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Conserved domains on  [gi|32698686|ref|NP_055383|]
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polypeptide N-acetylgalactosaminyltransferase 5 isoform 1 [Homo sapiens]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase( domain architecture ID 11551826)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 499-800 8.82e-179

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: 519.07  E-value: 8.82e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 499 SVIMCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTKDYLKDNLD-KYMSQFPKVRILRLKERHGLIRARLAGAQ 577
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEeYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 578 NATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDViaKN 657
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 658 RIKETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND-NPYSFPKD 736
Cdd:cd02510 159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFPGG 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32698686 737 rMKTVERNLVRVAEVWLDEYKELFYGHGDHLidQGLDVGNLTQQRELRKKLKCKSFKWYLENVF 800
Cdd:cd02510 239 -SGTVLRNYKRVAEVWMDEYKEYFYKARPEL--RNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT5 cd23436
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 806-938 1.95e-80

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 5 (GALNT5) and similar proteins; GALNT5 (EC 2.4.1.41), also called polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, protein-UDP acetylgalactosaminyltransferase 5, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, 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. GALNT5 has activity toward EA2 peptide substrate but has a weak activity toward Muc2 or Muc1b substrates. GALNT5 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: 467314  Cd Length: 132  Bit Score: 256.26  E-value: 1.95e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 806 PIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHK 885
Cdd:cd23436   1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32698686 886 STSVFhPELVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYY 938
Cdd:cd23436  81 SLIAF-PELMDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132
 
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 ...
 499-800 8.82e-179

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: 519.07  E-value: 8.82e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 499 SVIMCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTKDYLKDNLD-KYMSQFPKVRILRLKERHGLIRARLAGAQ 577
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEeYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 578 NATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDViaKN 657
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 658 RIKETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND-NPYSFPKD 736
Cdd:cd02510 159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFPGG 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32698686 737 rMKTVERNLVRVAEVWLDEYKELFYGHGDHLidQGLDVGNLTQQRELRKKLKCKSFKWYLENVF 800
Cdd:cd02510 239 -SGTVLRNYKRVAEVWMDEYKEYFYKARPEL--RNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT5 cd23436
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 806-938 1.95e-80

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 5 (GALNT5) and similar proteins; GALNT5 (EC 2.4.1.41), also called polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, protein-UDP acetylgalactosaminyltransferase 5, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, 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. GALNT5 has activity toward EA2 peptide substrate but has a weak activity toward Muc2 or Muc1b substrates. GALNT5 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: 467314  Cd Length: 132  Bit Score: 256.26  E-value: 1.95e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 806 PIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHK 885
Cdd:cd23436   1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32698686 886 STSVFhPELVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYY 938
Cdd:cd23436  81 SLIAF-PELMDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 499-679 6.89e-35

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: 130.59  E-value: 6.89e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686   499 SVIMCFVDEvWSTLLRSVHSVINRspPHLIKEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQN 578
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQ--TYPNFEIIVVDDGST-DGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686   579 ATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYmtvdnfqrgifvWPMNFGWRTIPPDVIAKNR 658
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY------------RRASRITLSRLPFFLGLRL 144

                         170       180
                  ....*....|....*....|.
gi 32698686   659 IKETDTIRCPVMAGGLFSIDK 679
Cdd:pfam00535 145 LGLNLPFLIGGFALYRREALE 165
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
810-932 5.01e-17

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 78.34  E-value: 5.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686   810 ASGVLINVALGKCISIE-----NTTVILEDCDGSKELQQFNYTWLRLIKC--GEWCIA--PIPDKGAVRLHPCDNRNKGL 880
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPggssaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDvgSTADGAKVVLWPCHPGNGNQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 32698686   881 KWLHKSTSvfhpelvNHIVfeNNQQLLCLEGNFSQKILK---VAACDPVKPYQKW 932
Cdd:pfam00652  81 RWRYDEDG-------TQIR--NPQSGKCLDVSGAGTSNGkviLWTCDSGNPNQQW 126
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
496-754 6.59e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 74.26  E-value: 6.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 496 PTTSVIMCFVDEvWSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYmsQFPKVRILRLKERHGLIRARLAG 575
Cdd:COG1216   3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGST-DGTAELLAAL--AFPRVRVIRNPENLGFAAARNLG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 576 AQNATGDVLTFLDSHVECNVGWLEPLLErvylsrkkVACpvievindkdmsymtvdnfqrgifvwpmnfgwrtippdvia 655
Cdd:COG1216  77 LRAAGGDYLLFLDDDTVVEPDWLERLLA--------AAC----------------------------------------- 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 656 knriketdtircpvmagglFSIDKSYFFELGTYDPGLDVWGGEnMELSFKVWMCGGEIEIIPCSRVGHIFRNDnpySFPK 735
Cdd:COG1216 108 -------------------LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGAS---SGPL 164

                       250
                ....*....|....*....
gi 32698686 736 DRMKTVERNLVRVAEVWLD 754
Cdd:COG1216 165 LRAYYLGRNRLLFLRKHGP 183
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 815-935 1.05e-14

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 71.39  E-value: 1.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686    815 INVALGKCISI--ENTTVILEDCDGSKELQQFNYTWLRLIKC--GEWCIAPIPDKGA-VRLHPCDNRNKGLKWLHKSTSV 889
Cdd:smart00458   2 ISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGStVTLYSCDGTNDNQYWEVNKDGT 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 32698686    890 FHpelvnhivfeNNQQLLCLEGNFSQKILKVAA--CDPvKPYQKWKFE 935
Cdd:smart00458  82 IR----------NPDSGKCLDVKDGNTGTKVILwtCSG-NPNQKWIFE 118
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 530-588 2.38e-05

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 47.35  E-value: 2.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32698686  530 EILLVDDFSTkDYLKDNLDKYMSQFPKVRILRlKERHGLIRARLAGAQNATGDVLTFLD 588
Cdd:PRK10073  37 EIIIVNDGST-DNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAVATGKYVAFPD 93
 
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 ...
 499-800 8.82e-179

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: 519.07  E-value: 8.82e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 499 SVIMCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTKDYLKDNLD-KYMSQFPKVRILRLKERHGLIRARLAGAQ 577
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEeYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 578 NATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDViaKN 657
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 658 RIKETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND-NPYSFPKD 736
Cdd:cd02510 159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFPGG 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32698686 737 rMKTVERNLVRVAEVWLDEYKELFYGHGDHLidQGLDVGNLTQQRELRKKLKCKSFKWYLENVF 800
Cdd:cd02510 239 -SGTVLRNYKRVAEVWMDEYKEYFYKARPEL--RNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT5 cd23436
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 806-938 1.95e-80

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 5 (GALNT5) and similar proteins; GALNT5 (EC 2.4.1.41), also called polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, protein-UDP acetylgalactosaminyltransferase 5, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, 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. GALNT5 has activity toward EA2 peptide substrate but has a weak activity toward Muc2 or Muc1b substrates. GALNT5 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: 467314  Cd Length: 132  Bit Score: 256.26  E-value: 1.95e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 806 PIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHK 885
Cdd:cd23436   1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32698686 886 STSVFhPELVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYY 938
Cdd:cd23436  81 SLIAF-PELMDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 499-679 6.89e-35

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: 130.59  E-value: 6.89e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686   499 SVIMCFVDEvWSTLLRSVHSVINRspPHLIKEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQN 578
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQ--TYPNFEIIVVDDGST-DGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686   579 ATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYmtvdnfqrgifvWPMNFGWRTIPPDVIAKNR 658
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY------------RRASRITLSRLPFFLGLRL 144

                         170       180
                  ....*....|....*....|.
gi 32698686   659 IKETDTIRCPVMAGGLFSIDK 679
Cdd:pfam00535 145 LGLNLPFLIGGFALYRREALE 165
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
810-932 5.01e-17

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 78.34  E-value: 5.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686   810 ASGVLINVALGKCISIE-----NTTVILEDCDGSKELQQFNYTWLRLIKC--GEWCIA--PIPDKGAVRLHPCDNRNKGL 880
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPggssaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDvgSTADGAKVVLWPCHPGNGNQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 32698686   881 KWLHKSTSvfhpelvNHIVfeNNQQLLCLEGNFSQKILK---VAACDPVKPYQKW 932
Cdd:pfam00652  81 RWRYDEDG-------TQIR--NPQSGKCLDVSGAGTSNGkviLWTCDSGNPNQQW 126
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
496-754 6.59e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 74.26  E-value: 6.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 496 PTTSVIMCFVDEvWSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYmsQFPKVRILRLKERHGLIRARLAG 575
Cdd:COG1216   3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGST-DGTAELLAAL--AFPRVRVIRNPENLGFAAARNLG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 576 AQNATGDVLTFLDSHVECNVGWLEPLLErvylsrkkVACpvievindkdmsymtvdnfqrgifvwpmnfgwrtippdvia 655
Cdd:COG1216  77 LRAAGGDYLLFLDDDTVVEPDWLERLLA--------AAC----------------------------------------- 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 656 knriketdtircpvmagglFSIDKSYFFELGTYDPGLDVWGGEnMELSFKVWMCGGEIEIIPCSRVGHIFRNDnpySFPK 735
Cdd:COG1216 108 -------------------LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGAS---SGPL 164

                       250
                ....*....|....*....
gi 32698686 736 DRMKTVERNLVRVAEVWLD 754
Cdd:COG1216 165 LRAYYLGRNRLLFLRKHGP 183
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 815-935 1.05e-14

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 71.39  E-value: 1.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686    815 INVALGKCISI--ENTTVILEDCDGSKELQQFNYTWLRLIKC--GEWCIAPIPDKGA-VRLHPCDNRNKGLKWLHKSTSV 889
Cdd:smart00458   2 ISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGStVTLYSCDGTNDNQYWEVNKDGT 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 32698686    890 FHpelvnhivfeNNQQLLCLEGNFSQKILKVAA--CDPvKPYQKWKFE 935
Cdd:smart00458  82 IR----------NPDSGKCLDVKDGNTGTKVILwtCSG-NPNQKWIFE 118
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 496-604 4.87e-14

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 72.04  E-value: 4.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 496 PTTSVIMCFVDEvWSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAG 575
Cdd:COG0463   2 PLVSVVIPTYNE-EEYLEEALESLLAQTYPDF--EIIVVDDGST-DGTAEILRELAAKDPRIRVIRLERNRGKGAARNAG 77

                        90       100
                ....*....|....*....|....*....
gi 32698686 576 AQNATGDVLTFLDSHVECNVGWLEPLLER 604
Cdd:COG0463  78 LAAARGDYIAFLDADDQLDPEKLEELVAA 106
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 493-728 5.25e-14

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: 74.01  E-value: 5.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 493 NNLPTTSVIMCFVDEvWSTLLRSVHSVINRSPPHLIKEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHGLIRAR 572
Cdd:COG1215  26 ADLPRVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIARELAAEYPRVRVIERPENGGKAAAL 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 573 LAGAQNATGDVLTFLDSHVECNVGWLEPLLErvYLSRKKVACPvievindkdmsymtvdnfqrgifvwpmnfgwrtippd 652
Cdd:COG1215 104 NAGLKAARGDIVVFLDADTVLDPDWLRRLVA--AFADPGVGAS------------------------------------- 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32698686 653 viaknriketdtircpvmaGGLFSIDKSYFFELGTYDPGLdvwGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND 728
Cdd:COG1215 145 -------------------GANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPET 198
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 500-614 1.11e-13

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: 69.46  E-value: 1.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 500 VIMCFVDEVwSTLLRSVHSVINRSPPHLikEILLVDDFSTKDYLKDnLDKYMSQFPKVRILRLKERHGLIRARLAGAQNA 579
Cdd:cd00761   1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTLEI-LEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 32698686 580 TGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVAC 614
Cdd:cd00761  77 RGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 808-934 1.15e-12

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: 65.78  E-value: 1.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 808 VRASGVLINVALGKCI----SIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGlKWL 883
Cdd:cd23437   2 NLAWGEIRNLGTGLCLdtmgHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETG-KWE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32698686 884 HkstsvfhpelvnhivFENNQQL------LCLEGNFSQKILKVAACDPVKPYQKWKF 934
Cdd:cd23437  81 Y---------------DEATGQIrhkgtgKCLDLNEGTNKLILQPCDSSSPSQKWEF 122
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 810-935 5.56e-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: 60.84  E-value: 5.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 810 ASGVLINVALGKCIS------IENTTVILEDCDGSKELQQFNYTWLRLIKCGEWC--IAPIPDKgaVRLHPCDNRNKGLK 881
Cdd:cd23462   4 AYGEIRNLAGKLCLDapgrkkELNKPVGLYPCHGQGGNQYWMLTKDGEIRRDDLCldYAGGSGD--VTLYPCHGMKGNQF 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 32698686 882 WLHKSTSvfhpelvNHIVFENNQqlLCLEGNFSQKILKVAACDPVKPYQKWKFE 935
Cdd:cd23462  82 WIYDEET-------KQIVHGTSK--KCLELSDDSSKLVMEPCNGSSPRQQWEFE 126
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 810-934 1.64e-09

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: 56.58  E-value: 1.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 810 ASGVLINVALGKCI----SIENTTVILEDC--DGSKELQQFNYTW---LRlIKCGEWCI-APIPDKGA-VRLHPCDNrNK 878
Cdd:cd23439   1 ASGEIRNVGSGLCIdtkhGGENDEVRLSKCvkDGGGGEQQFELTWhedIR-PKKRKVCFdVSSHTPGApVILYACHG-MK 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32698686 879 GLKW--LHKSTS-VFHPelVNHivfennqqlLCLEGNFSQKILKVAACDPVKPYQKWKF 934
Cdd:cd23439  79 GNQLwkYRPNTKqLYHP--VSG---------LCLDADPGSGKVFMNHCDESSDTQKWTW 126
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 496-589 2.76e-09

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: 57.98  E-value: 2.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 496 PTTSVIM--CFVDEVWstLLRSVHSVINRSPPHLikEILLVDDFSTKDYLKDNLDKYMSQFPKVRILRLKERHGLIRARL 573
Cdd:cd04184   1 PLISIVMpvYNTPEKY--LREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATN 76

                        90
                ....*....|....*.
gi 32698686 574 AGAQNATGDVLTFLDS 589
Cdd:cd04184  77 SALELATGEFVALLDH 92
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 810-934 1.09e-07

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: 51.64  E-value: 1.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 810 ASGVLINVAL-GKCISIENT----TVILEDCDGSK----ELQQFNYTWLRLIKCG--EWCIAPIPDKgaVRLHPCdnrnk 878
Cdd:cd23461   2 ASGVIQSVAFpNLCLDILGRshggPPVLAKCSSNKsmpgTFQNFSLTFHRQIKHGtsDDCLEVRGNN--VRLSRC----- 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 32698686 879 glkwlHKSTS--VFHPELVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKF 934
Cdd:cd23461  75 -----HYQGGnqYWKYDYETHQLINGGQNNKCLEADVESLKITLSICDSDNVEQKWKW 127
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 820-934 1.47e-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: 1.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 820 GKCI----SIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPI-PDKGA-VRLHPCDNRNKGLKWLHkstsvfhpe 893
Cdd:cd23434   9 NLCLdtlgHKAGGTVGLYPCHGTGGNQEWSFTKDGQIKHDDLCLTVVdRAPGSlVTLQPCREDDSNQKWEQ--------- 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32698686 894 lvnhivFENNQQL------LCLEG-NFSQKILKVAACDPVKPYQKWKF 934
Cdd:cd23434  80 ------IENNSKLrhvgsnLCLDSrNAKSGGLTVETCDPSSGSQQWKF 121
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 812-934 4.64e-07

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: 49.36  E-value: 4.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 812 GVLINVALGKCISI---ENT--TVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKgAVRLHPCDNRNKGLKWLHKS 886
Cdd:cd23460   3 GQIKHTESGLCLDWageSNGdkTVALKPCHGGGGNQFWMYTGDGQIRQDHLCLTADEGN-KVTLRECADQLPSQEWSYDE 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32698686 887 tsvfhpelvNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKF 934
Cdd:cd23460  82 ---------KTGTIRHRSTGLCLTLDANNDVVILKECDSNSLWQKWIF 120
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 512-589 5.69e-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: 50.65  E-value: 5.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 512 LLRSVHSVINRSPPHlikEILLVDDFSTkdylkDN----LDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFL 587
Cdd:cd04179  15 LVERLLAVLEEGYDY---EIIVVDDGST-----DGtaeiARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARGDIVVTM 86


                ..
gi 32698686 588 DS 589
Cdd:cd04179  87 DA 88
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 512-589 5.14e-06

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: 47.86  E-value: 5.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 512 LLRSVHSVINRSPPHLikEILLVDDFSTkdylkDN----LDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFL 587
Cdd:cd04187  15 LYERLKAVLESLGYDY--EIIFVDDGST-----DRtleiLRELAARDPRVKVIRLSRNFGQQAALLAGLDHARGDAVITM 87


                ..
gi 32698686 588 DS 589
Cdd:cd04187  88 DA 89
beta-trefoil_Ricin_GALNTL6 cd23477
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 806-936 1.71e-05

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase-like 6 (GALNTL6) and similar proteins; GALNTL6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 17, GalNAc-T17, pp-GaNTase 17, protein-UDP acetylgalactosaminyltransferase 17, putative polypeptide N-acetylgalactosaminyltransferase 17, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNTL6 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467355  Cd Length: 148  Bit Score: 45.70  E-value: 1.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 806 PIVRASGVLINVALGKCISIEN----TTVILEDC--DGSKEL----QQFNYTWLRLIKCGE------WCIAPIPDKGAVR 869
Cdd:cd23477   2 PPPAAWGEIRNVAANLCVDSKHgatgTELRLDICvkDGSERTwsheQLFTFGWREDIRPGEplhtrkFCFDAISHNSPVT 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32698686 870 LHPCDNRNKGLKWLH-KSTSVFHPelvnhivFENNqqllCLEGNFSQKILKVAACDPVKPYQKWKFEK 936
Cdd:cd23477  82 LYDCHGMKGNQLWSYrKDKTLFHP-------VSNS----CMDCNPADKKIFMNRCDPLSETQQWIFEH 138
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 530-588 2.38e-05

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 47.35  E-value: 2.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32698686  530 EILLVDDFSTkDYLKDNLDKYMSQFPKVRILRlKERHGLIRARLAGAQNATGDVLTFLD 588
Cdd:PRK10073  37 EIIIVNDGST-DNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAVATGKYVAFPD 93
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 518-723 5.10e-05

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: 45.69  E-value: 5.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 518 SVINRSPPHLIKEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHgLIRARLAGAQNATGDVLTFLDSHVECNVGW 597
Cdd:cd02525  21 SLLNQSYPKDLIEIIVVDGGST-DGTREIVQEYAAKDPRIRLIDNPKRI-QSAGLNIGIRNSRGDIIIRVDAHAVYPKDY 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 598 LEPLLErvYLSRKKVACpVIEVINDKDMSymtvdNFQRGIfVWPMNFGWRTIppdvIAKNRIKETDTIRCPVMAGGLFSi 677
Cdd:cd02525  99 ILELVE--ALKRTGADN-VGGPMETIGES-----KFQKAI-AVAQSSPLGSG----GSAYRGGAVKIGYVDTVHHGAYR- 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 32698686 678 dKSYFFELGTYDPGLDVwgGENMELSFKVWMCGGEIEIIPCSRVGH 723
Cdd:cd02525 165 -REVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYY 207
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 530-590 7.42e-05

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: 45.22  E-value: 7.42e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32698686 530 EILLVDDfSTKDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD---SH 590
Cdd:cd06442  29 EIIVVDD-NSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDadlSH 91
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 814-933 2.68e-04

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 41.43  E-value: 2.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 814 LINVALGKCISIENTT--VILEDCDGSKELQQFNYTW---LRLIKCGEwCIA--PIPDKGAVRLHPCDNRNKGLKWlhks 886
Cdd:cd23385   5 IYNEDLGKCLAARSSSskVSLSTCNPNSPNQQWKWTSghrLFNVGTGK-CLGvsSSSPSSPLRLFECDSEDELQKW---- 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32698686 887 tsvfhpELVNHIVFENNQQLLCLEGNFSQKILKVaaCDPVKPYQKWK 933
Cdd:cd23385  80 ------KCSKDGLLLLKGLGLLLLYDKSGKNVVV--SKGSGLSSRWK 118
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 671-725 4.17e-04

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


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 39.90  E-value: 4.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 32698686   671 AGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEiIPCSRVGHIF 725
Cdd:pfam02709  20 FGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIE-RPPGDIGRYY 73
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 830-935 4.37e-04

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: 41.16  E-value: 4.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 830 VILEDCDGSKELQQFNYTW---LRLIKCGEWCIAPIPDkGAVRLHPCDNRNKGL----KWLHK-STSVFHPelvnhivfe 901
Cdd:cd23435  29 VIMYGCHGLGGNQYFEYTSkgeIRHNIGKELCLHASGS-DEVILQHCTSKGKDVppeqKWLFTqDGTIRNP--------- 98

                        90       100       110
                ....*....|....*....|....*....|....
gi 32698686 902 nnQQLLCLEGnfSQKILKVAACDPVKPYQKWKFE 935
Cdd:cd23435  99 --ASGLCLHA--SGYKVLLRTCNPSDDSQKWTFI 128
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 826-935 5.93e-04

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: 40.46  E-value: 5.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 826 ENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGA--VRLHPCDNRNKgLKWLHKSTSVFHpelvnhivFENN 903
Cdd:cd23441  24 GPALLILAPCSNSSDSQEWSFTKDGQLQTQGLCLTVDSSSKDlpVVLETCSDDPK-QKWTRTGRQLVH--------SESG 94

                        90       100       110
                ....*....|....*....|....*....|..
gi 32698686 904 qqlLCLEgNFSQKILKVAACDPVKPYQKWKFE 935
Cdd:cd23441  95 ---LCLD-SRKKKGLVVSPCRSGAPSQKWDFT 122
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 500-599 5.95e-04

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 42.28  E-value: 5.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 500 VIMCFVDEVwSTLLRSVHSVINRSPPHLIKEILLVDDFS---TKDYLKDNLDKymsQFPKVRILRLKERH--GLIRARLA 574
Cdd:cd04192   1 VVIAARNEA-ENLPRLLQSLSALDYPKEKFEVILVDDHStdgTVQILEFAAAK---PNFQLKILNNSRVSisGKKNALTT 76

                        90       100
                ....*....|....*....|....*..
gi 32698686 575 GAQNATGDVLTFLDShvECNV--GWLE 599
Cdd:cd04192  77 AIKAAKGDWIVTTDA--DCVVpsNWLL 101
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 806-936 1.61e-03

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


Pssm-ID: 467354  Cd Length: 150  Bit Score: 39.94  E-value: 1.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 806 PIVRASGVLINVALGKCISIEN----TTVILEDCDGSK------ELQQFNYTWLRLIKCGE------WCIAPIPDKGAVR 869
Cdd:cd23476   2 PPAAAWGEIRNVGTGLCADTKHgalgSPLRLEGCVKGRgeaawnNGQVFTFGWREDIRPGDpqhtkkFCFDAISHNSPVT 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32698686 870 LHPCDNRNKGLKWLH-KSTSVFHPelvnhivFENNqqllCLEGNFSQKILKVAACDPVKPYQKWKFEK 936
Cdd:cd23476  82 LYDCHGMKGNQLWRYrKDKTLYHP-------VSNS----CMDCSESDHRIFMNTCNPSSPTQQWLFEH 138
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 509-614 2.06e-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: 39.85  E-value: 2.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 509 WSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKymsQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD 588
Cdd:cd04186   9 LEYLKACLDSLLAQTYPDF--EVIVVDNAST-DGSVELLRE---LFPEVRLIRNGENLGFGAGNNQGIREAKGDYVLLLN 82

                        90       100
                ....*....|....*....|....*.
gi 32698686 589 SHVECNVGWLEPLLERvYLSRKKVAC 614
Cdd:cd04186  83 PDTVVEPGALLELLDA-AEQDPDVGI 107
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 808-936 7.57e-03

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 1 (Pgant1) and similar proteins; Pgant1, also called pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant1 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers the monoglycosylated Muc5AC-3 as a substrate. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467337 [Multi-domain]  Cd Length: 132  Bit Score: 37.68  E-value: 7.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698686 808 VRASGVLINVALGKCISI----ENTTVILE--DCDGSKELQQ-FNYTWLRLIKCGEWCIAPIPDKGA-VRLHPCDNRNKG 879
Cdd:cd23459   4 VLAYGQVRNPGTNLCLDTlqrdEDKGYNLGlyPCQGGLSSNQlFSLSKKGELRREESCADVQGTEESkVILITCHGLEKF 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 32698686 880 L-KWLHKSTsvfhpelvNHIVFENNQQLLCLEGNFSQKILKVAACDPvKPYQKWKFEK 936
Cdd:cd23459  84 NqKWKHTKG--------GQIVHLASGKCLDAEGLKSGDDVTLAKCDG-SLSQKWTFEH 132
 
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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