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Conserved domains on  [gi|162951828|ref|NP_056551|]
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polypeptide N-acetylgalactosaminyltransferase 3 [Mus musculus]

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 ...
 188-493 5.50e-163

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: 468.22  E-value: 5.50e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 188 SVIIVFHNEAWSTLLRTVHSVLYSSPAILLKEIILVDDASVDDYLHEKLEEYIKQFS-IVKIVRQQERKGLITARLLGAA 266
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLpKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 267 VATAETLTFLDAHCECFYGWLEPLLARIAENYTAVVSPDIASIDLNTFEFNKpspyGSNHNRGNFDWSLSFGWESLPDHE 346
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRG----SSGDARGGFDWSLHFKWLPLPEEE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 347 KqRRKDETYPIKTPTFAGGLFSISKKYFEHIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSK-SPHTF 425
Cdd:cd02510  157 R-RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTF 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162951828 426 PKGTQVIARNQVRLAEVWMDEYKEIFYRRNTDAAKIvkqkSFGDLSKRFEIKKRLQCKNFTWYLNTIY 493
Cdd:cd02510  236 PGGSGTVLRNYKRVAEVWMDEYKEYFYKARPELRNI----DYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 502-630 4.52e-84

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


The actual alignment was detected with superfamily member cd23468:

Pssm-ID: 483949  Cd Length: 129  Bit Score: 259.36  E-value: 4.52e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 502 NPVISGYIKSVGQPLCLDVGENNQGGKPLILYTCHGLGGNQYFEYSAQREIRHNIQKELCLHATQGVVQLKACVYKGHRT 581
Cdd:cd23468    1 NPLIFGAIKNVGKELCLDVGENNHGGKPLIMYNCHGLGGNQYFEYSTHHEIRHNIQKELCLHGSQGSVQLKECTYKGRNT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 162951828 582 IAPGEQIWEIRKDQLLYNPLFKMCLSSNGEHPNLVPCDATDLLQKWIFS 630
Cdd:cd23468   81 AVLPEEKWELQKDQLLYNPALNMCLSANGENPSLVPCNPSDPFQQWIFR 129
 
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 ...
 188-493 5.50e-163

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: 468.22  E-value: 5.50e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 188 SVIIVFHNEAWSTLLRTVHSVLYSSPAILLKEIILVDDASVDDYLHEKLEEYIKQFS-IVKIVRQQERKGLITARLLGAA 266
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLpKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 267 VATAETLTFLDAHCECFYGWLEPLLARIAENYTAVVSPDIASIDLNTFEFNKpspyGSNHNRGNFDWSLSFGWESLPDHE 346
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRG----SSGDARGGFDWSLHFKWLPLPEEE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 347 KqRRKDETYPIKTPTFAGGLFSISKKYFEHIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSK-SPHTF 425
Cdd:cd02510  157 R-RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTF 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162951828 426 PKGTQVIARNQVRLAEVWMDEYKEIFYRRNTDAAKIvkqkSFGDLSKRFEIKKRLQCKNFTWYLNTIY 493
Cdd:cd02510  236 PGGSGTVLRNYKRVAEVWMDEYKEYFYKARPELRNI----DYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT3 cd23468
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 502-630 4.52e-84

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) and similar proteins; GALNT3 (EC 2.4.1.41), also called polypeptide GalNAc transferase 3, GalNAc-T3, pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, 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. 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. GALNT3 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: 467346  Cd Length: 129  Bit Score: 259.36  E-value: 4.52e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 502 NPVISGYIKSVGQPLCLDVGENNQGGKPLILYTCHGLGGNQYFEYSAQREIRHNIQKELCLHATQGVVQLKACVYKGHRT 581
Cdd:cd23468    1 NPLIFGAIKNVGKELCLDVGENNHGGKPLIMYNCHGLGGNQYFEYSTHHEIRHNIQKELCLHGSQGSVQLKECTYKGRNT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 162951828 582 IAPGEQIWEIRKDQLLYNPLFKMCLSSNGEHPNLVPCDATDLLQKWIFS 630
Cdd:cd23468   81 AVLPEEKWELQKDQLLYNPALNMCLSANGENPSLVPCNPSDPFQQWIFR 129
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 188-372 9.08e-34

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: 126.74  E-value: 9.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828  188 SVIIVFHNEaWSTLLRTVHSVLYSSPaiLLKEIILVDDASVDDyLHEKLEEYIKQFSIVKIVRQQERKGLITARLLGAAV 267
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTY--PNFEIIVVDDGSTDG-TVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828  268 ATAETLTFLDAHCECFYGWLEPLLARIAENYTAVVSPDIASIDLNTFEFNKPSPygsnhnrgnfdwslsFGWESLPDHEK 347
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASR---------------ITLSRLPFFLG 141

                         170       180
                  ....*....|....*....|....*
gi 162951828  348 QRRKDETYPIKTPTFAGGLFSISKK 372
Cdd:pfam00535 142 LRLLGLNLPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
506-627 7.89e-28

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 108.39  E-value: 7.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828  506 SGYIKSVGQPLCLDVGENNQGGKPLILYTCHGLGGNQYFEYSAQREIRHNIQkELCLHATQ----GVVQLKACVYKGhrt 581
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGGSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVAS-DLCLDVGStadgAKVVLWPCHPGN--- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 162951828  582 iapGEQIWEIRKD-QLLYNPLFKMCLSSNGEHPN-----LVPCDATDLLQKW 627
Cdd:pfam00652  78 ---GNQRWRYDEDgTQIRNPQSGKCLDVSGAGTSngkviLWTCDSGNPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 509-629 3.70e-20

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 86.41  E-value: 3.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828   509 IKSVGQPLCLDVgenNQGGKPLILYTCHGLGGNQYFEYSAQREIRHNiQKELCLHA---TQGVVQLKACVYKGhrtiapG 585
Cdd:smart00458   1 IISGNTGKCLDV---NGNKNPVGLFDCHGTGGNQLWKLTSDGAIRIK-DTDLCLTAngnTGSTVTLYSCDGTN------D 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 162951828   586 EQIWEIRKDQLLYNPLFKMCL----SSNGEHPNLVPCDATDlLQKWIF 629
Cdd:smart00458  71 NQYWEVNKDGTIRNPDSGKCLdvkdGNTGTKVILWTCSGNP-NQKWIF 117
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 185-302 3.32e-19

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 86.29  E-value: 3.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 185 PTTSVIIVFHNEAwSTLLRTVHSVLYSSPAILlkEIILVDDASVDDYLhEKLEEYIKQFSIVKIVRQQERKGLITARLLG 264
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTA-EILRELAAKDPRIRVIRLERNRGKGAARNAG 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 162951828 265 AAVATAETLTFLDAHCECFYGWLEPLLARIAENYTAVV 302
Cdd:COG0463   78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 493-567 8.17e-06

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


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 47.47  E-value: 8.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162951828 493 YPEAYVPDLNPVISGYIKSVGQpLCLDVGENNQGGKPLILYTCHGlGGNQYFEYSAQREIRhniQKELCLHATQG 567
Cdd:NF035930 106 YPDYPGQGGGGWGGREIRGKGG-LCLDVSGGLRPGNGLIVYNCNG-GENQRFTWGRGGELR---VGDLCLDVADG 175
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 219-297 1.18e-05

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 47.73  E-value: 1.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162951828 219 EIILVDDASVDDYLhEKLEEYIKQFSIVKIVrQQERKGLITARLLGAAVATAETLTFLDAHCECFYGWLEPLLArIAEN 297
Cdd:PRK10073  37 EIIIVNDGSTDNSV-EIAKHYAENYPHVRLL-HQANAGVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLMT-MALE 112
 
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 ...
 188-493 5.50e-163

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: 468.22  E-value: 5.50e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 188 SVIIVFHNEAWSTLLRTVHSVLYSSPAILLKEIILVDDASVDDYLHEKLEEYIKQFS-IVKIVRQQERKGLITARLLGAA 266
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLpKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 267 VATAETLTFLDAHCECFYGWLEPLLARIAENYTAVVSPDIASIDLNTFEFNKpspyGSNHNRGNFDWSLSFGWESLPDHE 346
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRG----SSGDARGGFDWSLHFKWLPLPEEE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 347 KqRRKDETYPIKTPTFAGGLFSISKKYFEHIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSK-SPHTF 425
Cdd:cd02510  157 R-RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTF 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162951828 426 PKGTQVIARNQVRLAEVWMDEYKEIFYRRNTDAAKIvkqkSFGDLSKRFEIKKRLQCKNFTWYLNTIY 493
Cdd:cd02510  236 PGGSGTVLRNYKRVAEVWMDEYKEYFYKARPELRNI----DYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT3 cd23468
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 502-630 4.52e-84

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) and similar proteins; GALNT3 (EC 2.4.1.41), also called polypeptide GalNAc transferase 3, GalNAc-T3, pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, 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. 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. GALNT3 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: 467346  Cd Length: 129  Bit Score: 259.36  E-value: 4.52e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 502 NPVISGYIKSVGQPLCLDVGENNQGGKPLILYTCHGLGGNQYFEYSAQREIRHNIQKELCLHATQGVVQLKACVYKGHRT 581
Cdd:cd23468    1 NPLIFGAIKNVGKELCLDVGENNHGGKPLIMYNCHGLGGNQYFEYSTHHEIRHNIQKELCLHGSQGSVQLKECTYKGRNT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 162951828 582 IAPGEQIWEIRKDQLLYNPLFKMCLSSNGEHPNLVPCDATDLLQKWIFS 630
Cdd:cd23468   81 AVLPEEKWELQKDQLLYNPALNMCLSANGENPSLVPCNPSDPFQQWIFR 129
beta-trefoil_Ricin_GALNT6 cd23470
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 503-630 4.62e-55

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 6 (GALNT6) and similar proteins; GALNT6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 6, GalNAc-T6, pp-GaNTase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6, 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. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT6 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 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: 467348  Cd Length: 128  Bit Score: 183.15  E-value: 4.62e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 503 PVISGYIKSVGQPLCLDVGENNQGGKPLILYTCHGLGGNQYFEYSAQREIRHNIQKELCLHATQGVVQLKACVYKGHRTI 582
Cdd:cd23470    1 PTFYGAIKNEGTNQCLDVGENNRGGKPLIMYSCHGMGGNQYFEYTTHKELRHNIAKQLCLRVSKGPVQLGECHYKGKNSQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 162951828 583 APGEQIWEIRKDQLLYNPLFKMCLSSNGEHPNLVPCDATDLLQKWIFS 630
Cdd:cd23470   81 VPPDEEWELTQDHLIRNSGSNMCLTARGKHPAMAPCNPADPHQLWSFS 128
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 503-629 8.73e-49

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: 166.35  E-value: 8.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 503 PVISGYIKSVGQPLCLDVGENN-QGGKPLILYTCHGLGGNQYFEYSAQREIRHNIQKELCLHATQGV-VQLKACVYKGHR 580
Cdd:cd23435    1 PGYYGALRNKGSELCLDVNNPNgQGGKPVIMYGCHGLGGNQYFEYTSKGEIRHNIGKELCLHASGSDeVILQHCTSKGKD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 162951828 581 tiAPGEQIWEIRKDQLLYNPLFKMCLSSNGEHPNLVPCDATDLLQKWIF 629
Cdd:cd23435   81 --VPPEQKWLFTQDGTIRNPASGLCLHASGYKVLLRTCNPSDDSQKWTF 127
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 188-372 9.08e-34

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: 126.74  E-value: 9.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828  188 SVIIVFHNEaWSTLLRTVHSVLYSSPaiLLKEIILVDDASVDDyLHEKLEEYIKQFSIVKIVRQQERKGLITARLLGAAV 267
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTY--PNFEIIVVDDGSTDG-TVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828  268 ATAETLTFLDAHCECFYGWLEPLLARIAENYTAVVSPDIASIDLNTFEFNKPSPygsnhnrgnfdwslsFGWESLPDHEK 347
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASR---------------ITLSRLPFFLG 141

                         170       180
                  ....*....|....*....|....*
gi 162951828  348 QRRKDETYPIKTPTFAGGLFSISKK 372
Cdd:pfam00535 142 LRLLGLNLPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
506-627 7.89e-28

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 108.39  E-value: 7.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828  506 SGYIKSVGQPLCLDVGENNQGGKPLILYTCHGLGGNQYFEYSAQREIRHNIQkELCLHATQ----GVVQLKACVYKGhrt 581
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGGSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVAS-DLCLDVGStadgAKVVLWPCHPGN--- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 162951828  582 iapGEQIWEIRKD-QLLYNPLFKMCLSSNGEHPN-----LVPCDATDLLQKW 627
Cdd:pfam00652  78 ---GNQRWRYDEDgTQIRNPQSGKCLDVSGAGTSngkviLWTCDSGNPNQQW 126
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 506-630 5.04e-26

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: 103.21  E-value: 5.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 506 SGYIKSVGQPLCLDV-GENNQGGKPLILYTCHGLGGNQYFEYSAQREIRHNiqkELCL--HATQGVVQLKACvykgHRTi 582
Cdd:cd23462    5 YGEIRNLAGKLCLDApGRKKELNKPVGLYPCHGQGGNQYWMLTKDGEIRRD---DLCLdyAGGSGDVTLYPC----HGM- 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 162951828 583 aPGEQIWE-IRKDQLLYNPLFKMCL--SSNGEHPNLVPCDATDLLQKWIFS 630
Cdd:cd23462   77 -KGNQFWIyDEETKQIVHGTSKKCLelSDDSSKLVMEPCNGSSPRQQWEFE 126
beta-trefoil_Ricin_GALNT4 cd23469
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 507-629 2.48e-21

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 4 (GALNT4) and similar proteins; GALNT4 (EC 2.4.1.41), also called polypeptide GalNAc transferase 4, GalNAc-T4, pp-GaNTase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT4 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: 467347  Cd Length: 136  Bit Score: 90.34  E-value: 2.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 507 GYIKSVG-QPLCLDVG--ENNQGGKPLILYTCHGLGGNQYFEYSAQREIRHNIQKELCLHATQGV--VQLKACVYKGHRT 581
Cdd:cd23469    5 GAVRSMGiSSECLDYNspEHNPTGAHLSLFGCHGQGGNQFFEYTSNKEIRFNSVTELCAEVPDQKnyIGMKHCPKDGSPV 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162951828 582 iaPGEQIWEIRKDQLLYNPLFKMCLSS--NGE-HPN--LVPCDATDLLQKWIF 629
Cdd:cd23469   85 --PANIIWHFKEDGTIYHPHSGMCISAyrTPEgRADvqMRTCDAGDKNQLWSF 135
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 507-629 2.06e-20

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: 87.11  E-value: 2.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 507 GYIKSVGQPLCLDVGENNQGGKPLILYTCHGLGGNQYFEYSAQREIRHNiqkELCLHATQGV-VQLKACVYKGhrtiapG 585
Cdd:cd23460    3 GQIKHTESGLCLDWAGESNGDKTVALKPCHGGGGNQFWMYTGDGQIRQD---HLCLTADEGNkVTLRECADQL------P 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 162951828 586 EQIWEIR-KDQLLYNPLFKMCL--SSNGEHPNLVPCDATDLLQKWIF 629
Cdd:cd23460   74 SQEWSYDeKTGTIRHRSTGLCLtlDANNDVVILKECDSNSLWQKWIF 120
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 509-629 3.70e-20

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 86.41  E-value: 3.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828   509 IKSVGQPLCLDVgenNQGGKPLILYTCHGLGGNQYFEYSAQREIRHNiQKELCLHA---TQGVVQLKACVYKGhrtiapG 585
Cdd:smart00458   1 IISGNTGKCLDV---NGNKNPVGLFDCHGTGGNQLWKLTSDGAIRIK-DTDLCLTAngnTGSTVTLYSCDGTN------D 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 162951828   586 EQIWEIRKDQLLYNPLFKMCL----SSNGEHPNLVPCDATDlLQKWIF 629
Cdd:smart00458  71 NQYWEVNKDGTIRNPDSGKCLdvkdGNTGTKVILWTCSGNP-NQKWIF 117
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 502-631 2.18e-19

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: 84.27  E-value: 2.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 502 NPVISGYIKSVGQPLCLDVGENNQGGkPLILYTCHGLGGNQYFEYSAQREIRHNiqkELCLHA--TQGVVQLKACVykgh 579
Cdd:cd23437    1 KNLAWGEIRNLGTGLCLDTMGHQNGG-PVGLYPCHGMGGNQLFRLNEAGQLAVG---EQCLTAsgSGGKVKLRKCN---- 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162951828 580 rtiAPGEQIWE-IRKDQLLYNPLFKMCLSSNGE--HPNLVPCDATDLLQKWIFSQ 631
Cdd:cd23437   73 ---LGETGKWEyDEATGQIRHKGTGKCLDLNEGtnKLILQPCDSSSPSQKWEFNE 124
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 185-302 3.32e-19

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 86.29  E-value: 3.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 185 PTTSVIIVFHNEAwSTLLRTVHSVLYSSPAILlkEIILVDDASVDDYLhEKLEEYIKQFSIVKIVRQQERKGLITARLLG 264
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTA-EILRELAAKDPRIRVIRLERNRGKGAARNAG 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 162951828 265 AAVATAETLTFLDAHCECFYGWLEPLLARIAENYTAVV 302
Cdd:COG0463   78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 189-315 6.49e-19

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: 84.09  E-value: 6.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 189 VIIVFHNEAwSTLLRTVHSVLYSSPAILlkEIILVDDASVDDYLhEKLEEYIKQFSIVKIVRQQERKGLITARLLGAAVA 268
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTL-EILEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 162951828 269 TAETLTFLDAHCECFYGWLEPLLARIAEN--YTAVVSPDIASIDLNTFE 315
Cdd:cd00761   77 RGEYILFLDADDLLLPDWLERLVAELLADpeADAVGGPGNLLFRRELLE 125
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
185-445 3.89e-18

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 83.12  E-value: 3.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 185 PTTSVIIVFHNEaWSTLLRTVHSVLYSSPAILlkEIILVDDASVDDYLhEKLEEYikQFSIVKIVRQQERKGLITARLLG 264
Cdd:COG1216    3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTA-ELLAAL--AFPRVRVIRNPENLGFAAARNLG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 265 AAVATAETLTFLDAHCECFYGWLEPLLAriaenytavvspdiasidlntfefnkpspygsnhnrgnfdwslsfgweslpd 344
Cdd:COG1216   77 LRAAGGDYLLFLDDDTVVEPDWLERLLA---------------------------------------------------- 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 345 hekqrrkdetypiktptfAGGLFsISKKYFEHIGSYDEEMEIWGGEnIEMSFRVWQCGGQLEIMPCSVVGHVfRSKSPHT 424
Cdd:COG1216  105 ------------------AACLL-IRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHL-GGASSGP 163

                        250       260
                 ....*....|....*....|.
gi 162951828 425 FPKgTQVIARNQVRLAEVWMD 445
Cdd:COG1216  164 LLR-AYYLGRNRLLFLRKHGP 183
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 500-629 4.97e-16

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: 75.05  E-value: 4.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 500 DLNPVISGYIKSVGQPLCLD-VGENNQGGKPLILYTCH-GLGGNQYFEYSAQREIRhniQKELCLHATQGV---VQLKAC 574
Cdd:cd23459    1 DEDVLAYGQVRNPGTNLCLDtLQRDEDKGYNLGLYPCQgGLSSNQLFSLSKKGELR---REESCADVQGTEeskVILITC 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162951828 575 vykgHRTiAPGEQIWEIRKDQLLYNPLFKMCLSS----NGEHPNLVPCDAtDLLQKWIF 629
Cdd:cd23459   78 ----HGL-EKFNQKWKHTKGGQIVHLASGKCLDAeglkSGDDVTLAKCDG-SLSQKWTF 130
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 507-631 7.33e-16

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


Pssm-ID: 467349  Cd Length: 140  Bit Score: 74.83  E-value: 7.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 507 GYIKSVG-QPLCLDVG---ENNQGGKPLILYTCHGLGGNQYFEYSAQREIRHNI-QKELCLHATQGVVQLKACVYKGHRT 581
Cdd:cd23471    5 GMLKNKGmTNYCFDYNppdEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTrQPEGCAAVDAGTDFLTMHLCRENRQ 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 162951828 582 IAPGEQIWEIRKDQLLYNPLFKMCL------SSNGEHPNLVPCDATDlLQKWIFSQ 631
Cdd:cd23471   85 AVPENQKFIFREDGSLFHVQTQKCVqavrneSSGSPAPVLRPCTDSD-HQKWFFKE 139
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 507-629 1.25e-15

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: 73.50  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 507 GYIKSVGQPLCLDVGENNQGGKPLIlYTCHGLGGNQYFEYSAQREIRHNiqkELCLHATQ--GVVQLKACvykgHRTiaP 584
Cdd:cd23433    7 GEIRNVETNLCLDTMGRKAGEKVGL-SSCHGQGGNQVFSYTAKGEIRSD---DLCLDASRkgGPVKLEKC----HGM--G 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 162951828 585 GEQIWEirkdqllYNP---LFK-----MCLS-SNGEHPNLV---PCDAtDLLQKWIF 629
Cdd:cd23433   77 GNQEWE-------YDKetkQIRhvnsgLCLTaPNEDDPNEPvlrPCDG-GPSQKWEL 125
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 182-302 1.62e-15

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: 77.86  E-value: 1.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 182 PPLPTTSVIIVFHNEAwSTLLRTVHSVLYSSPAILLKEIILVDDASVDDYLhEKLEEYIKQFSIVKIVRQQERKGLITAR 261
Cdd:COG1215   26 ADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETA-EIARELAAEYPRVRVIERPENGGKAAAL 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 162951828 262 LLGAAVATAETLTFLDAHCECFYGWLEPLLARIAENYTAVV 302
Cdd:COG1215  104 NAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS 144
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 506-630 6.61e-13

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: 65.89  E-value: 6.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 506 SGYIKSVGQP-LCLDVgENNQGGKPLILYTCHGL----GGNQYFEYSAQREIRHNiQKELCLHATQGVVQLKACVYKGhr 580
Cdd:cd23461    3 SGVIQSVAFPnLCLDI-LGRSHGGPPVLAKCSSNksmpGTFQNFSLTFHRQIKHG-TSDDCLEVRGNNVRLSRCHYQG-- 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 162951828 581 tiapGEQIW--EIRKDQLLYNPLFKMCLSSNGEHPN--LVPCDATDLLQKWIFS 630
Cdd:cd23461   79 ----GNQYWkyDYETHQLINGGQNNKCLEADVESLKitLSICDSDNVEQKWKWG 128
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 506-629 2.60e-12

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: 64.29  E-value: 2.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 506 SGYIKSVGQPLCLDVgENNQGGKPLILYTC--HGLGGNQYFEYSAQREIRHNIqKELCLHATQGV----VQLKACvYKGH 579
Cdd:cd23439    2 SGEIRNVGSGLCIDT-KHGGENDEVRLSKCvkDGGGGEQQFELTWHEDIRPKK-RKVCFDVSSHTpgapVILYAC-HGMK 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162951828 580 rtiapGEQIWEIRKDQL-LYNPLFKMCLSSNGEHPNLV--PCDATDLLQKWIF 629
Cdd:cd23439   79 -----GNQLWKYRPNTKqLYHPVSGLCLDADPGSGKVFmnHCDESSDTQKWTW 126
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 506-629 3.33e-12

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: 63.49  E-value: 3.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 506 SGYIKSVGqpLCLD-VGenNQGGKPLILYTCHGLGGNQYFEYSAQREIRHniqKELCLHATQGV----VQLKACVYKGHR 580
Cdd:cd23434    2 FGSLKQGN--LCLDtLG--HKAGGTVGLYPCHGTGGNQEWSFTKDGQIKH---DDLCLTVVDRApgslVTLQPCREDDSN 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162951828 581 tiapgeQIWE-IRKDQLLYNPLFKMCLSSNGEHPNLV---PCDATDLLQKWIF 629
Cdd:cd23434   75 ------QKWEqIENNSKLRHVGSNLCLDSRNAKSGGLtveTCDPSSGSQQWKF 121
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 506-629 1.02e-10

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: 59.67  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 506 SGYIKSVGQPLCLDVGENNQG-GKPLILYTCHGlGGNQYFEYSAQREIRHNIQKelCLHATQGVVQLKACVykghrTIAP 584
Cdd:cd23418    5 GGQIRGYGSGRCLDVPGGSTTnGTRLILWDCHG-GANQQFTFTSAGELRVGGDK--CLDAAGGGTTNGTPV-----VIWP 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162951828 585 ----GEQIWEIRKDQLLYNPLFKMCL------SSNGEHPNLVPCDATDlLQKWIF 629
Cdd:cd23418   77 cnggANQKWRFNSDGTIRNVNSGLCLdvagggTANGTRLILWSCNGGS-NQRWRR 130
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 507-629 1.03e-09

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 13 (GALNT13) and similar proteins; GALNT13 (EC 2.4.1.41), also called polypeptide GalNAc transferase 13, GalNAc-T13, pp-GaNTase 13, protein-UDP acetylgalactosaminyltransferase 13, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It 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. GALNT13 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). The 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: 467345  Cd Length: 127  Bit Score: 56.96  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 507 GYIKSVGQPLCLD-VG--ENNQGGkpliLYTCHGLGGNQYFEYSAQREIRHNiqkELCLHATQ--GVVQLKACVYkghrt 581
Cdd:cd23467    7 GEIRNVETNQCLDnMGrkENEKVG----IFNCHGMGGNQVFSYTADKEIRTD---DLCLDVSRlnGPVVMLKCHH----- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162951828 582 iAPGEQIWEIRKDQL-LYNPLFKMCLSSNGEHPNLVP----CDATDlLQKWIF 629
Cdd:cd23467   75 -MRGNQLWEYDAERLtLRHVNSNQCLDEPSEEDKMVPtmkdCSGSR-SQQWLL 125
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 506-593 2.68e-09

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 15 (GALNT15) and similar proteins; GALNT15 (EC 2.4.1.41), also called polypeptide GalNAc transferase 15, GalNAc-T15, polypeptide GalNAc transferase-like protein 2, GalNAc-T-like protein 2, pp-GaNTase-like protein 2, polypeptide N-acetylgalactosaminyltransferase-like protein 2, protein-UDP acetylgalactosaminyltransferase-like protein 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, GALNT15 can transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. It prefers Muc1a as its substrate. GALNT15 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467320 [Multi-domain]  Cd Length: 124  Bit Score: 55.52  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 506 SGYIKSVGQPLCLDVGENNQ-GGKPLILYTCHGLGGNQYFEYSAQREIRHNIQkELCLHATQGVVQLKACvykghrTIAP 584
Cdd:cd23442    5 SGQLYNTGTGYCADYIHGWRlAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSL-QLCLDVRQEQVVLQNC------TKEK 77


                 ....*....
gi 162951828 585 GEQIWEIRK 593
Cdd:cd23442   78 TSQKWDFQE 86
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 507-629 8.46e-09

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1) and similar proteins; GALNT1 (EC 2.4.1.41), also called polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT1 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 is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates.


Pssm-ID: 467344  Cd Length: 127  Bit Score: 54.28  E-value: 8.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 507 GYIKSVGQPLCLD---VGENNQGGkpliLYTCHGLGGNQYFEYSAQREIRHNiqkELCLHATQ--GVVQLKACVYkghrt 581
Cdd:cd23466    7 GEIRNVETNQCLDnmaRKENEKVG----IFNCHGMGGNQVFSYTANKEIRTD---DLCLDVSKlnGPVMMLKCHH----- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162951828 582 iAPGEQIWEIRKDQL-LYNPLFKMCLSSNGEHPNLVP----CDATDlLQKWIF 629
Cdd:cd23466   75 -LKGNQLWEYDPVKLtLLHVNSNQCLDKATEEDSQVPsirdCNGSR-SQQWLL 125
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 188-420 1.72e-08

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: 55.70  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 188 SVIIVFHNEAwSTLLRTVHSVLYSSPAILLKEIILVDDASVDDYLhEKLEEYIKQFSIVKIVrQQERKGLITARLLGAAV 267
Cdd:cd02525    3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTDGTR-EIVQEYAAKDPRIRLI-DNPKRIQSAGLNIGIRN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 268 ATAETLTFLDAHCECFYGWLEPLLARIAENYTAVVSPDIASIDLNTFEFN-------KPSPYGSNHNRGnfdwslsfgwe 340
Cdd:cd02525   80 SRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAiavaqssPLGSGGSAYRGG----------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 341 slpdhekqrRKDETYpikTPTFAGGLFsiSKKYFEHIGSYDEEMEIwgGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSK 420
Cdd:cd02525  149 ---------AVKIGY---VDTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPRST 212
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 189-302 2.47e-08

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: 54.12  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 189 VIIVFHNEAwSTLLRTVHSVLYSSPAILLKEIILVDDASVDDYLhEKLEEYIKQFSIVKIVRQQERKGLITARLLGAAVA 268
Cdd:cd04179    1 VVIPAYNEE-ENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTA-EIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAA 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 162951828 269 TAETLTFLDA---HCECFygwLEPLLARIAENYTAVV 302
Cdd:cd04179   79 RGDIVVTMDAdlqHPPED---IPKLLEKLLEGGADVV 112
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 502-629 8.52e-08

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 11 (GALNT11) and similar proteins; GALNT11 (EC 2.4.1.41), also called polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes its activation, modulating the balance between motile and immotile (sensory) cilia at the left-right organizer (LRO). GALNT11 displays the same enzyme activity toward MUC1, MUC4, and EA2 as GALNT1. It is not involved in glycosylation of erythropoietin (EPO). GALNT11 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467318 [Multi-domain]  Cd Length: 127  Bit Score: 51.22  E-value: 8.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 502 NPVISGYIKSVGQPLCLDV-GENNQGGKPLILYTCHGLGGNQYFEYSAQREIRhnIQKELCL---HATQGVVQLKACVYK 577
Cdd:cd23440    1 KVIRKGQLKHAGSGLCLVAeDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELR--LANLLCLdssETSSDFPRLMKCHGS 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 162951828 578 GhrtiapGEQIWEIRKDQLLYNPLFKMCLSS--NGEHPNLVP--CDaTDLLQKWIF 629
Cdd:cd23440   79 G------GSQQWRFKKDNRLYNPASGQCLAAskNGTSGYVTMdiCS-DSPSQKWVF 127
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 189-278 1.11e-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: 52.23  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 189 VIIVFHNEAwSTLLRTVHSVL---YSspailLKEIILVDDASVDDYLHEKLEEYIKQFSIVKIVRQQERKGliTARLLGA 265
Cdd:cd06423    1 IIVPAYNEE-AVIERTIESLLaldYP-----KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGG--KAGALNA 72

                         90
                 ....*....|....*
gi 162951828 266 AVATAET--LTFLDA 278
Cdd:cd06423   73 GLRHAKGdiVVVLDA 87
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 355-412 1.20e-07

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: 49.15  E-value: 1.20e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 162951828  355 YPIKTPTFAGGLFSISKKYFEHIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSV 412
Cdd:pfam02709  12 YKLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPGDI 69
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 189-303 4.75e-07

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: 51.14  E-value: 4.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 189 VIIVFHNEAwSTLLRTVHSVL---YssPAILLkEIILVDDASVDDYlhEKLEEYIKQFSI--VKIVRQQER--KGLITAR 261
Cdd:cd04192    1 VVIAARNEA-ENLPRLLQSLSaldY--PKEKF-EVILVDDHSTDGT--VQILEFAAAKPNfqLKILNNSRVsiSGKKNAL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 162951828 262 LLGAAVATAETLTFLDAHCECFYGWLEPLLARIAENYTAVVS 303
Cdd:cd04192   75 TTAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVA 116
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 183-278 5.15e-07

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: 51.43  E-value: 5.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 183 PLPTTSVIIVFHNEAwSTLLRTVHSVL---YSSPAIllkEIILVDDASVDDYLhEKLEEYIKQfsIVKIVRQQERKGLIT 259
Cdd:cd06439   27 YLPTVTIIIPAYNEE-AVIEAKLENLLaldYPRDRL---EIIVVSDGSTDGTA-EIAREYADK--GVKLLRFPERRGKAA 99

                         90
                 ....*....|....*....
gi 162951828 260 ARLLGAAVATAETLTFLDA 278
Cdd:cd06439  100 ALNRALALATGEIVVFTDA 118
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 189-415 7.07e-07

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: 49.48  E-value: 7.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 189 VIIVFHNeAWSTLLRTVHSVLYSSPAILlkEIILVDDASVDDYLhEKLEEyikQFSIVKIVRQQERKGLITARLLGAAVA 268
Cdd:cd04186    1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVDNASTDGSV-ELLRE---LFPEVRLIRNGENLGFGAGNNQGIREA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 269 TAETLTFLDAHCECFYGWLEPLLARIAENytavvsPDIASIdlntfefnkpspygsnhnrgnfdwslsfgweslpdhekq 348
Cdd:cd04186   74 KGDYVLLLNPDTVVEPGALLELLDAAEQD------PDVGIV--------------------------------------- 108

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162951828 349 rrkdetypikTPTFAGGLFSISKKYFEHIGSYDEEMEIWgGENIEMSFRVWQCGGQLEIMPCSVVGH 415
Cdd:cd04186  109 ----------GPKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYH 164
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 507-633 8.09e-07

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: 49.19  E-value: 8.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 507 GYIKSVGQPLCLDVgENNQGGKPLILYTC-HGLGG-----NQYFEYSAQREIR-----HNiqKELCLHATQ--GVVQLKA 573
Cdd:cd23476    8 GEIRNVGTGLCADT-KHGALGSPLRLEGCvKGRGEaawnnGQVFTFGWREDIRpgdpqHT--KKFCFDAIShnSPVTLYD 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162951828 574 CvyKGHRtiapGEQIWEIRKDQLLYNPLFKMCLS-SNGEHPNLV-PCDATDLLQKWIFSQND 633
Cdd:cd23476   85 C--HGMK----GNQLWRYRKDKTLYHPVSNSCMDcSESDHRIFMnTCNPSSPTQQWLFEHTN 140
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 506-627 3.51e-06

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467329 [Multi-domain]  Cd Length: 125  Bit Score: 46.56  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 506 SGYIKSVGQPLCLDV-GENNQGGKPLILYTCHGlGGNQYFEYSAQREIRhniQKELCLHATQG------VVQLKACvykg 578
Cdd:cd23451    2 TGPVRLANAGKCLDVpGSSTADGNPVQIYTCNG-TAAQKWTLGTDGTLR---VLGKCLDVSGGgtangtLVQLWDC---- 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162951828 579 HRTIApgeQIWEIRKDQLLYNPLFKMCLSSNGEHPN------LVPCDATDlLQKW 627
Cdd:cd23451   74 NGTGA---QKWVPRADGTLYNPQSGKCLDAPGGSTTdgtqlqLYTCNGTA-AQQW 124
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 506-627 3.67e-06

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: 46.59  E-value: 3.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 506 SGYIKSVGQPLCLDV-GENNQGGKPLILYTCHGlGGNQYFEYSAQR----EIRhNIQKELCLHATQG------VVQLKAC 574
Cdd:cd00161    2 TYRIVNAASGKCLDVaGGSTANGAPVQQWTCNG-GANQQWTLTPVGdgyyTIR-NVASGKCLDVAGGstangaNVQQWTC 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162951828 575 VYKGHrtiapgeQIWEIRKDQ----LLYNPLFKMCL------SSNGEHPNLVPCDATDlLQKW 627
Cdd:cd00161   80 NGGDN-------QQWRLEPVGdgyyRIVNKHSGKCLdvsggsTANGANVQQWTCNGGA-NQQW 134
beta-trefoil_Ricin_GALNTL6 cd23477
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 503-629 4.53e-06

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: 46.85  E-value: 4.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 503 PVISGYIKSVGQPLCLDvGENNQGGKPLILYTCHGLGGN------QYFEYSAQREIR-----HNiqKELCLHAT--QGVV 569
Cdd:cd23477    4 PAAWGEIRNVAANLCVD-SKHGATGTELRLDICVKDGSErtwsheQLFTFGWREDIRpgeplHT--RKFCFDAIshNSPV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162951828 570 QLKACvyKGHRtiapGEQIWEIRKDQLLYNPLFKMCLSSNGEHPNLV--PCDATDLLQKWIF 629
Cdd:cd23477   81 TLYDC--HGMK----GNQLWSYRKDKTLFHPVSNSCMDCNPADKKIFmnRCDPLSETQQWIF 136
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 509-579 6.82e-06

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: 45.81  E-value: 6.82e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162951828 509 IKSVGQPLCLDVGENNQGGKPLILYTCHGLgGNQYFEYSAQREIRHNIQKELCLHATQ-----GVVQLKACVYKGH 579
Cdd:cd23456    5 LKSQASGLCLDVSGGATNGANVVVYDCNNS-NSQKWYYDATGRLHSKANPGKCLDAGGensngANVVLWACNDSAN 79
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 552-627 6.90e-06

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: 45.67  E-value: 6.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 552 IRHNIQKeLCLHATQ--GVVQLKACVYKGHRtiapgeQIWEIRKDQLLYNPLFKMCLSSNGEHPN----LVPCDATDLLQ 625
Cdd:cd23385    5 IYNEDLG-KCLAARSssSKVSLSTCNPNSPN------QQWKWTSGHRLFNVGTGKCLGVSSSSPSsplrLFECDSEDELQ 77


                 ..
gi 162951828 626 KW 627
Cdd:cd23385   78 KW 79
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 493-567 8.17e-06

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


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 47.47  E-value: 8.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162951828 493 YPEAYVPDLNPVISGYIKSVGQpLCLDVGENNQGGKPLILYTCHGlGGNQYFEYSAQREIRhniQKELCLHATQG 567
Cdd:NF035930 106 YPDYPGQGGGGWGGREIRGKGG-LCLDVSGGLRPGNGLIVYNCNG-GENQRFTWGRGGELR---VGDLCLDVADG 175
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 516-630 9.55e-06

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467319 [Multi-domain]  Cd Length: 122  Bit Score: 45.09  E-value: 9.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 516 LCLDVGE-NNQGGKPLILYTCHGLGGNQYFEYSAQREIRhniQKELCLHATQG----VVQLKACvykghrtIAPGEQIWE 590
Cdd:cd23441   13 LCLDSDEqLFQGPALLILAPCSNSSDSQEWSFTKDGQLQ---TQGLCLTVDSSskdlPVVLETC-------SDDPKQKWT 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 162951828 591 iRKDQLLYNPLFKMCL-SSNGEHPNLVPCDATDLLQKWIFS 630
Cdd:cd23441   83 -RTGRQLVHSESGLCLdSRKKKGLVVSPCRSGAPSQKWDFT 122
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 219-297 1.18e-05

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 47.73  E-value: 1.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162951828 219 EIILVDDASVDDYLhEKLEEYIKQFSIVKIVrQQERKGLITARLLGAAVATAETLTFLDAHCECFYGWLEPLLArIAEN 297
Cdd:PRK10073  37 EIIIVNDGSTDNSV-EIAKHYAENYPHVRLL-HQANAGVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLMT-MALE 112
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 185-277 3.70e-05

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: 45.27  E-value: 3.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 185 PTTSVIIVFHNEAWSTLLRTVHSVL---YSSpaillKEIILVDDASVDDYLHEKLEEYIKQFSIVKIVRQQERKGLITAR 261
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRaqtYPN-----WELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAAT 75

                         90
                 ....*....|....*.
gi 162951828 262 LLGAAVATAETLTFLD 277
Cdd:cd04184   76 NSALELATGEFVALLD 91
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 219-278 4.81e-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: 4.81e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 219 EIILVDDASVDDYLhEKLEEYIKQFSIVKIVRQQERKGLITARLLGAAVATAETLTFLDA 278
Cdd:cd06442   29 EIIVVDDNSPDGTA-EIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDA 87
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 189-278 6.74e-04

DPG_synthase is involved in protein N-linked glycosylation; 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.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 41.40  E-value: 6.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 189 VIIVFHNEAwSTLLRTVHSVLYSSPAILLK--EIILVDDASVDDYLhEKLEEYIKQF-SIVKIVRQQERKGLITARLLGA 265
Cdd:cd04188    1 VVIPAYNEE-KRLPPTLEEAVEYLEERPSFsyEIIVVDDGSKDGTA-EVARKLARKNpALIRVLTLPKNRGKGGAVRAGM 78

                         90
                 ....*....|...
gi 162951828 266 AVATAETLTFLDA 278
Cdd:cd04188   79 LAARGDYILFADA 91
beta-trefoil_Ricin_MRC1 cd23407
ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 1 (MRC1) ...
 594-627 4.70e-03

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 1 (MRC1) and similar proteins; MRC1, also called MMR, C-type lectin domain family 13 member D (CLEC13D), C-type lectin domain family 13 member D-like (CLEC13DL), macrophage mannose receptor 1-like protein 1 (MRC1L1), or CD206, mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains. MRC1 acts as phagocytic receptor for bacteria, fungi and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC1 contains 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.


Pssm-ID: 467785  Cd Length: 123  Bit Score: 37.35  E-value: 4.70e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 162951828 594 DQLLYNPLFKMCL----SSNGEHPNLVPCDATDLLQKW 627
Cdd:cd23407   41 GSQILSVAFKLCLgvpsKKDWVTVTLFPCNEKSELQKW 78
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 188-324 6.60e-03

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 38.45  E-value: 6.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162951828 188 SVII-VFHNEAWSTLLRTVHSVLYSSpaILLKEIILVDDASVDDYLHEKLEEYIKQFSIvKIVRQQERKGLITARLLGAA 266
Cdd:cd04195    1 SVLMsVYIKEKPEFLREALESILKQT--LPPDEVVLVKDGPVTQSLNEVLEEFKRKLPL-KVVPLEKNRGLGKALNEGLK 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 162951828 267 VATAETLTFLDAHCECFYGWLEPLLARIAENYTAvvspDIASIDLNTFEFNkPSPYGS 324
Cdd:cd04195   78 HCTYDWVARMDTDDISLPDRFEKQLDFIEKNPEI----DIVGGGVLEFDSD-GNDIGK 130
 
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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