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Conserved domains on  [gi|1129973664|ref|XP_019744409|]
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PREDICTED: polypeptide N-acetylgalactosaminyltransferase 3 [Hippocampus comes]

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 ...
 198-503 2.31e-165

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: 474.39  E-value: 2.31e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 198 SVIIVFHNEAWSTLLRTVYSVLHTSPAILLKEIILVDDASADDVLKDELDEYLKA-LSIVRVVRQIERKGLITARLLGAS 276
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKyLPKVKVLRLKKREGLIRARIAGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 277 VATGDTLTFLDAHCECFHGWLEPLLARIAENSTAVVSPDISTIDLNTFEFMKPSPSgqnhNRGNFDWGLSFGWESLPDHE 356
Cdd:cd02510    81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGD----ARGGFDWSLHFKWLPLPEEE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 357 KnRRKDETYPIKTPTFAGGLFSISKEYFYHIGSYDEQMEIWGGENIEMSFRVWQCGGQLEIIPCSVVGHVFRTK-SPHTF 435
Cdd:cd02510   157 R-RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTF 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1129973664 436 PKGTQVIARNQVRLAEVWMDEYKEIFYRRNQQagqmAKDKTFGDVSKRVELRGRLQCKSFSWYLKNVY 503
Cdd:cd02510   236 PGGSGTVLRNYKRVAEVWMDEYKEYFYKARPE----LRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 512-639 1.33e-77

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: 242.79  E-value: 1.33e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 512 NPLRFGAVKNVGKDSCLDAGENNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNIQKELCLHGVQGPVKLEACQYKGRNT 591
Cdd:cd23468     1 NPLIFGAIKNVGKELCLDVGENNHGGKPLIMYNCHGLGGNQYFEYSTHHEIRHNIQKELCLHGSQGSVQLKECTYKGRNT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1129973664 592 AVGPEQKWQMQDNQLIYLPRSNMCLSARFEHPALTPCDPSDRYQLWAF 639
Cdd:cd23468    81 AVLPEEKWELQKDQLLYNPALNMCLSANGENPSLVPCNPSDPFQQWIF 128
 
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 ...
 198-503 2.31e-165

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: 474.39  E-value: 2.31e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 198 SVIIVFHNEAWSTLLRTVYSVLHTSPAILLKEIILVDDASADDVLKDELDEYLKA-LSIVRVVRQIERKGLITARLLGAS 276
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKyLPKVKVLRLKKREGLIRARIAGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 277 VATGDTLTFLDAHCECFHGWLEPLLARIAENSTAVVSPDISTIDLNTFEFMKPSPSgqnhNRGNFDWGLSFGWESLPDHE 356
Cdd:cd02510    81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGD----ARGGFDWSLHFKWLPLPEEE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 357 KnRRKDETYPIKTPTFAGGLFSISKEYFYHIGSYDEQMEIWGGENIEMSFRVWQCGGQLEIIPCSVVGHVFRTK-SPHTF 435
Cdd:cd02510   157 R-RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTF 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1129973664 436 PKGTQVIARNQVRLAEVWMDEYKEIFYRRNQQagqmAKDKTFGDVSKRVELRGRLQCKSFSWYLKNVY 503
Cdd:cd02510   236 PGGSGTVLRNYKRVAEVWMDEYKEYFYKARPE----LRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT3 cd23468
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 512-639 1.33e-77

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: 242.79  E-value: 1.33e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 512 NPLRFGAVKNVGKDSCLDAGENNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNIQKELCLHGVQGPVKLEACQYKGRNT 591
Cdd:cd23468     1 NPLIFGAIKNVGKELCLDVGENNHGGKPLIMYNCHGLGGNQYFEYSTHHEIRHNIQKELCLHGSQGSVQLKECTYKGRNT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1129973664 592 AVGPEQKWQMQDNQLIYLPRSNMCLSARFEHPALTPCDPSDRYQLWAF 639
Cdd:cd23468    81 AVLPEEKWELQKDQLLYNPALNMCLSANGENPSLVPCNPSDPFQQWIF 128
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 198-382 1.81e-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: 128.67  E-value: 1.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 198 SVIIVFHNEaWSTLLRTVYSVLHTSPaiLLKEIILVDDASADDvLKDELDEYLKALSIVRVVRQIERKGLITARLLGASV 277
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTY--PNFEIIVVDDGSTDG-TVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 278 ATGDTLTFLDAHCECFHGWLEPLLARIAENSTAVVSPDISTIDLNTFEFMKPSPsgqnhnrgnfdwglsFGWESLPDHEK 357
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASR---------------ITLSRLPFFLG 141

                         170       180
                  ....*....|....*....|....*
gi 1129973664 358 NRRKDETYPIKTPTFAGGLFSISKE 382
Cdd:pfam00535 142 LRLLGLNLPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
515-637 1.21e-25

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 102.22  E-value: 1.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 515 RFGAVKNVGKDSCLDAGENNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNIQkELCLHGVQ----GPVKLEACQYKGRN 590
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPGGSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVAS-DLCLDVGStadgAKVVLWPCHPGNGN 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1129973664 591 tavgpeQKWQMQ-DNQLIYLPRSNMCLSAR-----FEHPALTPCDPSDRYQLW 637
Cdd:pfam00652  80 ------QRWRYDeDGTQIRNPQSGKCLDVSgagtsNGKVILWTCDSGNPNQQW 126
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 195-312 4.80e-19

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 85.91  E-value: 4.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 195 PTTSVIIVFHNEAwSTLLRTVYSVLHTSPAILlkEIILVDDASADDVLkDELDEYLKALSIVRVVRQIERKGLITARLLG 274
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTA-EILRELAAKDPRIRVIRLERNRGKGAARNAG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1129973664 275 ASVATGDTLTFLDAHCECFHGWLEPLLARIAENSTAVV 312
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 521-640 1.09e-16

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 76.40  E-value: 1.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664  521 NVGKDSCLDAgenNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNiQKELCL---HGVQGPVKLEACQYKGRNtavgpeQ 597
Cdd:smart00458   3 SGNTGKCLDV---NGNKNPVGLFDCHGTGGNQLWKLTSDGAIRIK-DTDLCLtanGNTGSTVTLYSCDGTNDN------Q 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1129973664  598 KWQMQDNQLIYLPRSNMCLSARFE----HPALTPCDPSDrYQLWAFI 640
Cdd:smart00458  73 YWEVNKDGTIRNPDSGKCLDVKDGntgtKVILWTCSGNP-NQKWIFE 118
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 229-307 4.66e-05

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 45.81  E-value: 4.66e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129973664 229 EIILVDDASADDVLkDELDEYLKALSIVRVVRQiERKGLITARLLGASVATGDTLTFLDAHCECFHGWLEPLLArIAEN 307
Cdd:PRK10073   37 EIIIVNDGSTDNSV-EIAKHYAENYPHVRLLHQ-ANAGVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLMT-MALE 112
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 503-637 1.45e-04

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: 43.62  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 503 YPEVFMPDLNPLRFGAVKnvGKDS-CLDAGENNDGGKQLIMYPCHGlGGNQYFEFSTHHEIRhniQKELCLHGVQGPVKL 581
Cdd:NF035930  106 YPDYPGQGGGGWGGREIR--GKGGlCLDVSGGLRPGNGLIVYNCNG-GENQRFTWGRGGELR---VGDLCLDVADGNTRD 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1129973664 582 EA--CQYKGRNtavGPEQKWQMQDNQlIYLPRSNMCLS-----ARFEHPALT-PCDPSDRyQLW 637
Cdd:NF035930  180 GArvIAWSCSG---GPNQRWRWRGGQ-IRSRLSGKCLDieggrARPGQPVIVwSCNGGPN-QRW 238
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 198-503 2.31e-165

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: 474.39  E-value: 2.31e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 198 SVIIVFHNEAWSTLLRTVYSVLHTSPAILLKEIILVDDASADDVLKDELDEYLKA-LSIVRVVRQIERKGLITARLLGAS 276
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKyLPKVKVLRLKKREGLIRARIAGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 277 VATGDTLTFLDAHCECFHGWLEPLLARIAENSTAVVSPDISTIDLNTFEFMKPSPSgqnhNRGNFDWGLSFGWESLPDHE 356
Cdd:cd02510    81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGD----ARGGFDWSLHFKWLPLPEEE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 357 KnRRKDETYPIKTPTFAGGLFSISKEYFYHIGSYDEQMEIWGGENIEMSFRVWQCGGQLEIIPCSVVGHVFRTK-SPHTF 435
Cdd:cd02510   157 R-RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTF 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1129973664 436 PKGTQVIARNQVRLAEVWMDEYKEIFYRRNQQagqmAKDKTFGDVSKRVELRGRLQCKSFSWYLKNVY 503
Cdd:cd02510   236 PGGSGTVLRNYKRVAEVWMDEYKEYFYKARPE----LRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT3 cd23468
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 512-639 1.33e-77

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: 242.79  E-value: 1.33e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 512 NPLRFGAVKNVGKDSCLDAGENNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNIQKELCLHGVQGPVKLEACQYKGRNT 591
Cdd:cd23468     1 NPLIFGAIKNVGKELCLDVGENNHGGKPLIMYNCHGLGGNQYFEYSTHHEIRHNIQKELCLHGSQGSVQLKECTYKGRNT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1129973664 592 AVGPEQKWQMQDNQLIYLPRSNMCLSARFEHPALTPCDPSDRYQLWAF 639
Cdd:cd23468    81 AVLPEEKWELQKDQLLYNPALNMCLSANGENPSLVPCNPSDPFQQWIF 128
beta-trefoil_Ricin_GALNT6 cd23470
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 513-639 1.44e-60

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: 198.17  E-value: 1.44e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 513 PLRFGAVKNVGKDSCLDAGENNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNIQKELCLHGVQGPVKLEACQYKGRNTA 592
Cdd:cd23470     1 PTFYGAIKNEGTNQCLDVGENNRGGKPLIMYSCHGMGGNQYFEYTTHKELRHNIAKQLCLRVSKGPVQLGECHYKGKNSQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1129973664 593 VGPEQKWQMQDNQLIYLPRSNMCLSARFEHPALTPCDPSDRYQLWAF 639
Cdd:cd23470    81 VPPDEEWELTQDHLIRNSGSNMCLTARGKHPAMAPCNPADPHQLWSF 127
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 513-640 1.27e-51

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: 174.06  E-value: 1.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 513 PLRFGAVKNVGKDSCLDAGENN-DGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNIQKELCLH-GVQGPVKLEACQYKGRN 590
Cdd:cd23435     1 PGYYGALRNKGSELCLDVNNPNgQGGKPVIMYGCHGLGGNQYFEYTSKGEIRHNIGKELCLHaSGSDEVILQHCTSKGKD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1129973664 591 TAvgPEQKWQMQDNQLIYLPRSNMCLSARFEHPALTPCDPSDRYQLWAFI 640
Cdd:cd23435    81 VP--PEQKWLFTQDGTIRNPASGLCLHASGYKVLLRTCNPSDDSQKWTFI 128
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 198-382 1.81e-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: 128.67  E-value: 1.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 198 SVIIVFHNEaWSTLLRTVYSVLHTSPaiLLKEIILVDDASADDvLKDELDEYLKALSIVRVVRQIERKGLITARLLGASV 277
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTY--PNFEIIVVDDGSTDG-TVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 278 ATGDTLTFLDAHCECFHGWLEPLLARIAENSTAVVSPDISTIDLNTFEFMKPSPsgqnhnrgnfdwglsFGWESLPDHEK 357
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASR---------------ITLSRLPFFLG 141

                         170       180
                  ....*....|....*....|....*
gi 1129973664 358 NRRKDETYPIKTPTFAGGLFSISKE 382
Cdd:pfam00535 142 LRLLGLNLPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
515-637 1.21e-25

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 102.22  E-value: 1.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 515 RFGAVKNVGKDSCLDAGENNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNIQkELCLHGVQ----GPVKLEACQYKGRN 590
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPGGSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVAS-DLCLDVGStadgAKVVLWPCHPGNGN 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1129973664 591 tavgpeQKWQMQ-DNQLIYLPRSNMCLSAR-----FEHPALTPCDPSDRYQLW 637
Cdd:pfam00652  80 ------QRWRYDeDGTQIRNPQSGKCLDVSgagtsNGKVILWTCDSGNPNQQW 126
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 517-639 1.04e-24

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: 99.75  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 517 GAVKNVGKDSCLDA-GENNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNiqkELCL--HGVQGPVKLEACQYKGRNtav 593
Cdd:cd23462     6 GEIRNLAGKLCLDApGRKKELNKPVGLYPCHGQGGNQYWMLTKDGEIRRD---DLCLdyAGGSGDVTLYPCHGMKGN--- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1129973664 594 gpeQKWQM-QDNQLIYLPRSNMCLSARFEHPALT--PCDPSDRYQLWAF 639
Cdd:cd23462    80 ---QFWIYdEETKQIVHGTSKKCLELSDDSSKLVmePCNGSSPRQQWEF 125
beta-trefoil_Ricin_GALNT4 cd23469
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 517-639 4.06e-22

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: 92.66  E-value: 4.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 517 GAVKNVGKDS-CLD--AGENNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNIQKELCLHGVQGP--VKLEACQYKGrnT 591
Cdd:cd23469     5 GAVRSMGISSeCLDynSPEHNPTGAHLSLFGCHGQGGNQFFEYTSNKEIRFNSVTELCAEVPDQKnyIGMKHCPKDG--S 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1129973664 592 AVGPEQKWQMQDNQLIYLPRSNMCLSArFEHPALTP------CDPSDRYQLWAF 639
Cdd:cd23469    83 PVPANIIWHFKEDGTIYHPHSGMCISA-YRTPEGRAdvqmrtCDAGDKNQLWSF 135
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 517-639 1.27e-21

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: 90.82  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 517 GAVKNVGKDSCLDAGENNDGGKqLIMYPCHGLGGNQYFEFSTHHEIRHNiqkELCL--HGVQGPVKLEACqykgrntAVG 594
Cdd:cd23437     6 GEIRNLGTGLCLDTMGHQNGGP-VGLYPCHGMGGNQLFRLNEAGQLAVG---EQCLtaSGSGGKVKLRKC-------NLG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1129973664 595 PEQKWQ-MQDNQLIYLPRSNMCLSARF-EHPA-LTPCDPSDRYQLWAF 639
Cdd:cd23437    75 ETGKWEyDEATGQIRHKGTGKCLDLNEgTNKLiLQPCDSSSPSQKWEF 122
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 511-637 2.34e-21

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: 90.06  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 511 LNPLRFGAVKNVGKDSCLDAGENNDGGKqLIMYPCHGLGGNQYFEFSTHHEIRHNiqkELCLHGVQ--GPVKLEACQYKG 588
Cdd:cd23433     1 LDYYSLGEIRNVETNLCLDTMGRKAGEK-VGLSSCHGQGGNQVFSYTAKGEIRSD---DLCLDASRkgGPVKLEKCHGMG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1129973664 589 RNtavgpeQKWQ--MQDNQLIYLpRSNMCLSA----RFEHPALTPCDPSDrYQLW 637
Cdd:cd23433    77 GN------QEWEydKETKQIRHV-NSGLCLTApnedDPNEPVLRPCDGGP-SQKW 123
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 513-639 3.72e-19

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: 84.08  E-value: 3.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 513 PLRFGAVKNVG-KDSCLD---AGENNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNI-QKELCLHGVQGPVKLEACQYK 587
Cdd:cd23471     1 PGFFGMLKNKGmTNYCFDynpPDEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTrQPEGCAAVDAGTDFLTMHLCR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1129973664 588 GRNTAVGPEQKWQMQDNQLIYLPRSNMCLSA-RFEH-----PALTPCDPSDrYQLWAF 639
Cdd:cd23471    81 ENRQAVPENQKFIFREDGSLFHVQTQKCVQAvRNESsgspaPVLRPCTDSD-HQKWFF 137
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 195-312 4.80e-19

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 85.91  E-value: 4.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 195 PTTSVIIVFHNEAwSTLLRTVYSVLHTSPAILlkEIILVDDASADDVLkDELDEYLKALSIVRVVRQIERKGLITARLLG 274
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTA-EILRELAAKDPRIRVIRLERNRGKGAARNAG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1129973664 275 ASVATGDTLTFLDAHCECFHGWLEPLLARIAENSTAVV 312
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 510-640 1.69e-18

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: 81.98  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 510 DLNPLRFGAVKNVGKDSCLDA-GENNDGGKQLIMYPCH-GLGGNQYFEFSTHHEIRhniQKELCL---HGVQGPVKLEAC 584
Cdd:cd23459     1 DEDVLAYGQVRNPGTNLCLDTlQRDEDKGYNLGLYPCQgGLSSNQLFSLSKKGELR---REESCAdvqGTEESKVILITC 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 585 QykgrnTAVGPEQKWQMQDNQLIYLPRSNMCLSAR----FEHPALTPCDPSDrYQLWAFI 640
Cdd:cd23459    78 H-----GLEKFNQKWKHTKGGQIVHLASGKCLDAEglksGDDVTLAKCDGSL-SQKWTFE 131
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 199-312 1.94e-18

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: 82.55  E-value: 1.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 199 VIIVFHNEAwSTLLRTVYSVLHTSPAILlkEIILVDDASADDVLkDELDEYLKALSIVRVVRQIERKGLITARLLGASVA 278
Cdd:cd00761     1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTL-EILEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1129973664 279 TGDTLTFLDAHCECFHGWLEPLLARIAENSTAVV 312
Cdd:cd00761    77 RGEYILFLDADDLLLPDWLERLVAELLADPEADA 110
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 515-640 1.79e-17

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: 78.64  E-value: 1.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 515 RFGAVKNVGKDSCLDAGENNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNiqkELCLHGVQG-PVKLEACQYkgrntaV 593
Cdd:cd23460     1 GLGQIKHTESGLCLDWAGESNGDKTVALKPCHGGGGNQFWMYTGDGQIRQD---HLCLTADEGnKVTLRECAD------Q 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1129973664 594 GPEQKWQ--MQDNQLIYlPRSNMCLSAR--FEHPALTPCDPSDRYQLWAFI 640
Cdd:cd23460    72 LPSQEWSydEKTGTIRH-RSTGLCLTLDanNDVVILKECDSNSLWQKWIFQ 121
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
195-455 3.23e-17

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 80.42  E-value: 3.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 195 PTTSVIIVFHNEaWSTLLRTVYSVLHTSPAILlkEIILVDDASADDVLkdeldEYLKALSI--VRVVRQIERKGLITARL 272
Cdd:COG1216     3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTA-----ELLAALAFprVRVIRNPENLGFAAARN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 273 LGASVATGDTLTFLDAHCECFHGWLEPLLAriaenstavvspdistidlntfefmkpspsgqnhnrgnfdwglsfgwesl 352
Cdd:COG1216    75 LGLRAAGGDYLLFLDDDTVVEPDWLERLLA-------------------------------------------------- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 353 pdheknrrkdetypiktptfAGGLFsISKEYFYHIGSYDEQMEIWGGEnIEMSFRVWQCGGQLEIIPCSVVGHVFRtKSP 432
Cdd:COG1216   105 --------------------AACLL-IRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGG-ASS 161

                         250       260
                  ....*....|....*....|...
gi 1129973664 433 HTFPKgTQVIARNQVRLAEVWMD 455
Cdd:COG1216   162 GPLLR-AYYLGRNRLLFLRKHGP 183
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 521-640 1.09e-16

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 76.40  E-value: 1.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664  521 NVGKDSCLDAgenNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNiQKELCL---HGVQGPVKLEACQYKGRNtavgpeQ 597
Cdd:smart00458   3 SGNTGKCLDV---NGNKNPVGLFDCHGTGGNQLWKLTSDGAIRIK-DTDLCLtanGNTGSTVTLYSCDGTNDN------Q 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1129973664  598 KWQMQDNQLIYLPRSNMCLSARFE----HPALTPCDPSDrYQLWAFI 640
Cdd:smart00458  73 YWEVNKDGTIRNPDSGKCLDVKDGntgtKVILWTCSGNP-NQKWIFE 118
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 516-639 5.38e-16

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: 74.67  E-value: 5.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 516 FGAVKNvgKDSCLDAGENNDGGkQLIMYPCHGLGGNQYFEFSTHHEIRHniqKELCLHGVQG----PVKLEACQYKGRNt 591
Cdd:cd23434     2 FGSLKQ--GNLCLDTLGHKAGG-TVGLYPCHGTGGNQEWSFTKDGQIKH---DDLCLTVVDRapgsLVTLQPCREDDSN- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1129973664 592 avgpeQKWQMQD-NQLIYLPRSNMCLSARFEH---PALTPCDPSDRYQLWAF 639
Cdd:cd23434    75 -----QKWEQIEnNSKLRHVGSNLCLDSRNAKsggLTVETCDPSSGSQQWKF 121
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 192-312 2.81e-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: 77.09  E-value: 2.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 192 PRLPTTSVIIVFHNEAwSTLLRTVYSVLHTSPAILLKEIILVDDASADDVlKDELDEYLKALSIVRVVRQIERKGLITAR 271
Cdd:COG1215    26 ADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGSTDET-AEIARELAAEYPRVRVIERPENGGKAAAL 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1129973664 272 LLGASVATGDTLTFLDAHCECFHGWLEPLLARIAENSTAVV 312
Cdd:COG1215   104 NAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS 144
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 517-639 1.45e-12

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: 65.12  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 517 GAVKNVGKDS-CLDAgENNDGGKQLIMYPCHGL----GGNQYFEFSTHHEIRHNiQKELCLHGVQGPVKLEACQYKGRNt 591
Cdd:cd23461     4 GVIQSVAFPNlCLDI-LGRSHGGPPVLAKCSSNksmpGTFQNFSLTFHRQIKHG-TSDDCLEVRGNNVRLSRCHYQGGN- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1129973664 592 avgpeQKWQ--MQDNQLIYLPRSNMCLSARFEHPALT--PCDPSDRYQLWAF 639
Cdd:cd23461    81 -----QYWKydYETHQLINGGQNNKCLEADVESLKITlsICDSDNVEQKWKW 127
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 516-640 2.41e-11

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: 61.26  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 516 FGAVKNvgKDSCLDAGE-NNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRhniQKELCL----HGVQGPVKLEACqykgrn 590
Cdd:cd23441     5 YGQIKQ--GNLCLDSDEqLFQGPALLILAPCSNSSDSQEWSFTKDGQLQ---TQGLCLtvdsSSKDLPVVLETC------ 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1129973664 591 tAVGPEQKWQMQDNQLIYLPrSNMCL-SARFEHPALTPCDPSDRYQLWAFI 640
Cdd:cd23441    74 -SDDPKQKWTRTGRQLVHSE-SGLCLdSRKKKGLVVSPCRSGAPSQKWDFT 122
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 517-616 6.04e-11

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: 60.44  E-value: 6.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 517 GAVKNVGKDSCLD-AGENNDGGKQLIMYPCHGlGGNQYFEFSTHHEIRHNIQKELCLHGVQG----PVKLEACqykgrnt 591
Cdd:cd23418     6 GQIRGYGSGRCLDvPGGSTTNGTRLILWDCHG-GANQQFTFTSAGELRVGGDKCLDAAGGGTtngtPVVIWPC------- 77

                          90       100
                  ....*....|....*....|....*
gi 1129973664 592 AVGPEQKWQMQDNQLIYLPRSNMCL 616
Cdd:cd23418    78 NGGANQKWRFNSDGTIRNVNSGLCL 102
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 517-639 1.40e-10

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: 59.28  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 517 GAVKNVGKDSCLDAgENNDGGKQLIMYPC--HGLGGNQYFEFSTHHEIRHNIqKELCL----HGVQGPVKLEACQYKGRN 590
Cdd:cd23439     3 GEIRNVGSGLCIDT-KHGGENDEVRLSKCvkDGGGGEQQFELTWHEDIRPKK-RKVCFdvssHTPGAPVILYACHGMKGN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1129973664 591 tavgpeQKWQMQDNQL-IYLPRSNMCLSArfeHPA-----LTPCDPSDRYQLWAF 639
Cdd:cd23439    81 ------QLWKYRPNTKqLYHPVSGLCLDA---DPGsgkvfMNHCDESSDTQKWTW 126
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 516-637 4.39e-10

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: 57.75  E-value: 4.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 516 FGAVKNVGKDSCLDAGENNDGGKQLImYPCHGLGGNQYFEFSTHHEIRHNiqkELCL--HGVQGPVKLEACQYKGRNtav 593
Cdd:cd23466     6 LGEIRNVETNQCLDNMARKENEKVGI-FNCHGMGGNQVFSYTANKEIRTD---DLCLdvSKLNGPVMMLKCHHLKGN--- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1129973664 594 gpeQKWQMQDNQLIYLP-RSNMCLSARFEH----PALTPCDPSdRYQLW 637
Cdd:cd23466    79 ---QLWEYDPVKLTLLHvNSNQCLDKATEEdsqvPSIRDCNGS-RSQQW 123
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 516-637 5.82e-10

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: 57.35  E-value: 5.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 516 FGAVKNVGKDSCLDagenNDGGKQ---LIMYPCHGLGGNQYFEFSTHHEIRHNiqkELCLHG--VQGPVKLEACQYKGRN 590
Cdd:cd23467     6 LGEIRNVETNQCLD----NMGRKEnekVGIFNCHGMGGNQVFSYTADKEIRTD---DLCLDVsrLNGPVVMLKCHHMRGN 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1129973664 591 tavgpeQKWQMQDNQLIYLP-RSNMCLSARFEH----PALTPCDPSdRYQLW 637
Cdd:cd23467    79 ------QLWEYDAERLTLRHvNSNQCLDEPSEEdkmvPTMKDCSGS-RSQQW 123
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 517-637 4.53e-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: 54.75  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 517 GAVKNVGKDSCLDAGENND-GGKQLIMYPCHGLGGNQYFEFSTHHEIRHNIQkELCLHGVQGPVKLEACqykgrnTAVGP 595
Cdd:cd23442     6 GQLYNTGTGYCADYIHGWRlAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSL-QLCLDVRQEQVVLQNC------TKEKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1129973664 596 EQKWQMQDN-QLIYLPrSNMCLSA------RFEHpaLTPCDPSdRYQLW 637
Cdd:cd23442    79 SQKWDFQETgRIVHIL-SGKCIEAvesensKLLF--LSPCNGQ-RNQMW 123
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 199-312 1.78e-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: 54.50  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 199 VIIVFHNEAwSTLLRTVYSVLHTSPAILLKEIILVDDASADDVLkDELDEYLKALSIVRVVRQIERKGLITARLLGASVA 278
Cdd:cd04179     1 VVIPAYNEE-ENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTA-EIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAA 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1129973664 279 TGDTLTFLDA---HCECFhgwLEPLLARIAENSTAVV 312
Cdd:cd04179    79 RGDIVVTMDAdlqHPPED---IPKLLEKLLEGGADVV 112
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 199-400 2.55e-08

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: 54.99  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 199 VIIVFHNEAwSTLLRTVYSVLHTS-PAILLkEIILVDDASAD---DVLKDELDEYLKALSIVRVVRQiERKGLITARLLG 274
Cdd:cd04192     1 VVIAARNEA-ENLPRLLQSLSALDyPKEKF-EVILVDDHSTDgtvQILEFAAAKPNFQLKILNNSRV-SISGKKNALTTA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 275 ASVATGDTLTFLDAHCECFHGWLEPLLARIAENSTAVVSPDISTIDLNTFeFmkpspsgqnHNRGNFDW----GLSFGWE 350
Cdd:cd04192    78 IKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFKGKSL-L---------AKFQRLDWlsllGLIAGSF 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1129973664 351 SLpdheknrrkdetypiKTPTFAGGL-FSISKEYFYHIGSYDEQMEIWGGE 400
Cdd:cd04192   148 GL---------------GKPFMCNGAnMAYRKEAFFEVGGFEGNDHIASGD 183
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 198-428 2.80e-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: 55.32  E-value: 2.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 198 SVIIVFHNEAwSTLLRTVYSVLHTSPAILLKEIILVDDASADDVlKDELDEYLKALSIVRVvrqIERKGLI--TARLLGA 275
Cdd:cd02525     3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTDGT-REIVQEYAAKDPRIRL---IDNPKRIqsAGLNIGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 276 SVATGDTLTFLDAHCECFHGWLEPLLARIAENSTAVVSPDISTIDLNTFEFM-------KPSPSGQNHNRGNFDWGlsfg 348
Cdd:cd02525    78 RNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAiavaqssPLGSGGSAYRGGAVKIG---- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 349 weslpdheknrrkdetypiKTPTFAGGLFsiSKEYFYHIGSYDEQMEIwgGENIEMSFRVWQCGGQLEIIPCSVVGHVFR 428
Cdd:cd02525   154 -------------------YVDTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPR 210
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 512-639 5.37e-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: 51.99  E-value: 5.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 512 NPLRFGAVKNVGKDSCLDA-GENNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRhnIQKELCL---HGVQGPVKLEACqyk 587
Cdd:cd23440     1 KVIRKGQLKHAGSGLCLVAeDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELR--LANLLCLdssETSSDFPRLMKC--- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1129973664 588 grnTAVGPEQKWQMQDNQLIYLPRSNMCLSA----RFEHPALTPCDPSDRyQLWAF 639
Cdd:cd23440    76 ---HGSGGSQQWRFKKDNRLYNPASGQCLAAskngTSGYVTMDICSDSPS-QKWVF 127
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 365-430 8.75e-08

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: 49.53  E-value: 8.75e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1129973664 365 YPIKTPTFAGGLFSISKEYFYHIGSYDEQMEIWGGENIEMSFRVWQCGGQLEiIPCSVVGHVFRTK 430
Cdd:pfam02709  12 YKLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIE-RPPGDIGRYYMLY 76
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 517-599 1.63e-07

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 50.20  E-value: 1.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664  517 GAVKNVGKDSCLDAgeNNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRhNIQKELCLHGVQGPVKLEACQYKGRNtavGPE 596
Cdd:smart00458  39 GAIRIKDTDLCLTA--NGNTGSTVTLYSCDGTNDNQYWEVNKDGTIR-NPDSGKCLDVKDGNTGTKVILWTCSG---NPN 112


                   ...
gi 1129973664  597 QKW 599
Cdd:smart00458 113 QKW 115
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 517-618 6.68e-07

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: 48.48  E-value: 6.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 517 GAVKNVGKDSCLD-AGENNDGGKQLIMYPCHGlGGNQYFEFSTHHEIRhniQKELCLHGVQG------PVKLEACqykgr 589
Cdd:cd23451     3 GPVRLANAGKCLDvPGSSTADGNPVQIYTCNG-TAAQKWTLGTDGTLR---VLGKCLDVSGGgtangtLVQLWDC----- 73

                          90       100
                  ....*....|....*....|....*....
gi 1129973664 590 ntAVGPEQKWQMQDNQLIYLPRSNMCLSA 618
Cdd:cd23451    74 --NGTGAQKWVPRADGTLYNPQSGKCLDA 100
beta-trefoil_Ricin_GALNT5 cd23436
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 517-639 1.08e-06

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 5 (GALNT5) and similar proteins; GALNT5 (EC 2.4.1.41), also called polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, protein-UDP acetylgalactosaminyltransferase 5, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT5 has activity toward EA2 peptide substrate but has a weak activity toward Muc2 or Muc1b substrates. GALNT5 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467314  Cd Length: 132  Bit Score: 48.25  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 517 GAVKNVGKDSCLdAGENNDggkqLIMYPCHGLGGNQYFEFSTHHEIRHNiqkELCLHGV--QGPVKLEACQykGRNtavg 594
Cdd:cd23436     7 GLLVNVALRKCI-AIENTT----LTLQDCDLNNKSQHFNYTWLRLIRQG---ELCLAPVeaEGALTLHPCD--NTN---- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1129973664 595 PEQKW---------QMQDNQLIYLPRSNMCLSARFEHPAL--TPCDPSDRYQLWAF 639
Cdd:cd23436    73 NGLRWlhksliafpELMDHIMLEHQSQPTCLEADPSQKILrlNACDSFKRYQKWRF 128
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 516-637 3.27e-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: 46.98  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 516 FGAVKNVGKDSCLD-AGENNDGGKQLIMYPCHGlGGNQYFEF----STHHEIRhNIQKELCLhGVQG-------PVKLEA 583
Cdd:cd00161     2 TYRIVNAASGKCLDvAGGSTANGAPVQQWTCNG-GANQQWTLtpvgDGYYTIR-NVASGKCL-DVAGgstangaNVQQWT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1129973664 584 CQYkgrntavGPEQKWQMQDNQ----LIYLPRSNMCLSARFEHPA------LTPCDPSDrYQLW 637
Cdd:cd00161    79 CNG-------GDNQQWRLEPVGdgyyRIVNKHSGKCLDVSGGSTAnganvqQWTCNGGA-NQQW 134
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 229-312 7.96e-06

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: 47.53  E-value: 7.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 229 EIILVDDASADDVLkDELDEYLKALSIVRVVRQIERKGLITARLLGASVATGDTLTFLDA---HCECFhgwLEPLLARIA 305
Cdd:cd06442    29 EIIVVDDNSPDGTA-EIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDAdlsHPPEY---IPELLEAQL 104


                  ....*..
gi 1129973664 306 ENSTAVV 312
Cdd:cd06442   105 EGGADLV 111
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 229-287 4.04e-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: 44.89  E-value: 4.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1129973664 229 EIILVDDASADDVLKDELDEYLKALSIVRVVRQIERKGLITARLLGASVATGDTLTFLD 287
Cdd:cd04184    33 ELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALELATGEFVALLD 91
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 515-639 4.58e-05

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: 43.80  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 515 RFGAVKNVGKDSCLDAgENNDGGKQLIMYPC-HGLGG-----NQYFEFSTHHEIR-----HNiqKELCLHGVQ--GPVKL 581
Cdd:cd23476     6 AWGEIRNVGTGLCADT-KHGALGSPLRLEGCvKGRGEaawnnGQVFTFGWREDIRpgdpqHT--KKFCFDAIShnSPVTL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1129973664 582 EACQ-YKGrntavgpEQKWQMQDNQLIYLPRSNMCL--SARFEHPALTPCDPSDRYQLWAF 639
Cdd:cd23476    83 YDCHgMKG-------NQLWRYRKDKTLYHPVSNSCMdcSESDHRIFMNTCNPSSPTQQWLF 136
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 229-307 4.66e-05

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 45.81  E-value: 4.66e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129973664 229 EIILVDDASADDVLkDELDEYLKALSIVRVVRQiERKGLITARLLGASVATGDTLTFLDAHCECFHGWLEPLLArIAEN 307
Cdd:PRK10073   37 EIIIVNDGSTDNSV-EIAKHYAENYPHVRLLHQ-ANAGVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLMT-MALE 112
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 199-317 5.21e-05

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 44.09  E-value: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 199 VIIVFHNeAWSTLLRTVYSVLHTSPAILlkEIILVDDASADDvLKDELDEYLKalsIVRVVRQIERKGLITARLLGASVA 278
Cdd:cd04186     1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVDNASTDG-SVELLRELFP---EVRLIRNGENLGFGAGNNQGIREA 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1129973664 279 TGDTLTFLDAHCECFHGWLEPLLARIAENS-TAVVSPDIS 317
Cdd:cd04186    74 KGDYVLLLNPDTVVEPGALLELLDAAEQDPdVGIVGPKVS 113
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 194-288 5.99e-05

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: 44.88  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 194 LPTTSVIIVFHNEAwSTLLRTVYSVLHTS-PAILLkEIILVDDASAD---DVLKDELDEylkalsIVRVVRQIERKGLIT 269
Cdd:cd06439    28 LPTVTIIIPAYNEE-AVIEAKLENLLALDyPRDRL-EIIVVSDGSTDgtaEIAREYADK------GVKLLRFPERRGKAA 99

                          90
                  ....*....|....*....
gi 1129973664 270 ARLLGASVATGDTLTFLDA 288
Cdd:cd06439   100 ALNRALALATGEIVVFTDA 118
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 199-311 9.60e-05

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: 43.37  E-value: 9.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 199 VIIVFHNEAwSTLLRTVYSVLH-TSPAIllkEIILVDDASADDVLkDELDEYL-KALSIVRVVRQIERKGliTARLL--G 274
Cdd:cd06423     1 IIVPAYNEE-AVIERTIESLLAlDYPKL---EVIVVDDGSTDDTL-EILEELAaLYIRRVLVVRDKENGG--KAGALnaG 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1129973664 275 ASVATGDTLTFLDAHCECFHGWLEPLLARIAENSTAV 311
Cdd:cd06423    74 LRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVG 110
beta-trefoil_Ricin_RIPs_II_rpt1 cd23443
first ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ...
 522-618 1.35e-04

first ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating proteins (RIPs); Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. They consist of a catalytic A-chain which has rRNA N-glycosidase activity and a lectin B-chain containing two ricin B-type lectin domains 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 lectin chain facilitates the internalization of the catalytic chain on binding to the cell surface. The two chains are connected by a disulfide bridge. This model corresponds to the first ricin B-type lectin domain. Members of this subfamily includes Ricinus communis ricin, bitter gourd (Momordica charantia) seed lectin (BGSL), snake gourd (Trichosanthes anguina) seed lectin (SGSL), Sambucus ebulus ebulin I, Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf, Abrus precatorius abrin (ABR) and agglutinin-I (AAG), and Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs).


Pssm-ID: 467321 [Multi-domain]  Cd Length: 123  Bit Score: 41.89  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 522 VGKDS-CLD-AGENNDGGKQLIMYPCHGLGGNQYFEFSTHHEIRHNIQkelCL--HGVQG--PVKLEACqykgrNTAVGP 595
Cdd:cd23443     6 VGRDGlCVDvKDGYYSDGNPVILWPCKSQDANQLWTFKRDGTIRSNGK---CLttNGYSPgsYVVIYDC-----STAVAE 77

                          90       100
                  ....*....|....*....|...
gi 1129973664 596 EQKWQMQDNQLIYLPRSNMCLSA 618
Cdd:cd23443    78 ATKWEVSDDGTIINPASGLVLTA 100
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 503-637 1.45e-04

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: 43.62  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 503 YPEVFMPDLNPLRFGAVKnvGKDS-CLDAGENNDGGKQLIMYPCHGlGGNQYFEFSTHHEIRhniQKELCLHGVQGPVKL 581
Cdd:NF035930  106 YPDYPGQGGGGWGGREIR--GKGGlCLDVSGGLRPGNGLIVYNCNG-GENQRFTWGRGGELR---VGDLCLDVADGNTRD 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1129973664 582 EA--CQYKGRNtavGPEQKWQMQDNQlIYLPRSNMCLS-----ARFEHPALT-PCDPSDRyQLW 637
Cdd:NF035930  180 GArvIAWSCSG---GPNQRWRWRGGQ-IRSRLSGKCLDieggrARPGQPVIVwSCNGGPN-QRW 238
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 515-606 3.88e-04

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: 40.80  E-value: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 515 RFGAVKNVGKDSCLDAGENNDGGKQLIMYPCHGLGGNQYFEFSTHHeIRHNIQKELCLHGVQGP-----VKLEACQYKGR 589
Cdd:cd23456     1 KYFQLKSQASGLCLDVSGGATNGANVVVYDCNNSNSQKWYYDATGR-LHSKANPGKCLDAGGENsnganVVLWACNDSAN 79

                          90
                  ....*....|....*..
gi 1129973664 590 ntavgpeQKWQMQDNQL 606
Cdd:cd23456    80 -------QRWDFDGNFI 89
beta-trefoil_Ricin_AtEULS3-like cd23431
ricin B-type lectin domain, beta-trefoil fold, found in Arabidopsis thaliana Ricin B-like ...
 612-637 1.08e-03

ricin B-type lectin domain, beta-trefoil fold, found in Arabidopsis thaliana Ricin B-like lectin EULS3 (AtEULS3) and similar proteins; AtEULS3, also called euonymus lectin S3, is a Ricin B-like lectin that binds carbohydrates in vitro. It interacts through its lectin domain with glycan structures containing one or more Lewis X, Lewis Y or lactosamine motifs. It has been implicated in abiotic stress responses, abscisic acid-induced stomatal closure, as well as disease resistance against Pseudomonas syringae through its involvement in stomatal movement. All subfamily members 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 may harbor a sugar-binding pocket.


Pssm-ID: 467309  Cd Length: 152  Bit Score: 40.03  E-value: 1.08e-03
                          10        20
                  ....*....|....*....|....*.
gi 1129973664 612 SNMCLSARFEHPALTPCDPSDRYQLW 637
Cdd:cd23431    13 PGYNLTVRGGGVVLAPADPSDPYQLW 38
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 562-637 1.34e-03

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: 39.12  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 562 IRHNIQKeLCL--HGVQGPVKLEACqyKGRNtavgPEQKWQMQDNQLIYLPRSNMCLSARFEHPA----LTPCDPSDRYQ 635
Cdd:cd23385     5 IYNEDLG-KCLaaRSSSSKVSLSTC--NPNS----PNQQWKWTSGHRLFNVGTGKCLGVSSSSPSsplrLFECDSEDELQ 77


                  ..
gi 1129973664 636 LW 637
Cdd:cd23385    78 KW 79
beta-trefoil_Ricin_GALNTL6 cd23477
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 513-639 1.44e-03

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: 39.54  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129973664 513 PLRFGAVKNVGKDSCLDAgENNDGGKQLIMYPCHGLGGN------QYFEFSTHHEIR-----HNiqKELCLHGV--QGPV 579
Cdd:cd23477     4 PAAWGEIRNVAANLCVDS-KHGATGTELRLDICVKDGSErtwsheQLFTFGWREDIRpgeplHT--RKFCFDAIshNSPV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1129973664 580 KLEACQ-YKGrntavgpEQKWQMQDNQLIYLPRSNMCLSArfeHPA-----LTPCDPSDRYQLWAF 639
Cdd:cd23477    81 TLYDCHgMKG-------NQLWSYRKDKTLFHPVSNSCMDC---NPAdkkifMNRCDPLSETQQWIF 136
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 229-288 3.75e-03

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: 39.09  E-value: 3.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1129973664 229 EIILVDDASaddvlKDELDEYLKALS-----IVRVVRQIERKGLITARLLGASVATGDTLTFLDA 288
Cdd:cd04188    32 EIIVVDDGS-----KDGTAEVARKLArknpaLIRVLTLPKNRGKGGAVRAGMLAARGDYILFADA 91
beta-trefoil_Ricin_GALNT17 cd23474
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 512-549 8.23e-03

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


Pssm-ID: 467352  Cd Length: 142  Bit Score: 37.18  E-value: 8.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1129973664 512 NPLRFGAVKN-VGKDSCLDAG--ENNDGgkqlIMYPCHGLG 549
Cdd:cd23474     6 NTVAYGELRNnKAKDVCLDQGppENHTA----ILYPCHGWG 42
 
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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