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Conserved domains on  [gi|24584318|ref|NP_652069|]
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polypeptide N-acetylgalactosaminyltransferase 35A [Drosophila melanogaster]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase( domain architecture ID 11551840)

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 ...
 151-450 1.86e-177

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: 505.20  E-value: 1.86e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 151 SIVMCFYNEHKMTLMRSIKTVLERTPSYLLREIILVDDHSDLPELEFHLhgDLRARLKYDNLRYIKNEQREGLIRSRVIG 230
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLL--EEYYKKYLPKVKVLRLKKREGLIRARIAG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 231 AREAVGDVLVFLDSHIEVNQQWLEPLLRLIKSENATLAVPVIDLINADTFEYTPSP-LVRGGFNWGLHFRWENLPEGTlK 309
Cdd:cd02510  79 ARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEE-R 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 310 VPEDFRGPFRSPTMAGGLFAVNRKYFQHLGEYDMAMDIWGGENIEISFRAWQCGGAIKIVPCSRVGHIFR-KRRPYTSPD 388
Cdd:cd02510 158 RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPG 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584318 389 GANTMLKNSLRLAHVWMDQYKDYYLKHEKVPKTYDYGDISDRLKLRERLQCRDFAWYLKNVY 450
Cdd:cd02510 238 GSGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 478-609 1.09e-37

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: 135.97  E-value: 1.09e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 478 NYVDTFQLRLTGTELCaaVVAPKvkGFWKKGSSLQLQTCRRT-PNQLWYETEKAEIVLDKLLCLEASGD--AQVTVNKCH 554
Cdd:cd23440   1 KVIRKGQLKHAGSGLC--LVAED--EVSQKGSLLVLRPCSRNdKKQLWYYTEDGELRLANLLCLDSSETssDFPRLMKCH 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24584318 555 EMLGDQQWRHTRnaNSPVYNMAKGTCLRAAAPTTGALISLDLCSKSngAGGSWDI 609
Cdd:cd23440  77 GSGGSQQWRFKK--DNRLYNPASGQCLAASKNGTSGYVTMDICSDS--PSQKWVF 127
 
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 ...
 151-450 1.86e-177

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: 505.20  E-value: 1.86e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 151 SIVMCFYNEHKMTLMRSIKTVLERTPSYLLREIILVDDHSDLPELEFHLhgDLRARLKYDNLRYIKNEQREGLIRSRVIG 230
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLL--EEYYKKYLPKVKVLRLKKREGLIRARIAG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 231 AREAVGDVLVFLDSHIEVNQQWLEPLLRLIKSENATLAVPVIDLINADTFEYTPSP-LVRGGFNWGLHFRWENLPEGTlK 309
Cdd:cd02510  79 ARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEE-R 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 310 VPEDFRGPFRSPTMAGGLFAVNRKYFQHLGEYDMAMDIWGGENIEISFRAWQCGGAIKIVPCSRVGHIFR-KRRPYTSPD 388
Cdd:cd02510 158 RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPG 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584318 389 GANTMLKNSLRLAHVWMDQYKDYYLKHEKVPKTYDYGDISDRLKLRERLQCRDFAWYLKNVY 450
Cdd:cd02510 238 GSGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 478-609 1.09e-37

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: 135.97  E-value: 1.09e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 478 NYVDTFQLRLTGTELCaaVVAPKvkGFWKKGSSLQLQTCRRT-PNQLWYETEKAEIVLDKLLCLEASGD--AQVTVNKCH 554
Cdd:cd23440   1 KVIRKGQLKHAGSGLC--LVAED--EVSQKGSLLVLRPCSRNdKKQLWYYTEDGELRLANLLCLDSSETssDFPRLMKCH 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24584318 555 EMLGDQQWRHTRnaNSPVYNMAKGTCLRAAAPTTGALISLDLCSKSngAGGSWDI 609
Cdd:cd23440  77 GSGGSQQWRFKK--DNRLYNPASGQCLAASKNGTSGYVTMDICSDS--PSQKWVF 127
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 151-333 1.86e-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: 114.41  E-value: 1.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318   151 SIVMCFYNEHKmTLMRSIKTVLERTpsYLLREIILVDDHSDLPELEFHLhgdlRARLKYDNLRYIKNEQREGLIRSRVIG 230
Cdd:pfam00535   1 SVIIPTYNEEK-YLLETLESLLNQT--YPNFEIIVVDDGSTDGTVEIAE----EYAKKDPRVRVIRLPENRGKAGARNAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318   231 AREAVGDVLVFLDSHIEVNQQWLEPLLRLIKSENATLAVPVIDLINADTFEYTpsplvrggfnWGLHFRWENLPEGTLKV 310
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR----------RASRITLSRLPFFLGLR 143

                         170       180
                  ....*....|....*....|...
gi 24584318   311 PEDFRGPFRSPTMAGGLFAVNRK 333
Cdd:pfam00535 144 LLGLNLPFLIGGFALYRREALEE 166
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
148-413 4.20e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 77.34  E-value: 4.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 148 PQASIVMCFYNEHKMtLMRSIKTVLERTpsYLLREIILVDDHSDLPELEFhlhgdLRArLKYDNLRYIKNEQREGLIRSR 227
Cdd:COG1216   3 PKVSVVIPTYNRPEL-LRRCLESLLAQT--YPPFEVIVVDNGSTDGTAEL-----LAA-LAFPRVRVIRNPENLGFAAAR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 228 VIGAREAVGDVLVFLDSHIEVNQQWLEPLLRliksenatlavpvidlinadtfeytpsplvrggfnwglhfrwenlpegt 307
Cdd:COG1216  74 NLGLRAAGGDYLLFLDDDTVVEPDWLERLLA------------------------------------------------- 104

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 308 lkvpedfrgpfrsptmAGGLFaVNRKYFQHLGEYDMAMDIWGGEnIEISFRAWQCGGAIKIVPCSRVGHIFRKRRpyTSP 387
Cdd:COG1216 105 ----------------AACLL-IRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASS--GPL 164

                       250       260
                ....*....|....*....|....*.
gi 24584318 388 DGANTMLKNSLRLAHVWMDQYKDYYL 413
Cdd:COG1216 165 LRAYYLGRNRLLFLRKHGPRPLLRLA 190
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 489-610 7.68e-15

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 71.00  E-value: 7.68e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318    489 GTELCAAVVAPKvkgfwkkgSSLQLQTCRRT-PNQLWYETEKAEI-VLDKLLCLEASGDA--QVTVNKCHEMLGDQQWRH 564
Cdd:smart00458   5 NTGKCLDVNGNK--------NPVGLFDCHGTgGNQLWKLTSDGAIrIKDTDLCLTANGNTgsTVTLYSCDGTNDNQYWEV 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 24584318    565 trNANSPVYNMAKGTCLRAAAPTTGALISLDLCskSNGAGGSWDIV 610
Cdd:smart00458  77 --NKDGTIRNPDSGKCLDVKDGNTGTKVILWTC--SGNPNQKWIFE 118
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
506-590 3.48e-08

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 52.15  E-value: 3.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318   506 KKGSSLQLQTCRRT-PNQLWYETEKAEI-VLDKLLCLEASGDA---QVTVNKCHEMLGDQQWRHTRNANSpVYNMAKGTC 580
Cdd:pfam00652  21 SAGGPVGLYPCHGSnGNQLWTLTGDGTIrSVASDLCLDVGSTAdgaKVVLWPCHPGNGNQRWRYDEDGTQ-IRNPQSGKC 99

                          90
                  ....*....|
gi 24584318   581 LRAAAPTTGA 590
Cdd:pfam00652 100 LDVSGAGTSN 109
 
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 ...
 151-450 1.86e-177

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: 505.20  E-value: 1.86e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 151 SIVMCFYNEHKMTLMRSIKTVLERTPSYLLREIILVDDHSDLPELEFHLhgDLRARLKYDNLRYIKNEQREGLIRSRVIG 230
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLL--EEYYKKYLPKVKVLRLKKREGLIRARIAG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 231 AREAVGDVLVFLDSHIEVNQQWLEPLLRLIKSENATLAVPVIDLINADTFEYTPSP-LVRGGFNWGLHFRWENLPEGTlK 309
Cdd:cd02510  79 ARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEE-R 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 310 VPEDFRGPFRSPTMAGGLFAVNRKYFQHLGEYDMAMDIWGGENIEISFRAWQCGGAIKIVPCSRVGHIFR-KRRPYTSPD 388
Cdd:cd02510 158 RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPG 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584318 389 GANTMLKNSLRLAHVWMDQYKDYYLKHEKVPKTYDYGDISDRLKLRERLQCRDFAWYLKNVY 450
Cdd:cd02510 238 GSGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 478-609 1.09e-37

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: 135.97  E-value: 1.09e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 478 NYVDTFQLRLTGTELCaaVVAPKvkGFWKKGSSLQLQTCRRT-PNQLWYETEKAEIVLDKLLCLEASGD--AQVTVNKCH 554
Cdd:cd23440   1 KVIRKGQLKHAGSGLC--LVAED--EVSQKGSLLVLRPCSRNdKKQLWYYTEDGELRLANLLCLDSSETssDFPRLMKCH 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24584318 555 EMLGDQQWRHTRnaNSPVYNMAKGTCLRAAAPTTGALISLDLCSKSngAGGSWDI 609
Cdd:cd23440  77 GSGGSQQWRFKK--DNRLYNPASGQCLAASKNGTSGYVTMDICSDS--PSQKWVF 127
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 151-333 1.86e-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: 114.41  E-value: 1.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318   151 SIVMCFYNEHKmTLMRSIKTVLERTpsYLLREIILVDDHSDLPELEFHLhgdlRARLKYDNLRYIKNEQREGLIRSRVIG 230
Cdd:pfam00535   1 SVIIPTYNEEK-YLLETLESLLNQT--YPNFEIIVVDDGSTDGTVEIAE----EYAKKDPRVRVIRLPENRGKAGARNAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318   231 AREAVGDVLVFLDSHIEVNQQWLEPLLRLIKSENATLAVPVIDLINADTFEYTpsplvrggfnWGLHFRWENLPEGTLKV 310
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR----------RASRITLSRLPFFLGLR 143

                         170       180
                  ....*....|....*....|...
gi 24584318   311 PEDFRGPFRSPTMAGGLFAVNRK 333
Cdd:pfam00535 144 LLGLNLPFLIGGFALYRREALEE 166
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
148-413 4.20e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 77.34  E-value: 4.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 148 PQASIVMCFYNEHKMtLMRSIKTVLERTpsYLLREIILVDDHSDLPELEFhlhgdLRArLKYDNLRYIKNEQREGLIRSR 227
Cdd:COG1216   3 PKVSVVIPTYNRPEL-LRRCLESLLAQT--YPPFEVIVVDNGSTDGTAEL-----LAA-LAFPRVRVIRNPENLGFAAAR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 228 VIGAREAVGDVLVFLDSHIEVNQQWLEPLLRliksenatlavpvidlinadtfeytpsplvrggfnwglhfrwenlpegt 307
Cdd:COG1216  74 NLGLRAAGGDYLLFLDDDTVVEPDWLERLLA------------------------------------------------- 104

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 308 lkvpedfrgpfrsptmAGGLFaVNRKYFQHLGEYDMAMDIWGGEnIEISFRAWQCGGAIKIVPCSRVGHIFRKRRpyTSP 387
Cdd:COG1216 105 ----------------AACLL-IRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASS--GPL 164

                       250       260
                ....*....|....*....|....*.
gi 24584318 388 DGANTMLKNSLRLAHVWMDQYKDYYL 413
Cdd:COG1216 165 LRAYYLGRNRLLFLRKHGPRPLLRLA 190
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 489-610 7.68e-15

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 71.00  E-value: 7.68e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318    489 GTELCAAVVAPKvkgfwkkgSSLQLQTCRRT-PNQLWYETEKAEI-VLDKLLCLEASGDA--QVTVNKCHEMLGDQQWRH 564
Cdd:smart00458   5 NTGKCLDVNGNK--------NPVGLFDCHGTgGNQLWKLTSDGAIrIKDTDLCLTANGNTgsTVTLYSCDGTNDNQYWEV 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 24584318    565 trNANSPVYNMAKGTCLRAAAPTTGALISLDLCskSNGAGGSWDIV 610
Cdd:smart00458  77 --NKDGTIRNPDSGKCLDVKDGNTGTKVILWTC--SGNPNQKWIFE 118
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 148-370 5.50e-13

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 68.19  E-value: 5.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 148 PQASIVMCFYNEHKmTLMRSIKTVLERTPSYLlrEIILVDDHSD---LPELEfhlhgdlRARLKYDNLRYIKNEQREGLI 224
Cdd:COG0463   2 PLVSVVIPTYNEEE-YLEEALESLLAQTYPDF--EIIVVDDGSTdgtAEILR-------ELAAKDPRIRVIRLERNRGKG 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 225 RSRVIGAREAVGDVLVFLDSHIEVNQQWLEPLLRLIKSENAtlavpviDLINADTFEYTPSPLVRGGFNWGLHFRwenlp 304
Cdd:COG0463  72 AARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPA-------DLVYGSRLIREGESDLRRLGSRLFNLV----- 139

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24584318 305 egtlkvpedfRGPFRSPTMAGGLFAVNRKYFQHLGeYDMAMdiwgGENIEIsFRAWQCGGAIKIVP 370
Cdd:COG0463 140 ----------RLLTNLPDSTSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVP 189
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 143-265 1.17e-12

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: 69.00  E-value: 1.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 143 EAENLPQASIVMCFYNEHKMtLMRSIKTVLERTPSYLLREIILVDDHSDlPELEFHLHgdlRARLKYDNLRYIKNEQREG 222
Cdd:COG1215  24 APADLPRVSVIIPAYNEEAV-IEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIAR---ELAAEYPRVRVIERPENGG 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 24584318 223 LIRSRVIGAREAVGDVLVFLDSHIEVNQQWLEPLLRLIKSENA 265
Cdd:COG1215  99 KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGV 141
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 152-301 2.35e-12

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: 65.22  E-value: 2.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 152 IVMCFYNEhKMTLMRSIKTVLERTPSYLlrEIILVDDHSDLPELEFHLhgdlRARLKYDNLRYIKNEQREGLIRSRVIGA 231
Cdd:cd00761   1 VIIPAYNE-EPYLERCLESLLAQTYPNF--EVIVVDDGSTDGTLEILE----EYAKKDPRVIRVINEENQGLAAARNAGL 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584318 232 REAVGDVLVFLDSHIEVNQQWLEPLL-RLIKSENATLAVPVIdlinadTFEYTPSPLVRGGFNWGLHFRWE 301
Cdd:cd00761  74 KAARGEYILFLDADDLLLPDWLERLVaELLADPEADAVGGPG------NLLFRRELLEEIGGFDEALLSGE 138
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 484-581 1.79e-11

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: 61.61  E-value: 1.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 484 QLRLTGTELCaaVVAPKVKGFWKKgsSLQLQTCRRT-PNQLWYETEKAEIVLDKLlCLE-ASGDAQVTVNKCHEMLGDQQ 561
Cdd:cd23462   7 EIRNLAGKLC--LDAPGRKKELNK--PVGLYPCHGQgGNQYWMLTKDGEIRRDDL-CLDyAGGSGDVTLYPCHGMKGNQF 81

                        90       100
                ....*....|....*....|
gi 24584318 562 WRHTRNANSpVYNMAKGTCL 581
Cdd:cd23462  82 WIYDEETKQ-IVHGTSKKCL 100
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 151-376 2.75e-10

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: 61.09  E-value: 2.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 151 SIVMCFYNEHKmTLMRSIKTVLERTPSYLLREIILVDDHSDLPELEfhLHGDLRARlkYDNLRYIKNEQReglIRS--RV 228
Cdd:cd02525   3 SIIIPVRNEEK-YIEELLESLLNQSYPKDLIEIIVVDGGSTDGTRE--IVQEYAAK--DPRIRLIDNPKR---IQSagLN 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 229 IGAREAVGDVLVFLDSHIEVNQQWLEPLLRLIKSENATLAVPVIDLInadtfeytpsplVRGGFNWGLHFRwENLPEGTL 308
Cdd:cd02525  75 IGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETI------------GESKFQKAIAVA-QSSPLGSG 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584318 309 KVPedFRGPFRS----PTMAGGLFavNRKYFQHLGEYDMAMDIwgGENIEISFRAWQCGGAIKIVPCSRVGH 376
Cdd:cd02525 142 GSA--YRGGAVKigyvDTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYY 207
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 484-602 1.20e-08

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: 53.47  E-value: 1.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 484 QLRLTGTELCAAVVAPKvkgfwkKGSSLQLQTCR-RTPNQLWYETEKAEIVLDKLlCLEAS-GDAQVTVNKCHEMLGDQQ 561
Cdd:cd23433   8 EIRNVETNLCLDTMGRK------AGEKVGLSSCHgQGGNQVFSYTAKGEIRSDDL-CLDASrKGGPVKLEKCHGMGGNQE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 24584318 562 WRHTRNANS--PVYNmakGTCLRAAAPTTGALISLDLCSKSNG 602
Cdd:cd23433  81 WEYDKETKQirHVNS---GLCLTAPNEDDPNEPVLRPCDGGPS 120
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
506-590 3.48e-08

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 52.15  E-value: 3.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318   506 KKGSSLQLQTCRRT-PNQLWYETEKAEI-VLDKLLCLEASGDA---QVTVNKCHEMLGDQQWRHTRNANSpVYNMAKGTC 580
Cdd:pfam00652  21 SAGGPVGLYPCHGSnGNQLWTLTGDGTIrSVASDLCLDVGSTAdgaKVVLWPCHPGNGNQRWRYDEDGTQ-IRNPQSGKC 99

                          90
                  ....*....|
gi 24584318   581 LRAAAPTTGA 590
Cdd:pfam00652 100 LDVSGAGTSN 109
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 151-358 8.28e-07

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 51.12  E-value: 8.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318   151 SIVMCFYNEHKMTLMRsiKTVLERTPSYLLR-EIILVDDHSDLPELEfhlhgDLRARLKYDNLRYIKNEQRE--GLIRSR 227
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQ--ERILNQTFQYDPEfELIIINDGSTDKTLE-----EVSSIKDHNLQVYYPNAPDTtySLAASR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318   228 VIGAREAVGDVLVFLDSHIEVNQQWLEPLLRLIKSE------NATLAVPVIDLINADTfeytpSPLVRGGFnwglhFRWE 301
Cdd:pfam10111  74 NRGTSHAIGEYISFIDGDCLWSPDKFEKQLKIATSLalqeniQAAVVLPVTDLNDESS-----NFLRRGGD-----LTAS 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24584318   302 NLPEGTLKVPEDFRGPFRSPTmaGGLFAVNRKYFQHLGEYDMAMDIWGGENIEISFR 358
Cdd:pfam10111 144 GDVLRDLLVFYSPLAIFFAPN--SSNALINRQAFIEVGGFDESFRGHGAEDFDIFLR 198
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
484-562 9.69e-07

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 48.30  E-value: 9.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318   484 QLRLTGTELCAAVvapkvkGFWKKGSSLQLQTCRR-TPNQLWYETEKAEIVLDKL--LCLEASG----DAQVTVNKCHEM 556
Cdd:pfam00652  47 TIRSVASDLCLDV------GSTADGAKVVLWPCHPgNGNQRWRYDEDGTQIRNPQsgKCLDVSGagtsNGKVILWTCDSG 120


                  ....*.
gi 24584318   557 LGDQQW 562
Cdd:pfam00652 121 NPNQQW 126
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 484-586 1.86e-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: 1.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 484 QLRLTGTELCAAVVAPKvkgfwKKGSSLQLQTCR-RTPNQLWYETEKAEIVLDKLlCLEASGDAQVTVNKCHEMLGDQQW 562
Cdd:cd23460   4 QIKHTESGLCLDWAGES-----NGDKTVALKPCHgGGGNQFWMYTGDGQIRQDHL-CLTADEGNKVTLRECADQLPSQEW 77

                        90       100
                ....*....|....*....|....
gi 24584318 563 RHTRNaNSPVYNMAKGTCLRAAAP 586
Cdd:cd23460  78 SYDEK-TGTIRHRSTGLCLTLDAN 100
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 152-350 4.27e-06

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: 47.57  E-value: 4.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 152 IVMCFYNEHKmtlmrSIKTVLERTPSYLLR----EIILVDDHSDlpelefhlhgD------LRARLKYDNLRYIKNEQRE 221
Cdd:cd04179   1 VVIPAYNEEE-----NIPELVERLLAVLEEgydyEIIVVDDGST----------DgtaeiaRELAARVPRVRVIRLSRNF 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 222 GLIRSRVIGAREAVGDVLVFLDS----HIEVnqqwLEPLLRLIKSENAtlavpviDLINAdtfeytpSPLVRGG-FNWGL 296
Cdd:cd04179  66 GKGAAVRAGFKAARGDIVVTMDAdlqhPPED----IPKLLEKLLEGGA-------DVVIG-------SRFVRGGgAGMPL 127

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24584318 297 HFRWENlpegtlKVpedFRGPFRS------PTMAGGLFAVNRKYFQHLGE------YDMAMDIWGG 350
Cdd:cd04179 128 LRRLGS------RL---FNFLIRLllgvriSDTQSGFRLFRREVLEALLSllesngFEFGLELLVG 184
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 152-376 7.58e-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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 46.40  E-value: 7.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 152 IVMCFYNEHKMTLmRSIKTVLERTPSYLlrEIILVDDHSDLPELEFhlhgdlrARLKYDNLRYIKNEQREGLIRSRVIGA 231
Cdd:cd04186   1 IIIVNYNSLEYLK-ACLDSLLAQTYPDF--EVIVVDNASTDGSVEL-------LRELFPEVRLIRNGENLGFGAGNNQGI 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 232 REAVGDVLVFLDSHIEVNQQWLEPLLRLIKSENATLAVpvidlinadtfeytpSPLVRGGFnwgLHFRWenlpegtlkvp 311
Cdd:cd04186  71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIV---------------GPKVSGAF---LLVRR----------- 121

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584318 312 EDFRgpfrsptmAGGLFavNRKYFQHlgeydmamdiwgGENIEISFRAWQCGGAIKIVPCSRVGH 376
Cdd:cd04186 122 EVFE--------EVGGF--DEDFFLY------------YEDVDLCLRARLAGYRVLYVPQAVIYH 164
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 484-562 2.43e-05

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: 43.93  E-value: 2.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 484 QLRLTGteLCAAVVAPKvkgfwkKGSSLQLQTCRRTPNQLWYETEKAeIVLDKL-LCLEASGDAQVTVNKCHEMLGDQQW 562
Cdd:cd23441  49 QLQTQG--LCLTVDSSS------KDLPVVLETCSDDPKQKWTRTGRQ-LVHSESgLCLDSRKKKGLVVSPCRSGAPSQKW 119
beta-trefoil_Ricin_RIPs_II_rpt2 cd23444
second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ...
 532-602 2.52e-05

second 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 second ricin B-type lectin domain. Members of this family 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: 467322 [Multi-domain]  Cd Length: 122  Bit Score: 44.18  E-value: 2.52e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24584318 532 IVLDKLLCLEASGDAQVTVNKCHEMLGDQQWRhtrnanspVY-------NMAKGTCLRAAAPTTGALISLDLCSKSNG 602
Cdd:cd23444   6 IVGLNDLCLQANGGNNVWLEECVSNKKEQKWA--------LYpdgtirpNQNRNLCLTSSSDVQGSIIVVLSCSGSSG 75
beta-trefoil_Ricin_EW29-like cd23449
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ...
 521-563 2.62e-05

ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa galactose-binding lectin (EW29) and similar proteins; EW29 is a galactose-binding lectin from the earthworm Lumbricus terrestris. It contains 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 second ricin B-type lectin domain may harbor two sugar-binding pockets in subdomains alpha and gamma. EW29 uses these two sugar-binding sites for its function as a single domain-type hemagglutinin.


Pssm-ID: 467327 [Multi-domain]  Cd Length: 128  Bit Score: 44.20  E-value: 2.62e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24584318 521 NQLWYETEKAEIVLDKL--LCLEASGDAQVTVNKCHEMLGDQQWR 563
Cdd:cd23449  39 NQLWYEDEVTGTIRSKLndFCLDASGDKGLILNPYDPSNPKQQWK 83
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
538-603 3.16e-05

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 43.67  E-value: 3.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318   538 LCLEASG----DAQVTVNKCHEMLGDQQWRHTRNANspVYNMAKGTCLRAAAPTTGALISLDLCSKSNGA 603
Cdd:pfam00652  12 KCLDVPGgssaGGPVGLYPCHGSNGNQLWTLTGDGT--IRSVASDLCLDVGSTADGAKVVLWPCHPGNGN 79
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 513-585 8.51e-05

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket.


Pssm-ID: 467294 [Multi-domain]  Cd Length: 120  Bit Score: 42.42  E-value: 8.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 513 LQTCRRTPNQLWYETEKAEIVlDKL------LCLEASGDAQVTVNKCHEMlGDQQWRHTRNANSPV--YNMAKGTCLRAA 584
Cdd:cd23415  24 TGPCNGGPYQRWTWSGVGDGT-VTLrnaatgRCLDSNGNGGVYTLPCNGG-SYQRWRVTSTSGGGVtlRNVATGRCLDSN 101


                .
gi 24584318 585 A 585
Cdd:cd23415 102 G 102
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 484-600 8.73e-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: 42.70  E-value: 8.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 484 QLRLTGTELCAAVVAPKVKGfwkkGSSLQLQTCRRTP-NQLWYETEKAEIVLD--KLLCLEASGDAQVTVNKCHE----M 556
Cdd:cd23435   6 ALRNKGSELCLDVNNPNGQG----GKPVIMYGCHGLGgNQYFEYTSKGEIRHNigKELCLHASGSDEVILQHCTSkgkdV 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 24584318 557 LGDQQWRHTRNANspVYNMAKGTCLRAAapttGALISLDLCSKS 600
Cdd:cd23435  82 PPEQKWLFTQDGT--IRNPASGLCLHAS----GYKVLLRTCNPS 119
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 312-378 1.06e-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: 41.06  E-value: 1.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584318   312 EDFRGPFRSPTMAGGLFAVNRKYFQHLGEYDMAMDIWGGENIEISFRAWQCGGAIKIVPCsRVGHIF 378
Cdd:pfam02709   8 DKFGYKLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG-DIGRYY 73
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 152-272 1.12e-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: 43.82  E-value: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 152 IVMCFYNEHKmTLMRSIKTVLERTPSYLLREIILVDDHS-----DLpeLEF-HLHGDLrarlkydNLRYIKNEQREGLIR 225
Cdd:cd04192   1 VVIAARNEAE-NLPRLLQSLSALDYPKEKFEVILVDDHStdgtvQI--LEFaAAKPNF-------QLKILNNSRVSISGK 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 24584318 226 SRVI--GAREAVGDVLVFLDSHIEVNQQWLEPLLRLIKSENATL-AVPVI 272
Cdd:cd04192  71 KNALttAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLvAGPVI 120
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 482-601 1.14e-04

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 42.36  E-value: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 482 TFQLRLTGTELCAAVVApkvkGFWKKGSSLQLQTCRRTPNQLWYETEKA----EIVLDKL-LCLEASGD-----AQVTVN 551
Cdd:cd00161   2 TYRIVNAASGKCLDVAG----GSTANGAPVQQWTCNGGANQQWTLTPVGdgyyTIRNVASgKCLDVAGGstangANVQQW 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 24584318 552 KCHEmLGDQQWRHTRNANSPVY--NMAKGTCL--RAAAPTTGALISLDLCSKSN 601
Cdd:cd00161  78 TCNG-GDNQQWRLEPVGDGYYRivNKHSGKCLdvSGGSTANGANVQQWTCNGGA 130
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 483-562 1.56e-04

ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467334 [Multi-domain]  Cd Length: 122  Bit Score: 41.57  E-value: 1.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 483 FQLRLTGTELCAAVvapkvKGFWKKGSSLQLQTCRRTPNQLWYETEKAEI--VLDKLLCLEASG----DAQVTVNKCHEM 556
Cdd:cd23456   3 FQLKSQASGLCLDV-----SGGATNGANVVVYDCNNSNSQKWYYDATGRLhsKANPGKCLDAGGensnGANVVLWACNDS 77


                ....*.
gi 24584318 557 lGDQQW 562
Cdd:cd23456  78 -ANQRW 82
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 508-594 2.23e-04

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: 41.57  E-value: 2.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 508 GSSLQLQTCRRTPNQLWYETEKAEIVLDKLLCLEASG-----DAQVTVNKCHEMlGDQQWRHtrNANSPVYNMAKGTCLR 582
Cdd:cd23418  27 GTRLILWDCHGGANQQFTFTSAGELRVGGDKCLDAAGggttnGTPVVIWPCNGG-ANQKWRF--NSDGTIRNVNSGLCLD 103

                        90
                ....*....|....
gi 24584318 583 AA--APTTGALISL 594
Cdd:cd23418 104 VAggGTANGTRLIL 117
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 486-563 1.98e-03

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: 38.46  E-value: 1.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 486 RLTGTELCAAVVAPKvkgfwkKGSSLQLQTCRRTP-NQLWYETEKAEIV--LDKLLCLEASGDAQ--VTVNKCHEMLGDQ 560
Cdd:cd23434  44 QIKHDDLCLTVVDRA------PGSLVTLQPCREDDsNQKWEQIENNSKLrhVGSNLCLDSRNAKSggLTVETCDPSSGSQ 117


                ...
gi 24584318 561 QWR 563
Cdd:cd23434 118 QWK 120
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 484-581 3.25e-03

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: 38.40  E-value: 3.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 484 QLRLTGTELCAavvapKVKGFwKKGSSLQLQTCRRTPNQLWYETEK------------AEIVLDKLLCLEA-SGDAQVTV 550
Cdd:cd23476   9 EIRNVGTGLCA-----DTKHG-ALGSPLRLEGCVKGRGEAAWNNGQvftfgwredirpGDPQHTKKFCFDAiSHNSPVTL 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 24584318 551 NKCHEMLGDQQWRHTRNANspVYNMAKGTCL 581
Cdd:cd23476  83 YDCHGMKGNQLWRYRKDKT--LYHPVSNSCM 111
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 520-600 5.49e-03

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: 37.68  E-value: 5.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 520 PNQLWYETEKAEIVLDKLlCLEASGDA--QVTVNKCHE-MLGDQQWRHTRNANspVYNMAKGTCLRAAAPTTGALISLDL 596
Cdd:cd23459  43 SNQLFSLSKKGELRREES-CADVQGTEesKVILITCHGlEKFNQKWKHTKGGQ--IVHLASGKCLDAEGLKSGDDVTLAK 119


                ....
gi 24584318 597 CSKS 600
Cdd:cd23459 120 CDGS 123
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 151-246 6.62e-03

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 38.77  E-value: 6.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 151 SIVMCFYNEHKMTLMRSIKTVLERTPSyllrEIILVDDHSDLPELEfhlhgdLRARLKYDNLRYIKNEQREGLIRSRVIG 230
Cdd:cd06434   3 TVIIPVYDEDPDVFRECLRSILRQKPL----EIIVVTDGDDEPYLS------ILSQTVKYGGIFVITVPHPGKRRALAEG 72

                        90
                ....*....|....*.
gi 24584318 231 AREAVGDVLVFLDSHI 246
Cdd:cd06434  73 IRHVTTDIVVLLDSDT 88
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 157-269 8.34e-03

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


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 37.59  E-value: 8.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584318 157 YNEHKmTLMRSIKTVLERTpsYLLREIILVDDHSDLPELEFhlhGDLRARLKYDNLRYIKNEQREGliRSRVI--GAREA 234
Cdd:cd06423   6 YNEEA-VIERTIESLLALD--YPKLEVIVVDDGSTDDTLEI---LEELAALYIRRVLVVRDKENGG--KAGALnaGLRHA 77

                        90       100       110
                ....*....|....*....|....*....|....*
gi 24584318 235 VGDVLVFLDSHIEVNQQWLEPLLRLIKSENATLAV 269
Cdd:cd06423  78 KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAV 112
 
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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