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Conserved domains on  [gi|326669672|ref|XP_003199061|]
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polypeptide N-acetylgalactosaminyltransferase 18 isoform X1 [Danio rerio]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase( domain architecture ID 10118412)

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 ...
 159-460 8.38e-152

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: 438.95  E-value: 8.38e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 159 SIVFIFVNEALSVILRSIHSVMNRTPSHLLKEIILVDDNSNNDELKEKLQDFVKetnaKQPGFIKVVRHSRQEGLIRSRV 238
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYK----KYLPKVKVLRLKKREGLIRARI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 239 SGWRAASAPVVALFDAHVEFNIGWAEPILQRIKEDRTRIISPSFDNIKYDTFEIEEYPLSAQG-FDWELWCRYLNPPKSW 317
Cdd:cd02510   77 AGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGgFDWSLHFKWLPLPEEE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 318 WNLNNSTAPIRSPALIGC-FVVDRLYFAEIGLLDEGMEIYGGENVELGVRVWQCGGSVEVLPCARIAHIER-AHKPYTED 395
Cdd:cd02510  157 RRRESPTAPIRSPTMAGGlFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFP 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 326669672 396 LTAH-VRRNALRVAEVWMDEFKSHVYMAWNIPQedsGIDIGDIAERKALRKKLQCKTFRWYLVNIY 460
Cdd:cd02510  237 GGSGtVLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 463-604 3.86e-102

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


The actual alignment was detected with superfamily member cd23475:

Pssm-ID: 483949  Cd Length: 142  Bit Score: 305.69  E-value: 3.86e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 463 MRMYTDTVAYGVLRNSLKTDLCLDQGPDTDNIPILYLCHGMTPQNVYYTSTQQLFVGILSPTVDDDDNKCLVDVNGRPRL 542
Cdd:cd23475    1 MRMYTDTIAYGVLQNSLKTDLCLDQGPDTDNIPIMYICHGMTPQNVYYTSNQQLHVGILSPTIDDDDNRCLVDVNSRPRL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326669672 543 IECSYAVAKRMKLHWRFTQGGSIQNTKSKRCLELVENNDNEFGFQLTLQKCTGQNWTITNML 604
Cdd:cd23475   81 IECSYAKAKRMKLYWLFTQGGSIQNKKSKRCLELQENADNEFGYQLVLQKCSGQRWTITNVL 142
 
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 ...
 159-460 8.38e-152

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: 438.95  E-value: 8.38e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 159 SIVFIFVNEALSVILRSIHSVMNRTPSHLLKEIILVDDNSNNDELKEKLQDFVKetnaKQPGFIKVVRHSRQEGLIRSRV 238
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYK----KYLPKVKVLRLKKREGLIRARI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 239 SGWRAASAPVVALFDAHVEFNIGWAEPILQRIKEDRTRIISPSFDNIKYDTFEIEEYPLSAQG-FDWELWCRYLNPPKSW 317
Cdd:cd02510   77 AGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGgFDWSLHFKWLPLPEEE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 318 WNLNNSTAPIRSPALIGC-FVVDRLYFAEIGLLDEGMEIYGGENVELGVRVWQCGGSVEVLPCARIAHIER-AHKPYTED 395
Cdd:cd02510  157 RRRESPTAPIRSPTMAGGlFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFP 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 326669672 396 LTAH-VRRNALRVAEVWMDEFKSHVYMAWNIPQedsGIDIGDIAERKALRKKLQCKTFRWYLVNIY 460
Cdd:cd02510  237 GGSGtVLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT18 cd23475
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 463-604 3.86e-102

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 18 (GALNT18) and similar proteins; GALNT18 (EC 2.4.1.41), also called polypeptide GalNAc transferase 18, GalNAc-T18, polypeptide GalNAc transferase-like protein 4, GalNAc-T-like protein 4, pp-GaNTase-like protein 4, polypeptide N-acetylgalactosaminyltransferase-like protein 4, protein-UDP acetylgalactosaminyltransferase-like protein 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT18 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467353  Cd Length: 142  Bit Score: 305.69  E-value: 3.86e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 463 MRMYTDTVAYGVLRNSLKTDLCLDQGPDTDNIPILYLCHGMTPQNVYYTSTQQLFVGILSPTVDDDDNKCLVDVNGRPRL 542
Cdd:cd23475    1 MRMYTDTIAYGVLQNSLKTDLCLDQGPDTDNIPIMYICHGMTPQNVYYTSNQQLHVGILSPTIDDDDNRCLVDVNSRPRL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326669672 543 IECSYAVAKRMKLHWRFTQGGSIQNTKSKRCLELVENNDNEFGFQLTLQKCTGQNWTITNML 604
Cdd:cd23475   81 IECSYAKAKRMKLYWLFTQGGSIQNKKSKRCLELQENADNEFGYQLVLQKCSGQRWTITNVL 142
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 159-292 2.13e-23

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: 97.08  E-value: 2.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672  159 SIVFIFVNEAlSVILRSIHSVMNRTpsHLLKEIILVDDNSNnDELKEKLQDFvketnAKQPGFIKVVRHSRQEGLIRSRV 238
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGST-DGTVEIAEEY-----AKKDPRVRVIRLPENRGKAGARN 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 326669672  239 SGWRAASAPVVALFDAHVEFNIGWAEPILQRIKEDRTRIISPSFDNIKYDTFEI 292
Cdd:pfam00535  72 AGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY 125
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
156-413 9.56e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 70.41  E-value: 9.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 156 PQVSIVFIFVNEAlSVILRSIHSVMNRTPSHLlkEIILVDDNSnNDELKEKLQDFvketnakQPGFIKVVRHSRQEGLIR 235
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGS-TDGTAELLAAL-------AFPRVRVIRNPENLGFAA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 236 SRVSGWRAASAPVVALFDAHVEFNIGWAEPILQRikedrtriispsfdnikydtfeieeyplsaqgfdwelwcrylnppk 315
Cdd:COG1216   72 ARNLGLRAAGGDYLLFLDDDTVVEPDWLERLLAA---------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 316 swwnlnnstapirspaliGCFVVDRLYFAEIGLLDEGMEIYGGEnVELGVRVWQCGGSVEVLPCARIAHIERA-HKPYTE 394
Cdd:COG1216  106 ------------------ACLLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGAsSGPLLR 166

                        250
                 ....*....|....*....
gi 326669672 395 dlTAHVRRNALRVAEVWMD 413
Cdd:COG1216  167 --AYYLGRNRLLFLRKHGP 183
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
471-598 1.18e-13

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 67.94  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672  471 AYGVLRNsLKTDLCLD-QGPDTDNIPI-LYLCHGM-TPQNVYYTSTQQLFVGIlsptvdddDNKCLvDV-----NGRPRL 542
Cdd:pfam00652   1 ATGRIRN-RASGKCLDvPGGSSAGGPVgLYPCHGSnGNQLWTLTGDGTIRSVA--------SDLCL-DVgstadGAKVVL 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326669672  543 IECSYAVAKRmklHWRFTQGGS-IQNTKSKRCLELVENNDNefGFQLTLQKC----TGQNW 598
Cdd:pfam00652  71 WPCHPGNGNQ---RWRYDEDGTqIRNPQSGKCLDVSGAGTS--NGKVILWTCdsgnPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 478-601 1.30e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 47.51  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672   478 SLKTDLCLDQgPDTDNIPILYLCHGMTP-QNVYYTSTQQLFVgilsptvdDDDNKCLvDVNG----RPRLIECSYAVAKr 552
Cdd:smart00458   3 SGNTGKCLDV-NGNKNPVGLFDCHGTGGnQLWKLTSDGAIRI--------KDTDLCL-TANGntgsTVTLYSCDGTNDN- 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 326669672   553 mkLHWRFTQGGSIQNTKSKRCLELVENNdneFGFQLTLQKCTG---QNWTIT 601
Cdd:smart00458  72 --QYWEVNKDGTIRNPDSGKCLDVKDGN---TGTKVILWTCSGnpnQKWIFE 118
 
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 ...
 159-460 8.38e-152

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: 438.95  E-value: 8.38e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 159 SIVFIFVNEALSVILRSIHSVMNRTPSHLLKEIILVDDNSNNDELKEKLQDFVKetnaKQPGFIKVVRHSRQEGLIRSRV 238
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYK----KYLPKVKVLRLKKREGLIRARI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 239 SGWRAASAPVVALFDAHVEFNIGWAEPILQRIKEDRTRIISPSFDNIKYDTFEIEEYPLSAQG-FDWELWCRYLNPPKSW 317
Cdd:cd02510   77 AGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGgFDWSLHFKWLPLPEEE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 318 WNLNNSTAPIRSPALIGC-FVVDRLYFAEIGLLDEGMEIYGGENVELGVRVWQCGGSVEVLPCARIAHIER-AHKPYTED 395
Cdd:cd02510  157 RRRESPTAPIRSPTMAGGlFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFP 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 326669672 396 LTAH-VRRNALRVAEVWMDEFKSHVYMAWNIPQedsGIDIGDIAERKALRKKLQCKTFRWYLVNIY 460
Cdd:cd02510  237 GGSGtVLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT18 cd23475
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 463-604 3.86e-102

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 18 (GALNT18) and similar proteins; GALNT18 (EC 2.4.1.41), also called polypeptide GalNAc transferase 18, GalNAc-T18, polypeptide GalNAc transferase-like protein 4, GalNAc-T-like protein 4, pp-GaNTase-like protein 4, polypeptide N-acetylgalactosaminyltransferase-like protein 4, protein-UDP acetylgalactosaminyltransferase-like protein 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT18 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467353  Cd Length: 142  Bit Score: 305.69  E-value: 3.86e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 463 MRMYTDTVAYGVLRNSLKTDLCLDQGPDTDNIPILYLCHGMTPQNVYYTSTQQLFVGILSPTVDDDDNKCLVDVNGRPRL 542
Cdd:cd23475    1 MRMYTDTIAYGVLQNSLKTDLCLDQGPDTDNIPIMYICHGMTPQNVYYTSNQQLHVGILSPTIDDDDNRCLVDVNSRPRL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326669672 543 IECSYAVAKRMKLHWRFTQGGSIQNTKSKRCLELVENNDNEFGFQLTLQKCTGQNWTITNML 604
Cdd:cd23475   81 IECSYAKAKRMKLYWLFTQGGSIQNKKSKRCLELQENADNEFGYQLVLQKCSGQRWTITNVL 142
beta-trefoil_Ricin_GALNT8-like cd23438
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 468-602 6.95e-66

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8)-like subfamily; The GALNT8-like subfamily includes GALNT8, GALNT9, GALNT17 and GALNT18. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT9 does not glycosylate apomucin or SDC3. Members of this family comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467316  Cd Length: 134  Bit Score: 211.52  E-value: 6.95e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 468 DTVAYGVLRNSLKTDLCLDQGPDTDNIPILYLCHGMTPQNVYYTSTQQLFVGILSPTVdDDDNKCLVDV--NGRPRLIEC 545
Cdd:cd23438    1 NTVAYGEMRNSLVTDLCLDQGPKENHTAILYPCHGWSPQLVRYTKDGQLYLGQLGSTA-SPDTRCLVDDgkSDKPQLLDC 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 326669672 546 SYaVAKRMKLHWRFTQGGSIQNTKSKRCLELVENNDNeFGFQLTLQKCTGQNWTITN 602
Cdd:cd23438   80 SK-VKNRLQKYWDFSQGGAIQNRATGRCLEVEEDKLN-FGHRLVLQTCSGQKWNIKN 134
beta-trefoil_Ricin_GALNT17 cd23474
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 463-604 2.99e-37

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 17 (GALNT17) and similar proteins; GALNT17 (EC 2.4.1.41), also called polypeptide GalNAc transferase-like protein 3, GalNAc-T-like protein 3, pp-GaNTase-like protein 3, protein-UDP acetylgalactosaminyltransferase-like protein 3, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3, or Williams-Beuren syndrome chromosomal region 17 protein, may catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT17 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467352  Cd Length: 142  Bit Score: 135.41  E-value: 2.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 463 MRMYTDTVAYGVLRNSLKTDLCLDQGPDTDNIPILYLCHGMTPQNVYYTSTQQLFVGILSPTVDDDDNKCLVD--VNGRP 540
Cdd:cd23474    1 MRRYNNTVAYGELRNNKAKDVCLDQGPPENHTAILYPCHGWGPQLARYTKEGYLHLGALGTTTLLPDTRCLVDnkKSRFP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 326669672 541 RLIECSYAVAKRMKlHWRFTQGGSIQNTKSKRCLElVENNDNeFGFQLTLQKCTGQNWTITNML 604
Cdd:cd23474   81 QLLDCDKVKSILHK-RWNFIQNGAIMNLGTGRCLE-VENRGN-FGIDLILRSCTGQRWTIKNFI 141
beta-trefoil_Ricin_GALNT9 cd23473
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 463-602 4.73e-36

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 9 (GALNT9) and similar proteins; GALNT9 (EC 2.4.1.41), also called polypeptide GalNAc transferase 9, GalNAc-T9, pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT9 does not glycosylate apomucin or SDC3. GALNT9 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467351  Cd Length: 145  Bit Score: 132.01  E-value: 4.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 463 MRMYTDTVAYGVLRNSLKTDLCLDQGPDTDNIPILYLCHGMTPQNVYYTSTQQLFVGILSPTVDDDDNKCLVDvNGR--- 539
Cdd:cd23473    1 MRIYNNTITYGEVRNSKASGYCLDQGSEEDDKAILYPCHGMSSQLVRYSTEGLLQLGPLGSTAFLPDTKCLVD-DGRgrt 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 326669672 540 PRLIECSyAVAKRMKLHWRFTQGGSIQNTKSKRCLELVENNDNEFGFQLTLQKCTGQNWTITN 602
Cdd:cd23473   80 PTLKKCE-DVARPAQRLWDFTQNGPIISRDTGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRN 141
beta-trefoil_Ricin_GALNT8 cd23472
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 460-604 5.24e-36

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8) and similar proteins; GALNT8 (EC 2.4.1.41), also called polypeptide GalNAc transferase 8, GalNAc-T8, pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8, may catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT8 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467350  Cd Length: 146  Bit Score: 131.86  E-value: 5.24e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 460 YPEMRMYTDTVAYGVLRNSLKTDLCLDQGPDTDNIPILYLCHGMTPQNVYYTSTQQLFVGILSPTVDDDDnKCLVD--VN 537
Cdd:cd23472    1 YPVLMPIQTIVGYGTMKNSLNENICIDQGPVPGNTPIMYGCHGYSPQFVYYHLTGELYVGGLKADIYASD-RCLTDpgEG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326669672 538 GRPRLIECSYAVAKRMKLHWRFTQGGSIQNTKSKRCLELVENNDNEFgFQLTLQKCTGQNWTITNML 604
Cdd:cd23472   80 WKPELVSCQDATLKGLNMYWDFKQGTAIINRKTKRCLEISLDKTPSY-YTLILQTCTGQKWEIQHVL 145
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 159-292 2.13e-23

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: 97.08  E-value: 2.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672  159 SIVFIFVNEAlSVILRSIHSVMNRTpsHLLKEIILVDDNSNnDELKEKLQDFvketnAKQPGFIKVVRHSRQEGLIRSRV 238
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGST-DGTVEIAEEY-----AKKDPRVRVIRLPENRGKAGARN 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 326669672  239 SGWRAASAPVVALFDAHVEFNIGWAEPILQRIKEDRTRIISPSFDNIKYDTFEI 292
Cdd:pfam00535  72 AGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY 125
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
156-413 9.56e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 70.41  E-value: 9.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 156 PQVSIVFIFVNEAlSVILRSIHSVMNRTPSHLlkEIILVDDNSnNDELKEKLQDFvketnakQPGFIKVVRHSRQEGLIR 235
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGS-TDGTAELLAAL-------AFPRVRVIRNPENLGFAA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 236 SRVSGWRAASAPVVALFDAHVEFNIGWAEPILQRikedrtriispsfdnikydtfeieeyplsaqgfdwelwcrylnppk 315
Cdd:COG1216   72 ARNLGLRAAGGDYLLFLDDDTVVEPDWLERLLAA---------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 316 swwnlnnstapirspaliGCFVVDRLYFAEIGLLDEGMEIYGGEnVELGVRVWQCGGSVEVLPCARIAHIERA-HKPYTE 394
Cdd:COG1216  106 ------------------ACLLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGAsSGPLLR 166

                        250
                 ....*....|....*....
gi 326669672 395 dlTAHVRRNALRVAEVWMD 413
Cdd:COG1216  167 --AYYLGRNRLLFLRKHGP 183
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
471-598 1.18e-13

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 67.94  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672  471 AYGVLRNsLKTDLCLD-QGPDTDNIPI-LYLCHGM-TPQNVYYTSTQQLFVGIlsptvdddDNKCLvDV-----NGRPRL 542
Cdd:pfam00652   1 ATGRIRN-RASGKCLDvPGGSSAGGPVgLYPCHGSnGNQLWTLTGDGTIRSVA--------SDLCL-DVgstadGAKVVL 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326669672  543 IECSYAVAKRmklHWRFTQGGS-IQNTKSKRCLELVENNDNefGFQLTLQKC----TGQNW 598
Cdd:pfam00652  71 WPCHPGNGNQ---RWRYDEDGTqIRNPQSGKCLDVSGAGTS--NGKVILWTCdsgnPNQQW 126
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 156-384 4.03e-12

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 65.88  E-value: 4.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 156 PQVSIVFIFVNEAlSVILRSIHSVMNRTPSHLlkEIILVDDNSNnDELKEKLQDFvketnAKQPGFIKVVRHSRQEGLIR 235
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGST-DGTAEILREL-----AAKDPRIRVIRLERNRGKGA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 236 SRVSGWRAASAPVVALFDAHVEFNIGWAEPILQRIKEDRTRIISPSFdniKYDTFEIEEYPLSAQGFDWELWCRYLNPPK 315
Cdd:COG0463   73 ARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSR---LIREGESDLRRLGSRLFNLVRLLTNLPDST 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326669672 316 SwwnlnnstapirspaliGCFVVDRLYFAEIGlLDEGMeiygGENVELgVRVWQCGGSVEVLPCARIAH 384
Cdd:COG0463  150 S-----------------GFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVPVRYRAG 195
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 470-601 1.01e-11

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: 62.35  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 470 VAYGVLRNSLkTDLCLDQGPDTDN---IPILYLCHGMtPQNVY--YTSTQQLFVGILSPtvddddnKCLVDVNGRPRLI- 543
Cdd:cd23435    2 GYYGALRNKG-SELCLDVNNPNGQggkPVIMYGCHGL-GGNQYfeYTSKGEIRHNIGKE-------LCLHASGSDEVILq 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 326669672 544 ECSY---AVAKRMKlhWRFTQGGSIQNTKSKRCLELVenndnefGFQLTLQKCTG----QNWTIT 601
Cdd:cd23435   73 HCTSkgkDVPPEQK--WLFTQDGTIRNPASGLCLHAS-------GYKVLLRTCNPsddsQKWTFI 128
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 152-309 1.38e-11

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 65.92  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 152 PSNLPQVSIVFIFVNEALsVILRSIHSVMNRTPSHLLKEIILVDDNSNnDELKEKLQDFvketnAKQPGFIKVVRHSRQE 231
Cdd:COG1215   25 PADLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIAREL-----AAEYPRVRVIERPENG 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326669672 232 GLIRSRVSGWRAASAPVVALFDAHVEFNIGWAEPILQRIKEDRTRIISPSFdNIKYDTFE-IEEYPLSAQGFDWELWCR 309
Cdd:COG1215   98 GKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGANL-AFRREALEeVGGFDEDTLGEDLDLSLR 175
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 471-601 4.50e-10

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: 57.45  E-value: 4.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 471 AYGVLRNsLKTDLCLD--QGPDTDNIPILYLCHGMTPQNV-YYTSTQQLFvgilsptvddDDNKCLVDVNGRPR-LIECS 546
Cdd:cd23460    1 GLGQIKH-TESGLCLDwaGESNGDKTVALKPCHGGGGNQFwMYTGDGQIR----------QDHLCLTADEGNKVtLRECA 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 547 YAVAKRMklhWRFT-QGGSIQNTKSKRCLELVENNDnefgfQLTLQKCTG----QNWTIT 601
Cdd:cd23460   70 DQLPSQE---WSYDeKTGTIRHRSTGLCLTLDANND-----VVILKECDSnslwQKWIFQ 121
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 468-602 4.61e-10

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: 57.72  E-value: 4.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 468 DTVAYGVLRNSlKTDLCLD--QGPDTDNIPI-LYLCHGM--TPQNVYYTSTQQLfvgilsptvdDDDNKCLvDVNG---- 538
Cdd:cd23459    3 DVLAYGQVRNP-GTNLCLDtlQRDEDKGYNLgLYPCQGGlsSNQLFSLSKKGEL----------RREESCA-DVQGtees 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326669672 539 RPRLIECSYAVAKRMKlhWRFTQGGSIQNTKSKRCLElVENNDNefGFQLTLQKCTG---QNWTITN 602
Cdd:cd23459   71 KVILITCHGLEKFNQK--WKHTKGGQIVHLASGKCLD-AEGLKS--GDDVTLAKCDGslsQKWTFEH 132
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 470-602 2.12e-09

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: 55.76  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 470 VAYGVLRNsLKTDLCLD-QGPDTDNIPILYLCHGM-TPQNVYYTSTQQLFVGilsptvddddNKCLVDV--NGRPRLIEC 545
Cdd:cd23437    3 LAWGEIRN-LGTGLCLDtMGHQNGGPVGLYPCHGMgGNQLFRLNEAGQLAVG----------EQCLTASgsGGKVKLRKC 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326669672 546 SyavaKRMKLHWRFT-QGGSIQNTKSKRCLELVENNDnefgfQLTLQKCTG----QNWTITN 602
Cdd:cd23437   72 N----LGETGKWEYDeATGQIRHKGTGKCLDLNEGTN-----KLILQPCDSsspsQKWEFNE 124
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 160-312 2.26e-09

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: 56.36  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 160 IVFIFVNEAlSVILRSIHSVMNRTPSHLlkEIILVDDNSnNDELKEKLQDFvketnAKQPGFIKVVRHSRQEGLIRSRVS 239
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGS-TDGTLEILEEY-----AKKDPRVIRVINEENQGLAAARNA 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 326669672 240 GWRAASAPVVALFDAHVEFNIGWAEPILQRIKEDRTR--IISPSFDNIKYDTFE---IEEYPLSAQGFDWELWCRYLN 312
Cdd:cd00761   72 GLKAARGEYILFLDADDLLLPDWLERLVAELLADPEAdaVGGPGNLLFRRELLEeigGFDEALLSGEEDDDFLLRLLR 149
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 468-599 3.18e-08

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: 52.37  E-value: 3.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 468 DTVAYGVLRNsLKTDLCLD-QGPDTD--NIPILYLCHGMTP-QNVYYTSTQQLFVgilsptvdddDNKCLvDVNGRP--- 540
Cdd:cd23462    1 EALAYGEIRN-LAGKLCLDaPGRKKElnKPVGLYPCHGQGGnQYWMLTKDGEIRR----------DDLCL-DYAGGSgdv 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 326669672 541 RLIECSYAVAKRMklhWRFT-QGGSIQNTKSKRCLELvenndNEFGFQLTLQKCTG----QNWT 599
Cdd:cd23462   69 TLYPCHGMKGNQF---WIYDeETKQIVHGTSKKCLEL-----SDDSSKLVMEPCNGssprQQWE 124
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 166-254 1.61e-07

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 51.81  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 166 NEA--LSVILRSIHSVMNRTPSHllkEIILVDDNSNnDELKEKLQDFvketnAKQPGFIKVVRHSRQEGLIRSRVSGWRA 243
Cdd:cd04179    7 NEEenIPELVERLLAVLEEGYDY---EIIVVDDGST-DGTAEIAREL-----AARVPRVRVIRLSRNFGKGAAVRAGFKA 77

                         90
                 ....*....|.
gi 326669672 244 ASAPVVALFDA 254
Cdd:cd04179   78 ARGDIVVTMDA 88
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 482-599 1.09e-06

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: 48.11  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 482 DLCLDQGPDTDNIP---ILYLCHGMTPQNVYYTSTQQLFVGilsptvdddDNKCLvDV------NGRPRLIE-CSYAVAK 551
Cdd:cd23418   14 GRCLDVPGGSTTNGtrlILWDCHGGANQQFTFTSAGELRVG---------GDKCL-DAagggttNGTPVVIWpCNGGANQ 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 326669672 552 RmklhWRFTQGGSIQNTKSKRCLElVENNDNEFGFQLTLQKCTG---QNWT 599
Cdd:cd23418   84 K----WRFNSDGTIRNVNSGLCLD-VAGGGTANGTRLILWSCNGgsnQRWR 129
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 478-601 1.30e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 47.51  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672   478 SLKTDLCLDQgPDTDNIPILYLCHGMTP-QNVYYTSTQQLFVgilsptvdDDDNKCLvDVNG----RPRLIECSYAVAKr 552
Cdd:smart00458   3 SGNTGKCLDV-NGNKNPVGLFDCHGTGGnQLWKLTSDGAIRI--------KDTDLCL-TANGntgsTVTLYSCDGTNDN- 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 326669672   553 mkLHWRFTQGGSIQNTKSKRCLELVENNdneFGFQLTLQKCTG---QNWTIT 601
Cdd:smart00458  72 --QYWEVNKDGTIRNPDSGKCLDVKDGN---TGTKVILWTCSGnpnQKWIFE 118
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 472-598 3.15e-06

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 12 (GALNT12) and similar proteins; GALNT12 (EC 2.4.1.41), also called polypeptide GalNAc transferase 12, GalNAc-T12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT12 has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with non-glycosylated Muc2 and Muc7. It displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. It may play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs. GALNT12 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467349  Cd Length: 140  Bit Score: 47.10  E-value: 3.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 472 YGVLRNSLKTDLCLDQGP-DTDNIP----ILYLCHGMTpQNVY--YTSTQQLFVGILSPtvddddNKCLVDVNGRPRLI- 543
Cdd:cd23471    4 FGMLKNKGMTNYCFDYNPpDEHQIAghqvILYQCHGMG-QNQFfeYTSQNEIRYNTRQP------EGCAAVDAGTDFLTm 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326669672 544 ----ECSYAVAKRMKlhWRFTQGGSIQNTKSKRCLELVENNDNEfGFQLTLQKCTG---QNW 598
Cdd:cd23471   77 hlcrENRQAVPENQK--FIFREDGSLFHVQTQKCVQAVRNESSG-SPAPVLRPCTDsdhQKW 135
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 473-599 4.12e-06

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: 46.17  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 473 GVLRNSLKTdLCLD--QGPDTDNIPI-LYLCHGMTPQNVYYTSTQQL-FVGilsptvddddnKCLvDVNG-------RPR 541
Cdd:cd23451    3 GPVRLANAG-KCLDvpGSSTADGNPVqIYTCNGTAAQKWTLGTDGTLrVLG-----------KCL-DVSGggtangtLVQ 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326669672 542 LIECSYAVAKRmklhWRFTQGGSIQNTKSKRCLElVENNDNEFGFQLTLQKCTG---QNWT 599
Cdd:cd23451   70 LWDCNGTGAQK----WVPRADGTLYNPQSGKCLD-APGGSTTDGTQLQLYTCNGtaaQQWT 125
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 329-386 5.06e-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: 46.78  E-value: 5.06e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 326669672 329 SPALIGCF-VVDRLYFAEIGLLDEGMEIYGgENVELGVRVWQCGGSVEVLPCARIAHIE 386
Cdd:cd04186  109 GPKVSGAFlLVRREVFEEVGGFDEDFFLYY-EDVDLCLRARLAGYRVLYVPQAVIYHHG 166
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 468-601 7.91e-06

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: 45.47  E-value: 7.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 468 DTVAYGVLRNSlktDLCLD---QGPDTDNIPILYLCHGMTPQNVY-YTSTQQLFVGILSPTVDDDDNKClvdvngRPRLI 543
Cdd:cd23441    1 NELAYGQIKQG---NLCLDsdeQLFQGPALLILAPCSNSSDSQEWsFTKDGQLQTQGLCLTVDSSSKDL------PVVLE 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326669672 544 ECSyavaKRMKLHWRFTqGGSIQNTKSKRCLelvennDNEFGFQLTLQKC----TGQNWTIT 601
Cdd:cd23441   72 TCS----DDPKQKWTRT-GRQLVHSESGLCL------DSRKKKGLVVSPCrsgaPSQKWDFT 122
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 166-254 1.56e-04

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: 42.98  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 166 NEAlSVILRSIHSVMNRTPSHLlkEIILVDDNSNNDELkeklqDFVKETNAKQPGFIKVVRHSRQEGLIRSRVSGWRAAS 245
Cdd:cd06423    7 NEE-AVIERTIESLLALDYPKL--EVIVVDDGSTDDTL-----EILEELAALYIRRVLVVRDKENGGKAGALNAGLRHAK 78


                 ....*....
gi 326669672 246 APVVALFDA 254
Cdd:cd06423   79 GDIVVVLDA 87
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 471-598 2.19e-04

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


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 41.59  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 471 AYGVLRNSLkTDLCLD-QGPDTDN---IpILYLCHGmtpqnvyytSTQQLFVgiLSPTVDDD-------DNKCLvDVNG- 538
Cdd:cd00161    1 GTYRIVNAA-SGKCLDvAGGSTANgapV-QQWTCNG---------GANQQWT--LTPVGDGYytirnvaSGKCL-DVAGg 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326669672 539 ------RPRLIECSYAVAKRMKLHWRFTQGGSIQNTKSKRCLElVENNDNEFGFQLTLQKCTG---QNW 598
Cdd:cd00161   67 stangaNVQQWTCNGGDNQQWRLEPVGDGYYRIVNKHSGKCLD-VSGGSTANGANVQQWTCNGganQQW 134
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 156-253 4.23e-04

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 41.80  E-value: 4.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 156 PQVSIVFIFVNEALSVILRSIHSVMNRTPSHLlkEIILVDDNSNNDELKEKLQDFvketnAKQPGFIKVVRHSRQEGLIR 235
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKY-----AAQDPRIKVVFREENGGISA 73

                         90
                 ....*....|....*...
gi 326669672 236 SRVSGWRAASAPVVALFD 253
Cdd:cd04184   74 ATNSALELATGEFVALLD 91
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 471-599 1.68e-03

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: 38.57  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 471 AYGVLRNSlKTDLCLDQGPDTDnipiLYL--CHGMTPQ-----NVYYTSTQqlFVGILSptvddddNKCL-VDVNGRPRL 542
Cdd:cd23415    1 GTVRLRNV-ATGRCLDSNAGGN----VYTgpCNGGPYQrwtwsGVGDGTVT--LRNAAT-------GRCLdSNGNGGVYT 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 543 IECSYAVAKRMKLHWRFTQGGSIQNTKSKRCLelvennDNEFGFQLTLQKCTG---QNWT 599
Cdd:cd23415   67 LPCNGGSYQRWRVTSTSGGGVTLRNVATGRCL------DSNGSGGVYTRPCNGgsyQRWR 120
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 166-254 2.57e-03

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 39.82  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 166 NEA--LSVILRSIHSVMnrtpSHLLKEIILVDDNSNnDELKEKLQDFvketnAKQPGFIKVVRHSRQEGLIRSRVSGWRA 243
Cdd:cd06442    7 NERenIPELIERLDAAL----KGIDYEIIVVDDNSP-DGTAEIVREL-----AKEYPRVRLIVRPGKRGLGSAYIEGFKA 76

                         90
                 ....*....|.
gi 326669672 244 ASAPVVALFDA 254
Cdd:cd06442   77 ARGDVIVVMDA 87
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 524-606 6.45e-03

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 37.11  E-value: 6.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672   524 TVDDDDNKCLvDVNGRPRLI---ECSYAvAKRMKlhWRFTQGGSIQNTKSKRCLELVENNDNefgfQLTLQKCTGQN--- 597
Cdd:smart00458   1 IISGNTGKCL-DVNGNKNPVglfDCHGT-GGNQL--WKLTSDGAIRIKDTDLCLTANGNTGS----TVTLYSCDGTNdnq 72

                           90
                   ....*....|....*.
gi 326669672   598 -W------TITNMLPG 606
Cdd:smart00458  73 yWevnkdgTIRNPDSG 88
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 481-599 7.53e-03

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: 37.03  E-value: 7.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326669672 481 TDLCLD--QGPDTDNIPI-LYLCHGMTPQNVY-YTSTQQLFVGilsptvddDDNKCLvDVN-GRPRLIECSYAVAKRmkl 555
Cdd:cd23442   13 TGYCADyiHGWRLAGGPVeLSPCSGQNGNQLFeYTSDKEIRFG--------SLQLCL-DVRqEQVVLQNCTKEKTSQ--- 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 326669672 556 HWRFTQGGSIQNTKSKRCLELVENNDNEFgfqLTLQKCTG---QNWT 599
Cdd:cd23442   81 KWDFQETGRIVHILSGKCIEAVESENSKL---LFLSPCNGqrnQMWK 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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