650 1.76e-19

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: 84.72  E-value: 1.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELG--PCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHC-NLNEFK 606
Cdd:cd23462    1 EALAYGEIRNLAGKLCLDAPGRKKELNKPVGlyPCHGQGGNQYWMLTKDGEIRRDDLCLDYAGGSGDVTLYPChGMKGNQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 269784709 607 EWQYFKSLHRFTHITSGKCLDRSEVLHQVFISTCDSSKMTQKWE 650
Cdd:cd23462   81 FWIYDEETKQIVHGTSKKCLELSDDSSKLVMEPCNGSSPRQQWE 124
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 537-649 9.76e-17

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 76.40  E-value: 9.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709   537 IRGLETAYCIDSMGktNGGFVELGPCHRMGGNQLFRINEANQLM--QYDQCLT-KGPDGSKVMITHC-NLNEFKEWQYFK 612
Cdd:smart00458   1 IISGNTGKCLDVNG--NKNPVGLFDCHGTGGNQLWKLTSDGAIRikDTDLCLTaNGNTGSTVTLYSCdGTNDNQYWEVNK 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 269784709   613 SlHRFTHITSGKCLDRSEVLH--QVFISTCDSSKmTQKW 649
Cdd:smart00458  79 D-GTIRNPDSGKCLDVKDGNTgtKVILWTCSGNP-NQKW 115
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 534-649 1.30e-14

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: 70.83  E-value: 1.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 534 WGEIRGLETAYCIDSMGKTNGGFVELGPC--HRMGGNQLFRIN--EANQLMQYDQCL--TKGPDGSKVMITHC-----NL 602
Cdd:cd23439    2 SGEIRNVGSGLCIDTKHGGENDEVRLSKCvkDGGGGEQQFELTwhEDIRPKKRKVCFdvSSHTPGAPVILYAChgmkgNQ 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 269784709 603 NefkeWQYFKSLHRFTHITSGKCLDRSEVLHQVFISTCDSSKMTQKW 649
Cdd:cd23439   82 L----WKYRPNTKQLYHPVSGLCLDADPGSGKVFMNHCDESSDTQKW 124
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 534-653 3.90e-14

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: 69.66  E-value: 3.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 534 WGEIRGLETAYCIDSMGKTNGGFVELG--PCHRMG-GNQLFRINEANQLMQYDQCLT-KGPDGSKVMITHC--NLNEFKE 607
Cdd:cd23459    7 YGQVRNPGTNLCLDTLQRDEDKGYNLGlyPCQGGLsSNQLFSLSKKGELRREESCADvQGTEESKVILITChgLEKFNQK 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 269784709 608 WQYFKSLHRFtHITSGKCLDRSEV--LHQVFISTCDSSkMTQKWEMNN 653
Cdd:cd23459   87 WKHTKGGQIV-HLASGKCLDAEGLksGDDVTLAKCDGS-LSQKWTFEH 132
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 535-653 7.04e-14

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: 68.92  E-value: 7.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 535 GEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHC-NLNEFKEWQYFKS 613
Cdd:cd23466    7 GEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDDLCLDVSKLNGPVMMLKChHLKGNQLWEYDPV 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 269784709 614 LHRFTHITSGKCLDR-SEVLHQV-FISTCDSSKmTQKWEMNN 653
Cdd:cd23466   87 KLTLLHVNSNQCLDKaTEEDSQVpSIRDCNGSR-SQQWLLRN 127
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 534-651 5.54e-13

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: 65.89  E-value: 5.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 534 WGEIRGLETayCIDSMGKTNGG--FVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPD--GSKVMITHCNLNEFKEWQ 609
Cdd:cd23441    5 YGQIKQGNL--CLDSDEQLFQGpaLLILAPCSNSSDSQEWSFTKDGQLQTQGLCLTVDSSskDLPVVLETCSDDPKQKWT 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 269784709 610 YFKSlhRFTHITSGKCLDrSEVLHQVFISTCDSSKMTQKWEM 651
Cdd:cd23441   83 RTGR--QLVHSESGLCLD-SRKKKGLVVSPCRSGAPSQKWDF 121
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 535-649 9.69e-13

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: 65.43  E-value: 9.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 535 GEIRGLETAYCIDSMG--KTNGGFVELGPCHRMGGNQLFRINEANQL---MQYDQCLTKGPDGSkVMITHCNL-----NE 604
Cdd:cd23435    5 GALRNKGSELCLDVNNpnGQGGKPVIMYGCHGLGGNQYFEYTSKGEIrhnIGKELCLHASGSDE-VILQHCTSkgkdvPP 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 269784709 605 FKEWQYFKSLHRFtHITSGKCLDRSEvlHQVFISTCDSSKMTQKW 649
Cdd:cd23435   84 EQKWLFTQDGTIR-NPASGLCLHASG--YKVLLRTCNPSDDSQKW 125
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 210-434 3.31e-12

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 66.26  E-value: 3.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 210 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLDEYIKLWNGlVKVFRNERREGLIQARSIGAQ 289
Cdd:COG0463    5 SVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGS-TDGTAEILRELAAKDPR-IRVIRLERNRGKGAARNAGLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 290 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRAtctvpliDYIDGNDYSiepqQGGDEDGFARGAWDWSMLWKRIPLSH 369
Cdd:COG0463   80 AAR-GDYIAFLDADDQLDPEKLEELVAALEEGPA-------DLVYGSRLI----REGESDLRRLGSRLFNLVRLLTNLPD 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784709 370 kekakrkhktepyrspaMAGGLFAIEKDFFFELGlYDPGLqiwgGENFEIsYKIWQCGGKLLFVP 434
Cdd:COG0463  148 -----------------STSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVP 189
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 530-653 5.63e-12

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: 63.12  E-value: 5.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 530 RNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGP-DGSKVMITHCNLNEFKEW 608
Cdd:cd23467    2 RYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRlNGPVVMLKCHHMRGNQLW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 269784709 609 QYFKSLHRFTHITSGKCLDRSEVLHQVF--ISTCDSSKmTQKWEMNN 653
Cdd:cd23467   82 EYDAERLTLRHVNSNQCLDEPSEEDKMVptMKDCSGSR-SQQWLLRN 127
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 211-322 3.18e-11

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: 62.14  E-value: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 211 VVIVFHNEGwSTLMRTVHSVIKRTPRKYlaEIVLIDDFSnKEHLKEKLDEYIKlWNGLVKVFRNERREGLIQARSIGAQK 290
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGS-TDGTLEILEEYAK-KDPRVIRVINEENQGLAAARNAGLKA 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 269784709 291 AKlGQVLIYLDAHCEVAVNWYAPLVAPISKDR 322
Cdd:cd00761   76 AR-GEYILFLDADDLLLPDWLERLVAELLADP 106
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 210-440 1.26e-10

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: 62.84  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 210 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYLAEIVLIDDfSNKEHLKEKLDEYIKLWNGlVKVFRNERREGLIQARSIGAQ 289
Cdd:COG1215   32 SVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDD-GSTDETAEIARELAAEYPR-VRVIERPENGGKAAALNAGLK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 290 KAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRAtctvplidyidgndysiepqqggdedgfargawdwsmlwkriplsh 369
Cdd:COG1215  109 AAR-GDIVVFLDADTVLDPDWLRRLVAAFADPGV---------------------------------------------- 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784709 370 kekakrkhktepyrspAMAGGLFAIEKDFFFELGLYDPGLqiwGGENFEISYKIWQCGGKLLFVPCSRVGH 440
Cdd:COG1215  142 ----------------GASGANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYE 193
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 545-649 1.61e-10

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: 58.95  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 545 CIDSMGKTNGGFVELGPCHR----MGGNQLFRINEANQLMQY--DQCLTkgPDGSKVMITHCNLNEFKewQYFKSLHRFT 618
Cdd:cd23461   15 CLDILGRSHGGPPVLAKCSSnksmPGTFQNFSLTFHRQIKHGtsDDCLE--VRGNNVRLSRCHYQGGN--QYWKYDYETH 90

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 269784709 619 HITSG----KCLDRSEVLHQVFISTCDSSKMTQKW 649
Cdd:cd23461   91 QLINGgqnnKCLEADVESLKITLSICDSDNVEQKW 125
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 534-649 2.13e-09

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: 55.91  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 534 WGEIRGLETAYCID--SMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNL-NEFKEWQY 610
Cdd:cd23442    5 SGQLYNTGTGYCADyiHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSLQLCLDVRQEQVVLQNCTKeKTSQKWDF 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 269784709 611 FKSlHRFTHITSGKCLD--RSEVLHQVFISTCdSSKMTQKW 649
Cdd:cd23442   85 QET-GRIVHILSGKCIEavESENSKLLFLSPC-NGQRNQMW 123
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 210-440 4.63e-08

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: 54.55  E-value: 4.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 210 SVVIVFHNEGwSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEhLKEKLDEYIKLwNGLVKVFRNERReglIQ--ARSIG 287
Cdd:cd02525    3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTDG-TREIVQEYAAK-DPRIRLIDNPKR---IQsaGLNIG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 288 AQKAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRATCTVplidyidGNDYSIepqqggDEDGFARG-AWDWSMLWKRIP 366
Cdd:cd02525   77 IRNSR-GDIIIRVDAHAVYPKDYILELVEALKRTGADNVG-------GPMETI------GESKFQKAiAVAQSSPLGSGG 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784709 367 LSHKEKAKRKHKTEPYRSPAMagglfaiEKDFFFELGLYDPGLQIwgGENFEISYKIWQCGGKLLFVPCSRVGH 440
Cdd:cd02525  143 SAYRGGAVKIGYVDTVHHGAY-------RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYY 207
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 535-651 1.41e-07

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: 50.84  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 535 GEIRGLETAYCIDSMGK--TNGGFVELGPCHRMGGNQLFRINEANQLMQYDQ-CL-TKGPDGSKVMITHC-NLNEFKEWQ 609
Cdd:cd23440    6 GQLKHAGSGLCLVAEDEvsQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLlCLdSSETSSDFPRLMKChGSGGSQQWR 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 269784709 610 YFKSLHRFtHITSGKCLDRSEVLHQVFIST--CDSSKmTQKWEM 651
Cdd:cd23440   86 FKKDNRLY-NPASGQCLAASKNGTSGYVTMdiCSDSP-SQKWVF 127
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 534-649 1.89e-07

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: 50.45  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 534 WGEIRGLETAYCIDSMG--KTNGGFVELGPCHRmGGNQLFRINEAN------QLMQYDQCLT----KGPDGSKVMITHCN 601
Cdd:cd00161    2 TYRIVNAASGKCLDVAGgsTANGAPVQQWTCNG-GANQQWTLTPVGdgyytiRNVASGKCLDvaggSTANGANVQQWTCN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 269784709 602 LNEFKEWQYFKSLHRFTHIT---SGKCLD----RSEVLHQVFISTCDSSKmTQKW 649
Cdd:cd00161   81 GGDNQQWRLEPVGDGYYRIVnkhSGKCLDvsggSTANGANVQQWTCNGGA-NQQW 134
beta-trefoil_Ricin_GALNTL6 cd23477
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 529-655 2.43e-07

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase-like 6 (GALNTL6) and similar proteins; GALNTL6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 17, GalNAc-T17, pp-GaNTase 17, protein-UDP acetylgalactosaminyltransferase 17, putative polypeptide N-acetylgalactosaminyltransferase 17, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17, 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. GALNTL6 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: 467355  Cd Length: 148  Bit Score: 50.71  E-value: 2.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 529 PRNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGN------QLFR------INEANQLMQYDQCLTKGPDGSKVM 596
Cdd:cd23477    2 PPPAAWGEIRNVAANLCVDSKHGATGTELRLDICVKDGSErtwsheQLFTfgwredIRPGEPLHTRKFCFDAISHNSPVT 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 597 ITHCN-LNEFKEWQYFKSLHRFtHITSGKCLDRSEVLHQVFISTCDSSKMTQKWEMNNIH 655
Cdd:cd23477   82 LYDCHgMKGNQLWSYRKDKTLF-HPVSNSCMDCNPADKKIFMNRCDPLSETQQWIFEHTN 140
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 535-651 3.64e-07

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: 49.87  E-value: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 535 GEIRglETAYCIDSMGKTNGGF--VELGPCHRMGG----NQLFRINEANQLMQYDQCL---TKGPdGSKVMITHCNLNEF 605
Cdd:cd23478   10 GVIR--QRQNCLESRRVEGQELpnLSLSPCIKSKGvpakSQEWAYTYNQQIRQQQLCLsvhTLFP-GSPVVLVPCKEGDG 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 269784709 606 KEwQYFKSLHRFTHITSGKCLDR------SEVLHQVFISTCDSSKMTQKWEM 651
Cdd:cd23478   87 KQ-RWTKVGSHIEHMASRFCLDTemfgdgTESSKEIVINPCESSAMSQRWDM 137
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 534-649 4.16e-07

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10) and similar proteins; GALNT10 (EC 2.4.1.41), also called polypeptide GalNAc transferase 10, GalNAc-T10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. GALNT10 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467354  Cd Length: 150  Bit Score: 49.96  E-value: 4.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 534 WGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGN------QLFR------INEANQLMQYDQCLTKGPDGSKVMITHCN 601
Cdd:cd23476    7 WGEIRNVGTGLCADTKHGALGSPLRLEGCVKGRGEaawnngQVFTfgwredIRPGDPQHTKKFCFDAISHNSPVTLYDCH 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 269784709 602 -LNEFKEWQYFKSlHRFTHITSGKCLDRSEVLHQVFISTCDSSKMTQKW 649
Cdd:cd23476   87 gMKGNQLWRYRKD-KTLYHPVSNSCMDCSESDHRIFMNTCNPSSPTQQW 134
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 581-653 1.11e-05

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: 44.90  E-value: 1.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269784709 581 QYDQCLTKGPDGSKVMITHCNL-NEFKEWQYFkSLHRFTHITSGKCLDRSEVLHQVFIST--CDSSKMTQKWEMNN 653
Cdd:cd23385    9 DLGKCLAARSSSSKVSLSTCNPnSPNQQWKWT-SGHRLFNVGTGKCLGVSSSSPSSPLRLfeCDSEDELQKWKCSK 83
beta-trefoil_Ricin_GALNT16 cd23479
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 545-651 2.41e-05

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: 44.41  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 545 CIDSMGKTNGG--FVELGPCHRMGGNQLFR---INEANQLMQYDQCL--TKGPDGSKVMITHCNLNEFKEWQYFKSlHRF 617
Cdd:cd23479   16 CLESQGQDTTGdtLLGLGECRGTASNLPASqewVLSDPLIRQQDKCLaiTSFSPGSKVILELCNQKDGRQKWKLKG-SFI 94

                         90       100       110
                 ....*....|....*....|....*....|....
gi 269784709 618 THITSGKCLDRSEvlHQVFISTCDSSKMTQKWEM 651
Cdd:cd23479   95 QHQVSGLCLDSQS--GRVVINQCQADLASQQWEL 126
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 381-445 1.87e-04

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: 40.29  E-value: 1.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784709  381 PYRSPAMAGGLFAIEKDFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLLFVPCsRVGHIYRLE 445
Cdd:pfam02709  13 KLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG-DIGRYYMLY 76
beta-trefoil_Ricin_hemolysin cd23423
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ...
 583-656 2.37e-04

ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar proteins; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cytolysis by forming heptameric pores in target host membranes. After binding to target membranes, the protein assembles into a heptameric pre-pore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation. Hemolysin may be called "cytolysin" or "cytolytic toxin", according to a specific action for certain cells. For example, this subfamily includes Vibrio vulnificus cytolysin that attack blood cell membranes and cause cell rupture, thereby liberating hemoglobins. Members of this subfamily contain a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a putative sugar-binding pocket.


Pssm-ID: 467301 [Multi-domain]  Cd Length: 119  Bit Score: 41.21  E-value: 2.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784709 583 DQCLTKGPDGsKVMITHCNLNEFKEWQYFKSLHRFTHIT-SGKCLDRSEVLhQVFISTCDSSkMTQKWE--MNNIHS 656
Cdd:cd23423   14 NRCLTVDNNG-RVTLESCDSGDRNQSWILDSEGRYRSRVaPDLCLDADDDG-LLTLEQCSLS-LTQKWEweGDRLKN 87
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 211-302 3.75e-04

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: 41.79  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 211 VVIVFHNEGwSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEHLkEKLDEYIKLwNGLVKVFRNERREGLIQARSIGAQK 290
Cdd:cd04179    1 VVIPAYNEE-ENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTA-EIARELAAR-VPRVRVIRLSRNFGKGAAVRAGFKA 77

                         90
                 ....*....|..
gi 269784709 291 AKlGQVLIYLDA 302
Cdd:cd04179   78 AR-GDIVVTMDA 88
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 211-440 4.85e-04

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: 41.39  E-value: 4.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 211 VVIVFHNeGWSTLMRTVHSVIKRTPRKYlaEIVLIDDFSNK---EHLKEKLDEyiklwnglVKVFRNERREGLIQARSIG 287
Cdd:cd04186    1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVDNASTDgsvELLRELFPE--------VRLIRNGENLGFGAGNNQG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 288 AQKAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDratctvplidyidgNDYsiepqqggdedgfarGAWdwsmlwkripl 367
Cdd:cd04186   70 IREAK-GDYVLLLNPDTVVEPGALLELLDAAEQD--------------PDV---------------GIV----------- 108

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784709 368 shkekakrkhktepyrSPAMAGGLFAIEKDFFFELGLYDPGLQIWGgENFEISYKIWQCGGKLLFVPCSRVGH 440
Cdd:cd04186  109 ----------------GPKVSGAFLLVRREVFEEVGGFDEDFFLYY-EDVDLCLRARLAGYRVLYVPQAVIYH 164
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 211-324 5.26e-04

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: 41.89  E-value: 5.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 211 VVIVFHNEGwSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEhlKEKLDEYIKLWNGL-VKVFRNERREGLIQARSI--G 287
Cdd:cd04192    1 VVIAARNEA-ENLPRLLQSLSALDYPKEKFEVILVDDHSTDG--TVQILEFAAAKPNFqLKILNNSRVSISGKKNALttA 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 269784709 288 AQKAKlGQVLIYLDAHCEVAVNWYAPLVAPISKDRAT 324
Cdd:cd04192   78 IKAAK-GDWIVTTDADCVVPSNWLLTFVAFIQKEQIG 113
beta-trefoil_Ricin_LY75 cd23411
ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and ...
 567-649 5.95e-04

ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and similar proteins; Ly-75, also called C-type lectin domain family 13 member B, DEC-205, gp200-MR6, or CD205, 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. Ly-75 contains 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.


Pssm-ID: 467789  Cd Length: 116  Bit Score: 40.11  E-value: 5.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 567 GNQLFRINEANqlmqYDQCLTkgPDGSKVMITHCN-LNEFKEWQYFkSLHRFTHITSGKCL--DRSEVLHQVFISTCDSS 643
Cdd:cd23411    1 GNDIFTIQHEN----SGKCLK--VENSQISAVDCKqSSESLQWKWV-SEHRLFNLGSKQCLglDITKPSNTLKMFECDSK 73


                 ....*.
gi 269784709 644 KMTQKW 649
Cdd:cd23411   74 SVMLWW 79
beta-trefoil_Ricin_GALNT6 cd23470
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 534-649 8.87e-04

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: 39.85  E-value: 8.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 534 WGEIRGLETAYCIDsMGKTNGGFVEL--GPCHRMGGNQLF--------RINEANQL--------MQYDQCLTKGPDgskv 595
Cdd:cd23470    4 YGAIKNEGTNQCLD-VGENNRGGKPLimYSCHGMGGNQYFeytthkelRHNIAKQLclrvskgpVQLGECHYKGKN---- 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 269784709 596 miTHCNLNEfkEWQyFKSLHRFTHITSGKCLD-RSEvlhQVFISTCDSSKMTQKW 649
Cdd:cd23470   79 --SQVPPDE--EWE-LTQDHLIRNSGSNMCLTaRGK---HPAMAPCNPADPHQLW 125
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 535-649 1.79e-03

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: 38.85  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784709 535 GEIRGLETAYCID--SMGKTNGGFVELGPCHRmGGNQLFRINEANQLMQYDQCLT-KGP---DGSKVMITHCNLNEFKEW 608
Cdd:cd23451    3 GPVRLANAGKCLDvpGSSTADGNPVQIYTCNG-TAAQKWTLGTDGTLRVLGKCLDvSGGgtaNGTLVQLWDCNGTGAQKW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 269784709 609 QYFKSlHRFTHITSGKCLDRSEVLH----QVFISTCDSSKmTQKW 649
Cdd:cd23451   82 VPRAD-GTLYNPQSGKCLDAPGGSTtdgtQLQLYTCNGTA-AQQW 124
 
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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