NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19921720|ref|NP_610256|]
View 

polypeptide N-Acetylgalactosaminyltransferase 3 [Drosophila melanogaster]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase( domain architecture ID 11551826)

polypeptide N-acetylgalactosaminyltransferase catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 153-457 3.25e-159

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: 459.75  E-value: 3.25e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 153 SVIIVFHNEAWSVLLRTITSVINRSPRHLLKEIILVDDASDRSYLKRQLESYVKVLAVPTRIFRMKKRSGLVPARLLGAE 232
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 233 NARGDVLTFLDAHCECSRGWLEPLLSRIKESRKVVICPVIDIISDDNFSYTKTFENHWGAFNWQLSFRWFSSDRKRQTAg 312
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEERRR- 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 313 nssKDSTDPIATPGMAGGLFAIDRKYFYEMGSYDSNMRVWGGENVEMSFRIWQCGGRVEISPCSHVGHVFRSS-TPYTFP 391
Cdd:cd02510 160 ---ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFP 236

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921720 392 GGMSEVLTdNLARAATVWMDDwqYFIMLYTSGLTLGAKDKVNVTERVALRERLQCKPFSWYLENIW 457
Cdd:cd02510 237 GGSGTVLR-NYKRVAEVWMDE--YKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 515-661 1.05e-32

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: 122.17  E-value: 1.05e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 515 LMALIDLERDKCLRPLKEDVprsSLSAVTVGDCTSHaQSMDMFVITPKGQIMTnDNVCLTYRQQKlgvikmlknrnatts 594
Cdd:cd23460   2 LGQIKHTESGLCLDWAGESN---GDKTVALKPCHGG-GGNQFWMYTGDGQIRQ-DHLCLTADEGN--------------- 61

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921720 595 NVMLAQCASD-SSQLWTYDMDTQQISHRDTKLCLTLKAAtnsrlqkvEKVVLSMECDFKDITQKWGFI 661
Cdd:cd23460  62 KVTLRECADQlPSQEWSYDEKTGTIRHRSTGLCLTLDAN--------NDVVILKECDSNSLWQKWIFQ 121
 
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 ...
 153-457 3.25e-159

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: 459.75  E-value: 3.25e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 153 SVIIVFHNEAWSVLLRTITSVINRSPRHLLKEIILVDDASDRSYLKRQLESYVKVLAVPTRIFRMKKRSGLVPARLLGAE 232
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 233 NARGDVLTFLDAHCECSRGWLEPLLSRIKESRKVVICPVIDIISDDNFSYTKTFENHWGAFNWQLSFRWFSSDRKRQTAg 312
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEERRR- 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 313 nssKDSTDPIATPGMAGGLFAIDRKYFYEMGSYDSNMRVWGGENVEMSFRIWQCGGRVEISPCSHVGHVFRSS-TPYTFP 391
Cdd:cd02510 160 ---ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFP 236

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921720 392 GGMSEVLTdNLARAATVWMDDwqYFIMLYTSGLTLGAKDKVNVTERVALRERLQCKPFSWYLENIW 457
Cdd:cd02510 237 GGSGTVLR-NYKRVAEVWMDE--YKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 153-337 6.53e-33

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: 124.43  E-value: 6.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720   153 SVIIVFHNEaWSVLLRTITSVINRSprHLLKEIILVDDAS-DRSylKRQLESYVKVLaVPTRIFRMKKRSGLVPARLLGA 231
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQT--YPNFEIIVVDDGStDGT--VEIAEEYAKKD-PRVRVIRLPENRGKAGARNAGL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720   232 ENARGDVLTFLDAHCECSRGWLEPLLSRIKESRKVVICPVIDIISDDNFSYTKTFENHWGafnwqlsfrwfssdRKRQTA 311
Cdd:pfam00535  75 RAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLS--------------RLPFFL 140

                         170       180
                  ....*....|....*....|....*.
gi 19921720   312 GNSSKDSTDPIATPGMAGGLFAIDRK 337
Cdd:pfam00535 141 GLRLLGLNLPFLIGGFALYRREALEE 166
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 515-661 1.05e-32

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: 122.17  E-value: 1.05e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 515 LMALIDLERDKCLRPLKEDVprsSLSAVTVGDCTSHaQSMDMFVITPKGQIMTnDNVCLTYRQQKlgvikmlknrnatts 594
Cdd:cd23460   2 LGQIKHTESGLCLDWAGESN---GDKTVALKPCHGG-GGNQFWMYTGDGQIRQ-DHLCLTADEGN--------------- 61

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921720 595 NVMLAQCASD-SSQLWTYDMDTQQISHRDTKLCLTLKAAtnsrlqkvEKVVLSMECDFKDITQKWGFI 661
Cdd:cd23460  62 KVTLRECADQlPSQEWSYDEKTGTIRHRSTGLCLTLDAN--------NDVVILKECDSNSLWQKWIFQ 121
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
516-658 7.29e-18

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 80.27  E-value: 7.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720   516 MALIDLERDKCLrplkeDVPRSSL--SAVTVGDCTSHAQSmDMFVITPKGQIMTN-DNVCLTYRQQKLGvikmlknrnat 592
Cdd:pfam00652   3 GRIRNRASGKCL-----DVPGGSSagGPVGLYPCHGSNGN-QLWTLTGDGTIRSVaSDLCLDVGSTADG----------- 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19921720   593 tSNVMLAQCAS-DSSQLWTYDMDTQQISHRDTKLCLTLKAATNSRlqkvEKVVLSmECDFKDITQKW 658
Cdd:pfam00652  66 -AKVVLWPCHPgNGNQRWRYDEDGTQIRNPQSGKCLDVSGAGTSN----GKVILW-TCDSGNPNQQW 126
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 141-385 6.60e-17

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: 82.10  E-value: 6.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 141 RDKKYASGLPSTSVIIVFHNEAwSVLLRTITSVINRSPRHLLKEIILVDDASD---RSYLKRQLESYVKVlavptRIFRM 217
Cdd:COG1215  20 RRRRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGSTdetAEIARELAAEYPRV-----RVIER 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 218 KKRSGLVPARLLGAENARGDVLTFLDAHCECSRGWLEPLLSRIKESRKvvicpvidiisddnfsytktfenhwgafnwql 297
Cdd:COG1215  94 PENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGV-------------------------------- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 298 sfrwfssdrkrqtagnsskdstdpiatpGMAGGLFAIDRKYFYEMGSYDSNMrvwGGENVEMSFRIWQCGGRVEISPCSH 377
Cdd:COG1215 142 ----------------------------GASGANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAV 190


                ....*...
gi 19921720 378 VGHVFRSS 385
Cdd:COG1215 191 VYEEAPET 198
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 519-661 3.56e-13

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 66.38  E-value: 3.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720    519 IDLERDKCLrplkeDVPrSSLSAVTVGDCTSHaQSMDMFVITPKGQIMTND-NVCLTYRQQKlgvikmlknrnatTSNVM 597
Cdd:smart00458   2 ISGNTGKCL-----DVN-GNKNPVGLFDCHGT-GGNQLWKLTSDGAIRIKDtDLCLTANGNT-------------GSTVT 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19921720    598 LAQCASDS-SQLWTYDMDtQQISHRDTKLCLTLKAATNSrlqkveKVVLSMECDfKDITQKWGFI 661
Cdd:smart00458  62 LYSCDGTNdNQYWEVNKD-GTIRNPDSGKCLDVKDGNTG------TKVILWTCS-GNPNQKWIFE 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 ...
 153-457 3.25e-159

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: 459.75  E-value: 3.25e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 153 SVIIVFHNEAWSVLLRTITSVINRSPRHLLKEIILVDDASDRSYLKRQLESYVKVLAVPTRIFRMKKRSGLVPARLLGAE 232
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 233 NARGDVLTFLDAHCECSRGWLEPLLSRIKESRKVVICPVIDIISDDNFSYTKTFENHWGAFNWQLSFRWFSSDRKRQTAg 312
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEERRR- 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 313 nssKDSTDPIATPGMAGGLFAIDRKYFYEMGSYDSNMRVWGGENVEMSFRIWQCGGRVEISPCSHVGHVFRSS-TPYTFP 391
Cdd:cd02510 160 ---ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFP 236

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921720 392 GGMSEVLTdNLARAATVWMDDwqYFIMLYTSGLTLGAKDKVNVTERVALRERLQCKPFSWYLENIW 457
Cdd:cd02510 237 GGSGTVLR-NYKRVAEVWMDE--YKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 153-337 6.53e-33

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: 124.43  E-value: 6.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720   153 SVIIVFHNEaWSVLLRTITSVINRSprHLLKEIILVDDAS-DRSylKRQLESYVKVLaVPTRIFRMKKRSGLVPARLLGA 231
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQT--YPNFEIIVVDDGStDGT--VEIAEEYAKKD-PRVRVIRLPENRGKAGARNAGL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720   232 ENARGDVLTFLDAHCECSRGWLEPLLSRIKESRKVVICPVIDIISDDNFSYTKTFENHWGafnwqlsfrwfssdRKRQTA 311
Cdd:pfam00535  75 RAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLS--------------RLPFFL 140

                         170       180
                  ....*....|....*....|....*.
gi 19921720   312 GNSSKDSTDPIATPGMAGGLFAIDRK 337
Cdd:pfam00535 141 GLRLLGLNLPFLIGGFALYRREALEE 166
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 515-661 1.05e-32

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: 122.17  E-value: 1.05e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 515 LMALIDLERDKCLRPLKEDVprsSLSAVTVGDCTSHaQSMDMFVITPKGQIMTnDNVCLTYRQQKlgvikmlknrnatts 594
Cdd:cd23460   2 LGQIKHTESGLCLDWAGESN---GDKTVALKPCHGG-GGNQFWMYTGDGQIRQ-DHLCLTADEGN--------------- 61

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921720 595 NVMLAQCASD-SSQLWTYDMDTQQISHRDTKLCLTLKAAtnsrlqkvEKVVLSMECDFKDITQKWGFI 661
Cdd:cd23460  62 KVTLRECADQlPSQEWSYDEKTGTIRHRSTGLCLTLDAN--------NDVVILKECDSNSLWQKWIFQ 121
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
516-658 7.29e-18

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 80.27  E-value: 7.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720   516 MALIDLERDKCLrplkeDVPRSSL--SAVTVGDCTSHAQSmDMFVITPKGQIMTN-DNVCLTYRQQKLGvikmlknrnat 592
Cdd:pfam00652   3 GRIRNRASGKCL-----DVPGGSSagGPVGLYPCHGSNGN-QLWTLTGDGTIRSVaSDLCLDVGSTADG----------- 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19921720   593 tSNVMLAQCAS-DSSQLWTYDMDTQQISHRDTKLCLTLKAATNSRlqkvEKVVLSmECDFKDITQKW 658
Cdd:pfam00652  66 -AKVVLWPCHPgNGNQRWRYDEDGTQIRNPQSGKCLDVSGAGTSN----GKVILW-TCDSGNPNQQW 126
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 141-385 6.60e-17

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: 82.10  E-value: 6.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 141 RDKKYASGLPSTSVIIVFHNEAwSVLLRTITSVINRSPRHLLKEIILVDDASD---RSYLKRQLESYVKVlavptRIFRM 217
Cdd:COG1215  20 RRRRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGSTdetAEIARELAAEYPRV-----RVIER 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 218 KKRSGLVPARLLGAENARGDVLTFLDAHCECSRGWLEPLLSRIKESRKvvicpvidiisddnfsytktfenhwgafnwql 297
Cdd:COG1215  94 PENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGV-------------------------------- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 298 sfrwfssdrkrqtagnsskdstdpiatpGMAGGLFAIDRKYFYEMGSYDSNMrvwGGENVEMSFRIWQCGGRVEISPCSH 377
Cdd:COG1215 142 ----------------------------GASGANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAV 190


                ....*...
gi 19921720 378 VGHVFRSS 385
Cdd:COG1215 191 VYEEAPET 198
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 154-269 1.32e-16

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: 77.55  E-value: 1.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 154 VIIVFHNEAwSVLLRTITSVINRSPRHLlkEIILVDDAS-DRSYLKrqLESYVKvLAVPTRIFRMKKRSGLVPARLLGAE 232
Cdd:cd00761   1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGStDGTLEI--LEEYAK-KDPRVIRVINEENQGLAAARNAGLK 74

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19921720 233 NARGDVLTFLDAHCECSRGWLEPLLSRIKESRKVVIC 269
Cdd:cd00761  75 AARGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 150-380 1.98e-15

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 75.51  E-value: 1.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 150 PSTSVIIVFHNEAwSVLLRTITSVINRSPRHLlkEIILVDDAS-DRS--YLKRQLESYVKVlavptRIFRMKKRSGLVPA 226
Cdd:COG0463   2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGStDGTaeILRELAAKDPRI-----RVIRLERNRGKGAA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 227 RLLGAENARGDVLTFLDAHCECSRGWLEPLLSRIKESRKVVICPVIDIisDDNFSYTKTFENHWGAFNWQLSFrwfssdr 306
Cdd:COG0463  74 RNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLI--REGESDLRRLGSRLFNLVRLLTN------- 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921720 307 krqtagnsskdstdpiaTPGMAGGLFAIDRKYFYEMGsYDSNMrvwgGENVEMsFRIWQCGGRVEISPCSHVGH 380
Cdd:COG0463 145 -----------------LPDSTSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVPVRYRAG 195
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
150-386 5.01e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 71.18  E-value: 5.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 150 PSTSVIIVFHNEaWSVLLRTITSVINRSPRHLlkEIILVDDASD---RSYLKRQLESYVKVLAVPTRIfrmkkrsGLVPA 226
Cdd:COG1216   3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGSTdgtAELLAALAFPRVRVIRNPENL-------GFAAA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 227 RLLGAENARGDVLTFLDAHCECSRGWLEPLLSrikesrkvvicpvidiisddnfsytktfenhwgafnwqlsfrwfssdr 306
Cdd:COG1216  73 RNLGLRAAGGDYLLFLDDDTVVEPDWLERLLA------------------------------------------------ 104

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 307 krqtAGNsskdstdpiatpgmagglFAIDRKYFYEMGSYDSNMRVWGGEnVEMSFRIWQCGGRVEISPCSHVGHVFRSST 386
Cdd:COG1216 105 ----AAC------------------LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASS 161
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 556-660 2.85e-13

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: 66.94  E-value: 2.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 556 MFVITPKGQIMTNDnVCLTYRqqklgvikmlknrnATTSNVMLAQCASDSSQLWTYDMDTQQISHRDTKLCLTLKAATNs 635
Cdd:cd23437  41 LFRLNEAGQLAVGE-QCLTAS--------------GSGGKVKLRKCNLGETGKWEYDEATGQIRHKGTGKCLDLNEGTN- 104

                        90       100
                ....*....|....*....|....*
gi 19921720 636 rlqkveKVVLSmECDFKDITQKWGF 660
Cdd:cd23437 105 ------KLILQ-PCDSSSPSQKWEF 122
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 519-661 3.56e-13

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 66.38  E-value: 3.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720    519 IDLERDKCLrplkeDVPrSSLSAVTVGDCTSHaQSMDMFVITPKGQIMTND-NVCLTYRQQKlgvikmlknrnatTSNVM 597
Cdd:smart00458   2 ISGNTGKCL-----DVN-GNKNPVGLFDCHGT-GGNQLWKLTSDGAIRIKDtDLCLTANGNT-------------GSTVT 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19921720    598 LAQCASDS-SQLWTYDMDtQQISHRDTKLCLTLKAATNSrlqkveKVVLSMECDfKDITQKWGFI 661
Cdd:smart00458  62 LYSCDGTNdNQYWEVNKD-GTIRNPDSGKCLDVKDGNTG------TKVILWTCS-GNPNQKWIFE 118
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 556-658 2.21e-11

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1)-like subfamily; The GALNT1-like subfamily includes GALNT1 and GALNT13. They catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT1 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT13 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467311 [Multi-domain]  Cd Length: 127  Bit Score: 61.56  E-value: 2.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 556 MFVITPKGQIMTnDNVCLTYRQQKlgvikmlknrnattSNVMLAQC-ASDSSQLWTYDMDTQQISHRDTKLCLTLkaatn 634
Cdd:cd23433  42 VFSYTAKGEIRS-DDLCLDASRKG--------------GPVKLEKChGMGGNQEWEYDKETKQIRHVNSGLCLTA----- 101

                        90       100
                ....*....|....*....|....
gi 19921720 635 SRLQKVEKVVLsMECDfKDITQKW 658
Cdd:cd23433 102 PNEDDPNEPVL-RPCD-GGPSQKW 123
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 153-385 3.85e-11

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 63.79  E-value: 3.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 153 SVIIVFHNEAwSVLLRTITSVINRSPRHLLKEIILVDDASD---RSYLKRQLESYVKVlavptRIFRMKKRSgLVPARLL 229
Cdd:cd02525   3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTdgtREIVQEYAAKDPRI-----RLIDNPKRI-QSAGLNI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 230 GAENARGDVLTFLDAHCECSRGWLEPLLSRIKESRKVVICPVIDIISDDNFsytktfenhWGAFNWQLSFRWFSSDRKRQ 309
Cdd:cd02525  76 GIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKF---------QKAIAVAQSSPLGSGGSAYR 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921720 310 TaGNSSKDSTDPIatpgmAGGLFaiDRKYFYEMGSYDSNMRVwgGENVEMSFRIWQCGGRVEISPCSHVGHVFRSS 385
Cdd:cd02525 147 G-GAVKIGYVDTV-----HHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPRST 212
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 524-660 4.52e-09

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: 55.06  E-value: 4.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 524 DKCLRPLKEDvpRSSLSAVTVGDCtsHAQSMD-MFVITPKGQImTNDNVCLTYrqqklgvikmlknrNATTSNVMLAQC- 601
Cdd:cd23462  14 KLCLDAPGRK--KELNKPVGLYPC--HGQGGNqYWMLTKDGEI-RRDDLCLDY--------------AGGSGDVTLYPCh 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19921720 602 ASDSSQLWTYDMDTQQISHRDTKLCLTLKAATNsrlqkveKVVLsMECDFKDITQKWGF 660
Cdd:cd23462  75 GMKGNQFWIYDEETKQIVHGTSKKCLELSDDSS-------KLVM-EPCNGSSPRQQWEF 125
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 154-357 4.72e-09

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 57.30  E-value: 4.72e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 154 VIIVFHNEAWSvLLRTITSVINRS-PRHLLkEIILVDDAS-DRS-------YLKRQLEsyVKVLAVPTRIFRMKKRsglv 224
Cdd:cd04192   1 VVIAARNEAEN-LPRLLQSLSALDyPKEKF-EVILVDDHStDGTvqilefaAAKPNFQ--LKILNNSRVSISGKKN---- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 225 pARLLGAENARGDVLTFLDAHCECSRGWLEPLLSRI-KESRKVVICPVIDIISDDNFSYTKTFEnhwgafnwqlsfrWFS 303
Cdd:cd04192  73 -ALTTAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIqKEQIGLVAGPVIYFKGKSLLAKFQRLD-------------WLS 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19921720 304 SdrkrQTAGNSSKDSTDPIatpgMAGGL-FAIDRKYFYEMGSYDSNMRVWGGENV 357
Cdd:cd04192 139 L----LGLIAGSFGLGKPF----MCNGAnMAYRKEAFFEVGGFEGNDHIASGDDE 185
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 557-661 3.04e-08

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: 52.40  E-value: 3.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 557 FVITPKGQIMTNDNvCLTYRqqklgvikmlknRNATTSNVMLAQCASDSSQLWTYdmDTQQISHRDTKLCLTlkaatnsr 636
Cdd:cd23441  42 WSFTKDGQLQTQGL-CLTVD------------SSSKDLPVVLETCSDDPKQKWTR--TGRQLVHSESGLCLD-------- 98

                        90       100
                ....*....|....*....|....*
gi 19921720 637 LQKVEKVVLSmECDFKDITQKWGFI 661
Cdd:cd23441  99 SRKKKGLVVS-PCRSGAPSQKWDFT 122
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 557-660 1.29e-07

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467312 [Multi-domain]  Cd Length: 121  Bit Score: 50.78  E-value: 1.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 557 FVITPKGQImTNDNVCLTYRQQKLGvikmlknrnattSNVMLAQC-ASDSSQLWTYDMDTQQISHRDTKLCLTLKAATNS 635
Cdd:cd23434  37 WSFTKDGQI-KHDDLCLTVVDRAPG------------SLVTLQPCrEDDSNQKWEQIENNSKLRHVGSNLCLDSRNAKSG 103

                        90       100
                ....*....|....*....|....*
gi 19921720 636 RLqkvekvVLSmECDFKDITQKWGF 660
Cdd:cd23434 104 GL------TVE-TCDPSSGSQQWKF 121
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 547-661 1.59e-07

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: 50.78  E-value: 1.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 547 CTSHAQSMDMFVITPKGQImTNDNVCLTYRqqklgvikmlknrNATTSNVMLAQCASD--SSQLWTYDMdTQQISHRDTK 624
Cdd:cd23459  37 CQGGLSSNQLFSLSKKGEL-RREESCADVQ-------------GTEESKVILITCHGLekFNQKWKHTK-GGQIVHLASG 101

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19921720 625 LCLTLkaatnSRLQKVEKVVLsMECDfKDITQKWGFI 661
Cdd:cd23459 102 KCLDA-----EGLKSGDDVTL-AKCD-GSLSQKWTFE 131
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 154-349 1.66e-07

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: 51.84  E-value: 1.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 154 VIIVFHNEAwSVLLRTITSVIN-RSPRhllKEIILVDDAS-DRSY--LKRQLESYVKVLAVPTRIFRMKKRSGLVparlL 229
Cdd:cd06423   1 IIVPAYNEE-AVIERTIESLLAlDYPK---LEVIVVDDGStDDTLeiLEELAALYIRRVLVVRDKENGGKAGALN----A 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 230 GAENARGDVLTFLDAHCECSRGWLEPLLSRIKESRKVVICPVidiisddNFSYTKTFENHWGAFNWQLSFRWFSSDRKRQ 309
Cdd:cd06423  73 GLRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQG-------RVRVRNGSENLLTRLQAIEYLSIFRLGRRAQ 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19921720 310 TAGNsskdstdpiATPGMAGGLFAIDRKYFYEMGSYDSNM 349
Cdd:cd06423 146 SALG---------GVLVLSGAFGAFRREALREVGGWDEDT 176
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 154-244 2.93e-06

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


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 48.34  E-value: 2.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 154 VIIVFHNEAwsvllRTITSVINRSPRHLLK----EIILVDDAS-DRSY--LKRQLESYVKVlavptRIFRMKKRSGLVPA 226
Cdd:cd04179   1 VVIPAYNEE-----ENIPELVERLLAVLEEgydyEIIVVDDGStDGTAeiARELAARVPRV-----RVIRLSRNFGKGAA 70

                        90
                ....*....|....*...
gi 19921720 227 RLLGAENARGDVLTFLDA 244
Cdd:cd04179  71 VRAGFKAARGDIVVTMDA 88
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 150-243 7.54e-06

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: 47.20  E-value: 7.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 150 PSTSVIIVFHNEAWSVLLRTITSVINRSPRHLlkEIILVDDASDRSYLKRQLESYvKVLAVPTRIFRMKKRSGLVPARLL 229
Cdd:cd04184   1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKY-AAQDPRIKVVFREENGGISAATNS 77

                        90
                ....*....|....
gi 19921720 230 GAENARGDVLTFLD 243
Cdd:cd04184  78 ALELATGEFVALLD 91
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 133-244 8.74e-06

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. 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 of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 47.58  E-value: 8.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 133 KDYRTPECRDKKYasgLPSTSVIIVFHNEAwSVLLRTITSVINRS-PRHLLkEIILVDDAS-DRSY--LKRQLESYVKVL 208
Cdd:cd06439  15 LRPKPPSLPDPAY---LPTVTIIIPAYNEE-AVIEAKLENLLALDyPRDRL-EIIVVSDGStDGTAeiAREYADKGVKLL 89

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19921720 209 AVPtrifrmkKRSGLVPARLLGAENARGDVLTFLDA 244
Cdd:cd06439  90 RFP-------ERRGKAAALNRALALATGEIVVFTDA 118
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 154-380 1.07e-05

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 46.01  E-value: 1.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 154 VIIVFHNeAWSVLLRTITSVINRSPRHLlkEIILVDDASDRSYLK--RQLESYVKVLavptrifRMKKRSGLVPARLLGA 231
Cdd:cd04186   1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVDNASTDGSVEllRELFPEVRLI-------RNGENLGFGAGNNQGI 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 232 ENARGDVLTFLDAHCECSRGWLEPLLSRIKESRKVVICpvidiisddnfsytktfenhwgafnwqlsfrwfssdrkrqta 311
Cdd:cd04186  71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIV------------------------------------------ 108

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921720 312 gnsskdstdpiaTPGMAGGLFAIDRKYFYEMGSYDSNMRVWgGENVEMSFRIWQCGGRVEISPCSHVGH 380
Cdd:cd04186 109 ------------GPKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYH 164
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 154-244 4.96e-05

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 44.39  E-value: 4.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 154 VIIVFHNEAWSV--LLRTITSVINRSPRHLlkEIILVDDAS-DRSY--LKRQLESYVKVlavptRIFRMKKRSGLVPARL 228
Cdd:cd04187   1 IVVPVYNEEENLpeLYERLKAVLESLGYDY--EIIFVDDGStDRTLeiLRELAARDPRV-----KVIRLSRNFGQQAALL 73

                        90
                ....*....|....*.
gi 19921720 229 LGAENARGDVLTFLDA 244
Cdd:cd04187  74 AGLDHARGDAVITMDA 89
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 325-375 8.17e-05

N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 41.44  E-value: 8.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19921720   325 PGMAGGLFAIDRKYFYEMGSYDSNMRVWGGENVEMSFRIWQCGGRVEISPC 375
Cdd:pfam02709  17 KTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG 67
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 607-660 1.83e-04

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10)-like subfamily; The GALNT10-like subfamily includes GALNT10 and GALNTL6. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467317 [Multi-domain]  Cd Length: 126  Bit Score: 41.56  E-value: 1.83e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 19921720 607 QLWTYDMDTQQISHRDTKLCLTLKAATnsrlqkvEKVVLSMeCDFKDITQKWGF 660
Cdd:cd23439  81 QLWKYRPNTKQLYHPVSGLCLDADPGS-------GKVFMNH-CDESSDTQKWTW 126
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 595-660 1.89e-04

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant8 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467339  Cd Length: 128  Bit Score: 41.62  E-value: 1.89e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921720 595 NVMLAQCASD-SSQLWTYDMDTQQ-ISHRDTKLCLTLkaatnsrlqKVEKVVLSME-CDFKDITQKWGF 660
Cdd:cd23461  68 NVRLSRCHYQgGNQYWKYDYETHQlINGGQNNKCLEA---------DVESLKITLSiCDSDNVEQKWKW 127
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 150-385 1.07e-03

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 41.20  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720   150 PSTSVIIVFHNEAwSVLLRTITSVInRSPRHLLkEIILVDDASDRSYLK------RQLESYVKVLAVPTRI--FRMKKRs 221
Cdd:pfam13641   2 PDVSVVVPAFNED-SVLGRVLEAIL-AQPYPPV-EVVVVVNPSDAETLDvaeeiaARFPDVRLRVIRNARLlgPTGKSR- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720   222 glvpARLLGAENARGDVLTFLDAHCECSRGWLEPLLSRIKESR-KVVICPVidiisddNFSYTKTFENHWGAFNWQLsfR 300
Cdd:pfam13641  78 ----GLNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKvGAVGTPV-------FSLNRSTMLSALGALEFAL--R 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720   301 WFSSDRKRQTAGnsskdstdpiaTPGMAGGLFAIDRKYFYEMGSYDsnmrVWG--GENVEMSFRIWQCGGRVEISPCSHV 378
Cdd:pfam13641 145 HLRMMSLRLALG-----------VLPLSGAGSAIRREVLKELGLFD----PFFllGDDKSLGRRLRRHGWRVAYAPDAAV 209


                  ....*..
gi 19921720   379 GHVFRSS 385
Cdd:pfam13641 210 RTVFPTY 216
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 524-638 1.50e-03

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: 39.26  E-value: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 524 DKCLrplkeDVPRSSLS---AVTVGDCTSHA-QSmdmFVITPKGQIMTNDNVCLTyrqqklgvIKMLKNRNATTsnVMLA 599
Cdd:cd23418  14 GRCL-----DVPGGSTTngtRLILWDCHGGAnQQ---FTFTSAGELRVGGDKCLD--------AAGGGTTNGTP--VVIW 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 19921720 600 QCASDSSQLWTYDMDTqQISHRDTKLCLTLK---AATNSRLQ 638
Cdd:cd23418  76 PCNGGANQKWRFNSDG-TIRNVNSGLCLDVAgggTANGTRLI 116
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 587-661 1.55e-03

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


Pssm-ID: 467334 [Multi-domain]  Cd Length: 122  Bit Score: 38.88  E-value: 1.55e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921720 587 KNRNATTSNVMLAQCASDSSQLWTYDmDTQQISHR-DTKLCLTLKAATNSRlqkvEKVVLSmECDfKDITQKWGFI 661
Cdd:cd23456  17 SGGATNGANVVVYDCNNSNSQKWYYD-ATGRLHSKaNPGKCLDAGGENSNG----ANVVLW-ACN-DSANQRWDFD 85
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 153-372 2.87e-03

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily 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: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 39.86  E-value: 2.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 153 SVIIVFHNEAwSVLLRTITSVINRSPRHLlkEIILVD-DASDRSYLKRQLESYVKVLAVPTRIFRMKkrsglvparlLGA 231
Cdd:cd02522   2 SIIIPTLNEA-ENLPRLLASLRRLNPLPL--EIIVVDgGSTDGTVAIARSAGVVVISSPKGRARQMN----------AGA 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 232 ENARGDVLTFLDAHCECSRGWLEPLLSRIKESRKVVICpvidiisddnFSYtkTFENHwGAFNWQLSFRWFSSDRKRQTA 311
Cdd:cd02522  69 AAARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGA----------FRL--RFDDP-GPRLRLLELGANLRSRLFGLP 135

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19921720 312 GnsskdstdpiatpgmaG--GLFaIDRKYFYEMGSYDSN--MrvwggENVEMSFRIWQCGGRVEI 372
Cdd:cd02522 136 Y----------------GdqGLF-IRRELFEELGGFPELplM-----EDVELVRRLRRRGRPALL 178
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 151-245 4.04e-03

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 39.54  E-value: 4.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 151 STSVIIVFHNEAWSVLLRTITSVINRSPrhllKEIILVDDASDRSYLKR--QLESYVKVLAVPTRifRMKKRSGLVparl 228
Cdd:cd06434   1 DVTVIIPVYDEDPDVFRECLRSILRQKP----LEIIVVTDGDDEPYLSIlsQTVKYGGIFVITVP--HPGKRRALA---- 70

                        90
                ....*....|....*..
gi 19921720 229 LGAENARGDVLTFLDAH 245
Cdd:cd06434  71 EGIRHVTTDIVVLLDSD 87
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 524-635 4.13e-03

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: 38.12  E-value: 4.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921720 524 DKCLrplkeDVPRSSLS---AVTVGDCTSHA-QsmdMFVITPKG----QIM-TNDNVCLTYRQqklgvikmlkNRNATTS 594
Cdd:cd00161  11 GKCL-----DVAGGSTAngaPVQQWTCNGGAnQ---QWTLTPVGdgyyTIRnVASGKCLDVAG----------GSTANGA 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 19921720 595 NVMLAQCASDSSQLWTYD---MDTQQISHRDTKLCLTLKAATNS 635
Cdd:cd00161  73 NVQQWTCNGGDNQQWRLEpvgDGYYRIVNKHSGKCLDVSGGSTA 116
beta-trefoil_Ricin_hemolysin cd23423
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ...
 596-658 4.54e-03

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


Pssm-ID: 467301 [Multi-domain]  Cd Length: 119  Bit Score: 37.36  E-value: 4.54e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921720 596 VMLAQC-ASDSSQLWTYDMDTQQISHRDTKLCLTlkAATNSRLqKVEKvvlsmeCDFKDiTQKW 658
Cdd:cd23423  25 VTLESCdSGDRNQSWILDSEGRYRSRVAPDLCLD--ADDDGLL-TLEQ------CSLSL-TQKW 78
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH