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Conserved domains on  [gi|31982036|ref|NP_776100|]
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polypeptide N-acetylgalactosaminyltransferase 18 isoform 1 [Mus musculus]

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 ...
 157-473 2.42e-145

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: 422.77  E-value: 2.42e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 157 SIVFIFVNEALSVLLRSIHSAMERTPSHLLKEIILVDDNSSNEELKEKLTEYVDKvngqKPGFIKVVRHSKQEGLIRSRV 236
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKK----YLPKVKVLRLKKREGLIRARI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 237 SGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFEIEEYPLAAQG-FDWELWCRYLNPPKAW 315
Cdd:cd02510  77 AGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGgFDWSLHFKWLPLPEEE 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 316 WKLENSTAPIRSPALIGC-FIVDRQYFEEIGLLDEGMEVYGGENVELGIRvseishtglssapmmVWQCGGSVEVLPCSR 394
Cdd:cd02510 157 RRRESPTAPIRSPTMAGGlFAIDREWFLELGGYDEGMDIWGGENLELSFK---------------VWQCGGSIEIVPCSR 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 395 IAHIER-AHKPYTEDLTAH-VRRNALRVAEVWMDEFKSHVYMAWNIPQedsGIDIGDITARKALRKQLQCKTFRWYLVSV 472
Cdd:cd02510 222 VGHIFRrKRKPYTFPGGSGtVLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKSFKWYLENV 298


                .
gi 31982036 473 Y 473
Cdd:cd02510 299 Y 299
beta-trefoil_Ricin_GALNT18 cd23475
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 476-617 4.42e-109

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: 324.18  E-value: 4.42e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 476 MRMYSDIIAYGVLQNSLKTDLCLDQGPDTENVPIVYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRCLVDVNSRPRL 555
Cdd:cd23475   1 MRMYTDTIAYGVLQNSLKTDLCLDQGPDTDNIPIMYICHGMTPQNVYYTSNQQLHVGILSPTIDDDDNRCLVDVNSRPRL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31982036 556 IECSYAKAKRMKLHWQFSQGGSIQNRKSKRCLELQENSDMEFGFQLVLQKCSGQHWTITNVL 617
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 ...
 157-473 2.42e-145

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: 422.77  E-value: 2.42e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 157 SIVFIFVNEALSVLLRSIHSAMERTPSHLLKEIILVDDNSSNEELKEKLTEYVDKvngqKPGFIKVVRHSKQEGLIRSRV 236
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKK----YLPKVKVLRLKKREGLIRARI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 237 SGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFEIEEYPLAAQG-FDWELWCRYLNPPKAW 315
Cdd:cd02510  77 AGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGgFDWSLHFKWLPLPEEE 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 316 WKLENSTAPIRSPALIGC-FIVDRQYFEEIGLLDEGMEVYGGENVELGIRvseishtglssapmmVWQCGGSVEVLPCSR 394
Cdd:cd02510 157 RRRESPTAPIRSPTMAGGlFAIDREWFLELGGYDEGMDIWGGENLELSFK---------------VWQCGGSIEIVPCSR 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 395 IAHIER-AHKPYTEDLTAH-VRRNALRVAEVWMDEFKSHVYMAWNIPQedsGIDIGDITARKALRKQLQCKTFRWYLVSV 472
Cdd:cd02510 222 VGHIFRrKRKPYTFPGGSGtVLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKSFKWYLENV 298


                .
gi 31982036 473 Y 473
Cdd:cd02510 299 Y 299
beta-trefoil_Ricin_GALNT18 cd23475
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 476-617 4.42e-109

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: 324.18  E-value: 4.42e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 476 MRMYSDIIAYGVLQNSLKTDLCLDQGPDTENVPIVYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRCLVDVNSRPRL 555
Cdd:cd23475   1 MRMYTDTIAYGVLQNSLKTDLCLDQGPDTDNIPIMYICHGMTPQNVYYTSNQQLHVGILSPTIDDDDNRCLVDVNSRPRL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31982036 556 IECSYAKAKRMKLHWQFSQGGSIQNRKSKRCLELQENSDMEFGFQLVLQKCSGQHWTITNVL 617
Cdd:cd23475  81 IECSYAKAKRMKLYWLFTQGGSIQNKKSKRCLELQENADNEFGYQLVLQKCSGQRWTITNVL 142
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 157-343 1.76e-22

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: 94.38  E-value: 1.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036   157 SIVFIFVNEAlSVLLRSIHSAMERTpsHLLKEIILVDDNSSnEELKEKLTEYVdkvngQKPGFIKVVRHSKQEGLIRSRV 236
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGST-DGTVEIAEEYA-----KKDPRVRVIRLPENRGKAGARN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036   237 SGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFeieEYPLAAQGFDWELWCRYLNppkaww 316
Cdd:pfam00535  72 AGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETG---EYRRASRITLSRLPFFLGL------ 142

                         170       180
                  ....*....|....*....|....*..
gi 31982036   317 KLENSTAPIRSPaliGCFIVDRQYFEE 343
Cdd:pfam00535 143 RLLGLNLPFLIG---GFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
484-611 9.52e-15

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 71.02  E-value: 9.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036   484 AYGVLQNsLKTDLCLD-QGPDTENVPI-VYICHGM-TPQNVYYTSSQQIHVGIlsptvdddDNRCLvDV-----NSRPRL 555
Cdd:pfam00652   1 ATGRIRN-RASGKCLDvPGGSSAGGPVgLYPCHGSnGNQLWTLTGDGTIRSVA--------SDLCL-DVgstadGAKVVL 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982036   556 IECSYAKAKRmklHWQF-SQGGSIQNRKSKRCLELQENSDMefGFQLVLQKC----SGQHW 611
Cdd:pfam00652  71 WPCHPGNGNQ---RWRYdEDGTQIRNPQSGKCLDVSGAGTS--NGKVILWTCdsgnPNQQW 126
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
154-426 2.67e-11

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 63.09  E-value: 2.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 154 PEVSIVFIFVNEAlSVLLRSIHSAMERTPSHLlkEIILVDDNSSNEElkeklteyVDKVNGQKPGFIKVVRHSKQEGLIR 233
Cdd:COG1216   3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGT--------AELLAALAFPRVRVIRNPENLGFAA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 234 SRVSGWRAATAPVVALFDAHVEFNVGWAEPVLTRikenrkriispsfdnikydnfeieeyplaaqgfdwelwcrylnppk 313
Cdd:COG1216  72 ARNLGLRAAGGDYLLFLDDDTVVEPDWLERLLAA---------------------------------------------- 105

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 314 awwklenstapirspaliGCFIVDRQYFEEIGLLDEGMEVYGGEnVELGIRvseishtglssapmmVWQCGGSVEVLPCS 393
Cdd:COG1216 106 ------------------ACLLIRREVFEEVGGFDERFFLYGED-VDLCLR---------------LRKAGYRIVYVPDA 151

                       250       260       270
                ....*....|....*....|....*....|....
gi 31982036 394 RIAHIERA-HKPYTEdlTAHVRRNALRVAEVWMD 426
Cdd:COG1216 152 VVYHLGGAsSGPLLR--AYYLGRNRLLFLRKHGP 183
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 491-614 5.32e-08

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 51.74  E-value: 5.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036    491 SLKTDLCLDQgPDTENVPIVYICHGMTP-QNVYYTSSQQIHVgilsptvdDDDNRCLV---DVNSRPRLIECSYAKAKrm 566
Cdd:smart00458   3 SGNTGKCLDV-NGNKNPVGLFDCHGTGGnQLWKLTSDGAIRI--------KDTDLCLTangNTGSTVTLYSCDGTNDN-- 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 31982036    567 kLHWQFSQGGSIQNRKSKRCLELQENSdmeFGFQLVLQKCSG---QHWTIT 614
Cdd:smart00458  72 -QYWEVNKDGTIRNPDSGKCLDVKDGN---TGTKVILWTCSGnpnQKWIFE 118
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 493-611 3.18e-03

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 39.77  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036  493 KTDLCLD--QGPDTENVPIVYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRclvdVNSRPRLIECSYAKAKRmklhW 570
Cdd:NF035930 125 KGGLCLDvsGGLRPGNGLIVYNCNGGENQRFTWGRGGELRVGDLCLDVADGNTR----DGARVIAWSCSGGPNQR----W 196

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 31982036  571 QfSQGGSIQNRKSKRCLELqENSDMEFGFQLVLQKCSG---QHW 611
Cdd:NF035930 197 R-WRGGQIRSRLSGKCLDI-EGGRARPGQPVIVWSCNGgpnQRW 238
 
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 ...
 157-473 2.42e-145

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: 422.77  E-value: 2.42e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 157 SIVFIFVNEALSVLLRSIHSAMERTPSHLLKEIILVDDNSSNEELKEKLTEYVDKvngqKPGFIKVVRHSKQEGLIRSRV 236
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKK----YLPKVKVLRLKKREGLIRARI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 237 SGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFEIEEYPLAAQG-FDWELWCRYLNPPKAW 315
Cdd:cd02510  77 AGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGgFDWSLHFKWLPLPEEE 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 316 WKLENSTAPIRSPALIGC-FIVDRQYFEEIGLLDEGMEVYGGENVELGIRvseishtglssapmmVWQCGGSVEVLPCSR 394
Cdd:cd02510 157 RRRESPTAPIRSPTMAGGlFAIDREWFLELGGYDEGMDIWGGENLELSFK---------------VWQCGGSIEIVPCSR 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 395 IAHIER-AHKPYTEDLTAH-VRRNALRVAEVWMDEFKSHVYMAWNIPQedsGIDIGDITARKALRKQLQCKTFRWYLVSV 472
Cdd:cd02510 222 VGHIFRrKRKPYTFPGGSGtVLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKSFKWYLENV 298


                .
gi 31982036 473 Y 473
Cdd:cd02510 299 Y 299
beta-trefoil_Ricin_GALNT18 cd23475
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 476-617 4.42e-109

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: 324.18  E-value: 4.42e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 476 MRMYSDIIAYGVLQNSLKTDLCLDQGPDTENVPIVYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRCLVDVNSRPRL 555
Cdd:cd23475   1 MRMYTDTIAYGVLQNSLKTDLCLDQGPDTDNIPIMYICHGMTPQNVYYTSNQQLHVGILSPTIDDDDNRCLVDVNSRPRL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31982036 556 IECSYAKAKRMKLHWQFSQGGSIQNRKSKRCLELQENSDMEFGFQLVLQKCSGQHWTITNVL 617
Cdd:cd23475  81 IECSYAKAKRMKLYWLFTQGGSIQNKKSKRCLELQENADNEFGYQLVLQKCSGQRWTITNVL 142
beta-trefoil_Ricin_GALNT8-like cd23438
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 481-615 3.66e-71

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: 225.77  E-value: 3.66e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 481 DIIAYGVLQNSLKTDLCLDQGPDTENVPIVYICHGMTPQNVYYTSSQQIHVGILSPTVdDDDNRCLVDVNS--RPRLIEC 558
Cdd:cd23438   1 NTVAYGEMRNSLVTDLCLDQGPKENHTAILYPCHGWSPQLVRYTKDGQLYLGQLGSTA-SPDTRCLVDDGKsdKPQLLDC 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 31982036 559 SYAKaKRMKLHWQFSQGGSIQNRKSKRCLELQENSDmEFGFQLVLQKCSGQHWTITN 615
Cdd:cd23438  80 SKVK-NRLQKYWDFSQGGAIQNRATGRCLEVEEDKL-NFGHRLVLQTCSGQKWNIKN 134
beta-trefoil_Ricin_GALNT8 cd23472
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 473-618 8.18e-40

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: 142.65  E-value: 8.18e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 473 YPEMRMYSDIIAYGVLQNSLKTDLCLDQGPDTENVPIVYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDnRCLVD--VN 550
Cdd:cd23472   1 YPVLMPIQTIVGYGTMKNSLNENICIDQGPVPGNTPIMYGCHGYSPQFVYYHLTGELYVGGLKADIYASD-RCLTDpgEG 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982036 551 SRPRLIECSYAKAKRMKLHWQFSQGGSIQNRKSKRCLELQENSDMEFgFQLVLQKCSGQHWTITNVLR 618
Cdd:cd23472  80 WKPELVSCQDATLKGLNMYWDFKQGTAIINRKTKRCLEISLDKTPSY-YTLILQTCTGQKWEIQHVLM 146
beta-trefoil_Ricin_GALNT17 cd23474
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 476-618 9.04e-39

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: 139.65  E-value: 9.04e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 476 MRMYSDIIAYGVLQNSLKTDLCLDQGPDTENVPIVYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRCLVDvNSR--- 552
Cdd:cd23474   1 MRRYNNTVAYGELRNNKAKDVCLDQGPPENHTAILYPCHGWGPQLARYTKEGYLHLGALGTTTLLPDTRCLVD-NKKsrf 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982036 553 PRLIECSYAKAKRMKlHWQFSQGGSIQNRKSKRCLELQENSDmeFGFQLVLQKCSGQHWTITNVLR 618
Cdd:cd23474  80 PQLLDCDKVKSILHK-RWNFIQNGAIMNLGTGRCLEVENRGN--FGIDLILRSCTGQRWTIKNFIK 142
beta-trefoil_Ricin_GALNT9 cd23473
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 476-618 6.94e-35

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: 128.93  E-value: 6.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 476 MRMYSDIIAYGVLQNSLKTDLCLDQGPDTENVPIVYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRCLVD--VNSRP 553
Cdd:cd23473   1 MRIYNNTITYGEVRNSKASGYCLDQGSEEDDKAILYPCHGMSSQLVRYSTEGLLQLGPLGSTAFLPDTKCLVDdgRGRTP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31982036 554 RLIECSYAKAKRMKLhWQFSQGGSIQNRKSKRCLELQENSDMEFGFQLVLQKCSGQHWTITNVLR 618
Cdd:cd23473  81 TLKKCEDVARPAQRL-WDFTQNGPIISRDTGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIK 144
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 157-343 1.76e-22

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: 94.38  E-value: 1.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036   157 SIVFIFVNEAlSVLLRSIHSAMERTpsHLLKEIILVDDNSSnEELKEKLTEYVdkvngQKPGFIKVVRHSKQEGLIRSRV 236
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGST-DGTVEIAEEYA-----KKDPRVRVIRLPENRGKAGARN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036   237 SGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFeieEYPLAAQGFDWELWCRYLNppkaww 316
Cdd:pfam00535  72 AGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETG---EYRRASRITLSRLPFFLGL------ 142

                         170       180
                  ....*....|....*....|....*..
gi 31982036   317 KLENSTAPIRSPaliGCFIVDRQYFEE 343
Cdd:pfam00535 143 RLLGLNLPFLIG---GFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
484-611 9.52e-15

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 71.02  E-value: 9.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036   484 AYGVLQNsLKTDLCLD-QGPDTENVPI-VYICHGM-TPQNVYYTSSQQIHVGIlsptvdddDNRCLvDV-----NSRPRL 555
Cdd:pfam00652   1 ATGRIRN-RASGKCLDvPGGSSAGGPVgLYPCHGSnGNQLWTLTGDGTIRSVA--------SDLCL-DVgstadGAKVVL 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982036   556 IECSYAKAKRmklHWQF-SQGGSIQNRKSKRCLELQENSDMefGFQLVLQKC----SGQHW 611
Cdd:pfam00652  71 WPCHPGNGNQ---RWRYdEDGTQIRNPQSGKCLDVSGAGTS--NGKVILWTCdsgnPNQQW 126
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
154-426 2.67e-11

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 63.09  E-value: 2.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 154 PEVSIVFIFVNEAlSVLLRSIHSAMERTPSHLlkEIILVDDNSSNEElkeklteyVDKVNGQKPGFIKVVRHSKQEGLIR 233
Cdd:COG1216   3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGT--------AELLAALAFPRVRVIRNPENLGFAA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 234 SRVSGWRAATAPVVALFDAHVEFNVGWAEPVLTRikenrkriispsfdnikydnfeieeyplaaqgfdwelwcrylnppk 313
Cdd:COG1216  72 ARNLGLRAAGGDYLLFLDDDTVVEPDWLERLLAA---------------------------------------------- 105

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 314 awwklenstapirspaliGCFIVDRQYFEEIGLLDEGMEVYGGEnVELGIRvseishtglssapmmVWQCGGSVEVLPCS 393
Cdd:COG1216 106 ------------------ACLLIRREVFEEVGGFDERFFLYGED-VDLCLR---------------LRKAGYRIVYVPDA 151

                       250       260       270
                ....*....|....*....|....*....|....
gi 31982036 394 RIAHIERA-HKPYTEdlTAHVRRNALRVAEVWMD 426
Cdd:COG1216 152 VVYHLGGAsSGPLLR--AYYLGRNRLLFLRKHGP 183
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 154-347 6.56e-11

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 62.03  E-value: 6.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 154 PEVSIVFIFVNEAlSVLLRSIHSAMERTPSHLlkEIILVDDNSSNEELkEKLTEYvdkvnGQKPGFIKVVRHSKQEGLIR 233
Cdd:COG0463   2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTA-EILREL-----AAKDPRIRVIRLERNRGKGA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 234 SRVSGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFdniKYDNFEIEEYPLAAQGFDWELWCRYLNPPK 313
Cdd:COG0463  73 ARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSR---LIREGESDLRRLGSRLFNLVRLLTNLPDST 149

                       170       180       190
                ....*....|....*....|....*....|....
gi 31982036 314 AWWKLenstapIRSPALIGcFIVDRQYFEEIGLL 347
Cdd:COG0463 150 SGFRL------FRREVLEE-LGFDEGFLEDTELL 176
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 481-612 7.31e-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: 60.07  E-value: 7.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 481 DIIAYGVLQNsLKTDLCLD-QGPDTE-NVPI-VYICHGMTP-QNVYYTSSQQIHVgilsptvdddDNRCLvDVNSRP--- 553
Cdd:cd23462   1 EALAYGEIRN-LAGKLCLDaPGRKKElNKPVgLYPCHGQGGnQYWMLTKDGEIRR----------DDLCL-DYAGGSgdv 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31982036 554 RLIECSYAKAKRMklhWQFS-QGGSIQNRKSKRCLELQENSdmefgFQLVLQKCSG----QHWT 612
Cdd:cd23462  69 TLYPCHGMKGNQF---WIYDeETKQIVHGTSKKCLELSDDS-----SKLVMEPCNGssprQQWE 124
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 483-614 1.18e-10

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: 59.27  E-value: 1.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 483 IAYGVLQNSLkTDLCLDQGPDTEN---VPIVYICHGMtPQNVY--YTSSQQIHVGILSPTvddddnrCLVDVNSRPRLI- 556
Cdd:cd23435   2 GYYGALRNKG-SELCLDVNNPNGQggkPVIMYGCHGL-GGNQYfeYTSKGEIRHNIGKEL-------CLHASGSDEVILq 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31982036 557 ECSYAK---AKRMKlhWQFSQGGSIQNRKSKRCLELQensdmefGFQLVLQKCSG----QHWTIT 614
Cdd:cd23435  73 HCTSKGkdvPPEQK--WLFTQDGTIRNPASGLCLHAS-------GYKVLLRTCNPsddsQKWTFI 128
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 484-614 3.28e-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: 57.84  E-value: 3.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 484 AYGVLQNsLKTDLCLD--QGPDTENVPIVYICHGMTPQNV-YYTSSQQI-HvgilsptvdddDNRCL-VDVNSRPRLIEC 558
Cdd:cd23460   1 GLGQIKH-TESGLCLDwaGESNGDKTVALKPCHGGGGNQFwMYTGDGQIrQ-----------DHLCLtADEGNKVTLREC 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982036 559 SYAKAKRMklhWQFS-QGGSIQNRKSKRCLELQENSDmefgfQLVLQKCSG----QHWTIT 614
Cdd:cd23460  69 ADQLPSQE---WSYDeKTGTIRHRSTGLCLTLDANND-----VVILKECDSnslwQKWIFQ 121
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 150-272 2.43e-09

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: 58.98  E-value: 2.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 150 PDSLPEVSIVFIFVNEALsVLLRSIHSAMERTPSHLLKEIILVDDNSSnEELKEKLTEYvdkvnGQKPGFIKVVRHSKQE 229
Cdd:COG1215  25 PADLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIAREL-----AAEYPRVRVIERPENG 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 31982036 230 GLIRSRVSGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENR 272
Cdd:COG1215  98 GKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG 140
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 481-615 4.86e-09

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: 55.02  E-value: 4.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 481 DIIAYGVLQNSlKTDLCLD---QGPDTENVPIVYICHGM--TPQNVYYTSSQQIHvgilsptvddDDNRCLV---DVNSR 552
Cdd:cd23459   3 DVLAYGQVRNP-GTNLCLDtlqRDEDKGYNLGLYPCQGGlsSNQLFSLSKKGELR----------REESCADvqgTEESK 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982036 553 PRLIECSyaKAKRMKLHWQFSQGGSIQNRKSKRCLELqENSDMefGFQLVLQKCSG---QHWTITN 615
Cdd:cd23459  72 VILITCH--GLEKFNQKWKHTKGGQIVHLASGKCLDA-EGLKS--GDDVTLAKCDGslsQKWTFEH 132
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 491-614 5.32e-08

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 51.74  E-value: 5.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036    491 SLKTDLCLDQgPDTENVPIVYICHGMTP-QNVYYTSSQQIHVgilsptvdDDDNRCLV---DVNSRPRLIECSYAKAKrm 566
Cdd:smart00458   3 SGNTGKCLDV-NGNKNPVGLFDCHGTGGnQLWKLTSDGAIRI--------KDTDLCLTangNTGSTVTLYSCDGTNDN-- 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 31982036    567 kLHWQFSQGGSIQNRKSKRCLELQENSdmeFGFQLVLQKCSG---QHWTIT 614
Cdd:smart00458  72 -QYWEVNKDGTIRNPDSGKCLDVKDGN---TGTKVILWTCSGnpnQKWIFE 118
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 491-615 5.46e-08

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: 51.53  E-value: 5.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 491 SLKTDLCLD-QGPDTENVPIVYICHGM-TPQNVYYTSSQQIHVGilsptvddddNRCLVDV--NSRPRLIECSyakaKRM 566
Cdd:cd23437  10 NLGTGLCLDtMGHQNGGPVGLYPCHGMgGNQLFRLNEAGQLAVG----------EQCLTASgsGGKVKLRKCN----LGE 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 31982036 567 KLHWQF-SQGGSIQNRKSKRCLELQENSDMefgfqLVLQKCSG----QHWTITN 615
Cdd:cd23437  76 TGKWEYdEATGQIRHKGTGKCLDLNEGTNK-----LILQPCDSsspsQKWEFNE 124
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 158-310 7.42e-08

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: 52.12  E-value: 7.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 158 IVFIFVNEAlSVLLRSIHSAMERTPSHLlkEIILVDDNSSnEELKEKLTEYvdkvnGQKPGFIKVVRHSKQEGLIRSRVS 237
Cdd:cd00761   1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGST-DGTLEILEEY-----AKKDPRVIRVINEENQGLAAARNA 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982036 238 GWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPS-----FDNIKYDNFEIEEYPLAAQGFDWELWCRYLN 310
Cdd:cd00761  72 GLKAARGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGpgnllFRRELLEEIGGFDEALLSGEEDDDFLLRLLR 149
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 481-614 1.56e-07

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: 50.48  E-value: 1.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 481 DIIAYGVLQNSlktDLCLD-QGPDTENVPIVYICHGMTPQNV---YYTSSQQIHVGILSPTVDDDDNrclvdvNSRPRLI 556
Cdd:cd23441   1 NELAYGQIKQG---NLCLDsDEQLFQGPALLILAPCSNSSDSqewSFTKDGQLQTQGLCLTVDSSSK------DLPVVLE 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31982036 557 ECSyakaKRMKLHWQFsQGGSIQNRKSKRCLELQensdMEFGfqLVLQKCS----GQHWTIT 614
Cdd:cd23441  72 TCS----DDPKQKWTR-TGRQLVHSESGLCLDSR----KKKG--LVVSPCRsgapSQKWDFT 122
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 164-252 1.96e-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: 51.42  E-value: 1.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 164 NEA--LSVLLRSIHSAMERTPSHllkEIILVDDNSSN---EELKEKlteyvdkvnGQKPGFIKVVRHSKQEGLIRSRVSG 238
Cdd:cd04179   7 NEEenIPELVERLLAVLEEGYDY---EIIVVDDGSTDgtaEIAREL---------AARVPRVRVIRLSRNFGKGAAVRAG 74

                        90
                ....*....|....
gi 31982036 239 WRAATAPVVALFDA 252
Cdd:cd04179  75 FKAARGDIVVTMDA 88
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 495-612 1.20e-05

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.


Pssm-ID: 467297 [Multi-domain]  Cd Length: 130  Bit Score: 45.03  E-value: 1.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 495 DLCLDQGPDTENVP---IVYICHGMTPQNVYYTSSQQIHVGilsptvdddDNRCL-VDVNSRP---RLI--ECSYAKAKR 565
Cdd:cd23418  14 GRCLDVPGGSTTNGtrlILWDCHGGANQQFTFTSAGELRVG---------GDKCLdAAGGGTTngtPVViwPCNGGANQK 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 31982036 566 mklhWQFSQGGSIQNRKSKRCLELQENSDMEfGFQLVLQKCSG---QHWT 612
Cdd:cd23418  85 ----WRFNSDGTIRNVNSGLCLDVAGGGTAN-GTRLILWSCNGgsnQRWR 129
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 486-612 2.45e-05

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: 43.97  E-value: 2.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 486 GVLQNSlKTDLCLD--QGPDTENVPIVY-ICHGMTPQNVY-YTSSQQIHVGilsptvddDDNRCLvDVNS-RPRLIECSY 560
Cdd:cd23442   6 GQLYNT-GTGYCADyiHGWRLAGGPVELsPCSGQNGNQLFeYTSDKEIRFG--------SLQLCL-DVRQeQVVLQNCTK 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 31982036 561 AKAKRmklHWQFSQGGSIQNRKSKRCLELQENSDMEFGFqlvLQKCSG---QHWT 612
Cdd:cd23442  76 EKTSQ---KWDFQETGRIVHILSGKCIEAVESENSKLLF---LSPCNGqrnQMWK 124
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 484-611 6.31e-05

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: 43.13  E-value: 6.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 484 AYGVLQNSLkTDLCLD-QGPDTEN-VPIV-YICHGMTPQNVYYTSSQQIHVGILSptvdDDDNRCLvDV-------NSRP 553
Cdd:cd00161   1 GTYRIVNAA-SGKCLDvAGGSTANgAPVQqWTCNGGANQQWTLTPVGDGYYTIRN----VASGKCL-DVaggstanGANV 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982036 554 RLIECSYAKAKRMKLHWQFSQGGSIQNRKSKRCLELQENSdMEFGFQLVLQKCSG---QHW 611
Cdd:cd00161  75 QQWTCNGGDNQQWRLEPVGDGYYRIVNKHSGKCLDVSGGS-TANGANVQQWTCNGganQQW 134
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 485-611 2.36e-04

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: 41.70  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 485 YGVLQNSLKTDLCLDQGPDTEN-----VPIVYICHGMTpQNVY--YTSSQQIHVGILSP----TVDDDDNRCLVDVNSRP 553
Cdd:cd23471   4 FGMLKNKGMTNYCFDYNPPDEHqiaghQVILYQCHGMG-QNQFfeYTSQNEIRYNTRQPegcaAVDAGTDFLTMHLCREN 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982036 554 RLIECSYAKakrmklhWQFSQGGSIQNRKSKRCLELQENSDMEfGFQLVLQKCSG---QHW 611
Cdd:cd23471  83 RQAVPENQK-------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 ...
 496-612 8.41e-04

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: 39.62  E-value: 8.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 496 LCLD--QGPDTENVPI-VYICHGMTPQNVYYTSSQQIHVgilsptvdddDNRCLvDVN-------SRPRLIECSYAKAKR 565
Cdd:cd23451  12 KCLDvpGSSTADGNPVqIYTCNGTAAQKWTLGTDGTLRV----------LGKCL-DVSgggtangTLVQLWDCNGTGAQK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 31982036 566 mklhWQFSQGGSIQNRKSKRCLELQeNSDMEFGFQLVLQKCSG---QHWT 612
Cdd:cd23451  81 ----WVPRADGTLYNPQSGKCLDAP-GGSTTDGTQLQLYTCNGtaaQQWT 125
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 164-252 9.79e-04

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: 40.98  E-value: 9.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 164 NEA--LSVLLRSIHSAMERTPShllkEIILVDDNS---SNEELKEKLTEYvdkvngqkpGFIKVVRHSKQEGLIRSRVSG 238
Cdd:cd06442   7 NERenIPELIERLDAALKGIDY----EIIVVDDNSpdgTAEIVRELAKEY---------PRVRLIVRPGKRGLGSAYIEG 73

                        90
                ....*....|....
gi 31982036 239 WRAATAPVVALFDA 252
Cdd:cd06442  74 FKAARGDVIVVMDA 87
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 154-251 1.06e-03

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: 40.65  E-value: 1.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 154 PEVSIVFIFVNEALSVLLRSIHSAMERTPSHLlkEIILVDDNSSNEELKEKLTEYvdkvnGQKPGFIKVVRHSKQEGLIR 233
Cdd:cd04184   1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKY-----AAQDPRIKVVFREENGGISA 73

                        90
                ....*....|....*...
gi 31982036 234 SRVSGWRAATAPVVALFD 251
Cdd:cd04184  74 ATNSALELATGEFVALLD 91
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 164-252 1.62e-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: 39.90  E-value: 1.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036 164 NEAlSVLLRSIHSAMERTPSHLlkEIILVDDNSSNEELkEKLTEYvdkvnGQKPGFIKVVRHSKQEG-----LIRsrvsG 238
Cdd:cd06423   7 NEE-AVIERTIESLLALDYPKL--EVIVVDDGSTDDTL-EILEEL-----AALYIRRVLVVRDKENGgkagaLNA----G 73

                        90
                ....*....|....
gi 31982036 239 WRAATAPVVALFDA 252
Cdd:cd06423  74 LRHAKGDIVVVLDA 87
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 327-399 1.64e-03

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: 39.46  E-value: 1.64e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31982036 327 SPALIGCFI-VDRQYFEEIGLLDEGMEVYgGENVELGIRvseishtglssapmmVWQCGGSVEVLPCSRIAHIE 399
Cdd:cd04186 109 GPKVSGAFLlVRREVFEEVGGFDEDFFLY-YEDVDLCLR---------------ARLAGYRVLYVPQAVIYHHG 166
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 493-611 3.18e-03

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 39.77  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982036  493 KTDLCLD--QGPDTENVPIVYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRclvdVNSRPRLIECSYAKAKRmklhW 570
Cdd:NF035930 125 KGGLCLDvsGGLRPGNGLIVYNCNGGENQRFTWGRGGELRVGDLCLDVADGNTR----DGARVIAWSCSGGPNQR----W 196

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 31982036  571 QfSQGGSIQNRKSKRCLELqENSDMEFGFQLVLQKCSG---QHW 611
Cdd:NF035930 197 R-WRGGQIRSRLSGKCLDI-EGGRARPGQPVIVWSCNGgpnQRW 238
 
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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