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Conserved domains on  [gi|975830122|ref|NP_001305980|]
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polypeptide N-acetylgalactosaminyltransferase 15 isoform 2 [Homo sapiens]

Protein Classification

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 ...
 194-493 6.47e-160

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


:

Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 459.75  E-value: 6.47e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 194 SVILCFHDEAWSTLLRTVHSILDTVPRAFLKEIILVDDLSQQGQLKSALSEYVAR-LEGVKLLRSNKRLGAIRARMLGAT 272
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKyLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 273 RATGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVVSPVIDVIDWKTFQYYPSKDLQRGVLDWKLDFHWEPLPEHVRKAl 352
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEERRR- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 353 QSPISPIRSPVVPGEVVAMDRHYFQNTGAYDSLMSLRGGENLELSFKAWLCGGSVEILPCSRVGHIYQNQDS--HSPLDQ 430
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKRKpyTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 975830122 431 EATLRNRVRIAETWLGSFKETFYKHSPEAFslsKAEKPDCMERLQLQRRLGCRTFHWFLANVY 493
Cdd:cd02510  240 GTVLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 502-591 7.75e-36

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 cd23442:

Pssm-ID: 483949 [Multi-domain]  Cd Length: 124  Bit Score: 130.64  E-value: 7.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 502 RPSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpQHLCFAVRQEQVILQNCTEEgla 581
Cdd:cd23442    1 APYFSGQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGS-LQLCLDVRQEQVVLQNCTKE--- 76

                         90
                 ....*....|
gi 975830122 582 IHQQHWDFQE 591
Cdd:cd23442   77 KTSQKWDFQE 86
 
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 ...
 194-493 6.47e-160

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 459.75  E-value: 6.47e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 194 SVILCFHDEAWSTLLRTVHSILDTVPRAFLKEIILVDDLSQQGQLKSALSEYVAR-LEGVKLLRSNKRLGAIRARMLGAT 272
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKyLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 273 RATGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVVSPVIDVIDWKTFQYYPSKDLQRGVLDWKLDFHWEPLPEHVRKAl 352
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEERRR- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 353 QSPISPIRSPVVPGEVVAMDRHYFQNTGAYDSLMSLRGGENLELSFKAWLCGGSVEILPCSRVGHIYQNQDS--HSPLDQ 430
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKRKpyTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 975830122 431 EATLRNRVRIAETWLGSFKETFYKHSPEAFslsKAEKPDCMERLQLQRRLGCRTFHWFLANVY 493
Cdd:cd02510  240 GTVLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 502-591 7.75e-36

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: 130.64  E-value: 7.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 502 RPSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpQHLCFAVRQEQVILQNCTEEgla 581
Cdd:cd23442    1 APYFSGQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGS-LQLCLDVRQEQVVLQNCTKE--- 76

                         90
                 ....*....|
gi 975830122 582 IHQQHWDFQE 591
Cdd:cd23442   77 KTSQKWDFQE 86
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 194-349 1.17e-31

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: 120.58  E-value: 1.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122  194 SVILCFHDEaWSTLLRTVHSILDTVPRAFlkEIILVDDLSQQGqLKSALSEYVARLEGVKLLRSNKRLGAIRARMLGATR 273
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGSTDG-TVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 975830122  274 ATGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVVSPVIDVIDWKTFQYYPSKDLQRGVLDWKLDFHWEPLPEHVR 349
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFL 152
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 180-304 1.58e-17

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 83.64  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 180 LCLQQHPQDSLPTASVILCFHDEAwSTLLRTVHSILDTVPRAFLKEIILVDDLSQQGqLKSALSEYVARLEGVKLLRSNK 259
Cdd:COG1215   18 LARRRRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGSTDE-TAEIARELAAEYPRVRVIERPE 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 975830122 260 RLGAIRARMLGATRATGDVLVFMDAHCECHPGWLEPLLSRIAGDR 304
Cdd:COG1215   96 NGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG 140
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
505-592 5.61e-12

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 63.32  E-value: 5.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122  505 FSGKLHNTGLGLCADCQAeGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQhLCFAVRQE----QVILQNCTEEGl 580
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPG-GSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVASD-LCLDVGSTadgaKVVLWPCHPGN- 77

                          90
                  ....*....|..
gi 975830122  581 aiHQQHWDFQED 592
Cdd:pfam00652  78 --GNQRWRYDED 87
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 225-354 2.59e-03

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 40.41  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 225 EIILVDDLSQQGQLKSAlSEYVARLEGVKLLrSNKRLGAIRARMLGATRATGDVLVFMDAHCECHPGWLEPLLSRIAGDR 304
Cdd:PRK10073  37 EIIIVNDGSTDNSVEIA-KHYAENYPHVRLL-HQANAGVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDD 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 975830122 305 SRVVSPVIDVIDWK---TFQYYPSKDLQR-GVLDWkldfhweplPEHVRKALQS 354
Cdd:PRK10073 115 LDVAQCNADWCFRDtgeTWQSIPSDRLRStGVLSG---------PDWLRMALSS 159
 
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 ...
 194-493 6.47e-160

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 459.75  E-value: 6.47e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 194 SVILCFHDEAWSTLLRTVHSILDTVPRAFLKEIILVDDLSQQGQLKSALSEYVAR-LEGVKLLRSNKRLGAIRARMLGAT 272
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKyLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 273 RATGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVVSPVIDVIDWKTFQYYPSKDLQRGVLDWKLDFHWEPLPEHVRKAl 352
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEERRR- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 353 QSPISPIRSPVVPGEVVAMDRHYFQNTGAYDSLMSLRGGENLELSFKAWLCGGSVEILPCSRVGHIYQNQDS--HSPLDQ 430
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKRKpyTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 975830122 431 EATLRNRVRIAETWLGSFKETFYKHSPEAFslsKAEKPDCMERLQLQRRLGCRTFHWFLANVY 493
Cdd:cd02510  240 GTVLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 502-591 7.75e-36

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: 130.64  E-value: 7.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 502 RPSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpQHLCFAVRQEQVILQNCTEEgla 581
Cdd:cd23442    1 APYFSGQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGS-LQLCLDVRQEQVVLQNCTKE--- 76

                         90
                 ....*....|
gi 975830122 582 IHQQHWDFQE 591
Cdd:cd23442   77 KTSQKWDFQE 86
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 194-349 1.17e-31

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: 120.58  E-value: 1.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122  194 SVILCFHDEaWSTLLRTVHSILDTVPRAFlkEIILVDDLSQQGqLKSALSEYVARLEGVKLLRSNKRLGAIRARMLGATR 273
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGSTDG-TVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 975830122  274 ATGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVVSPVIDVIDWKTFQYYPSKDLQRGVLDWKLDFHWEPLPEHVR 349
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFL 152
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 180-304 1.58e-17

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 83.64  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 180 LCLQQHPQDSLPTASVILCFHDEAwSTLLRTVHSILDTVPRAFLKEIILVDDLSQQGqLKSALSEYVARLEGVKLLRSNK 259
Cdd:COG1215   18 LARRRRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGSTDE-TAEIARELAAEYPRVRVIERPE 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 975830122 260 RLGAIRARMLGATRATGDVLVFMDAHCECHPGWLEPLLSRIAGDR 304
Cdd:COG1215   96 NGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG 140
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 191-308 8.30e-17

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 79.36  E-value: 8.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 191 PTASVILCFHDEAwSTLLRTVHSILDTVPRAFlkEIILVDDLSQQGQLKsALSEYVARLEGVKLLRSNKRLGAIRARMLG 270
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTAE-ILRELAAKDPRIRVIRLERNRGKGAARNAG 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 975830122 271 ATRATGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVV 308
Cdd:COG0463   78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
191-298 1.77e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 75.41  E-value: 1.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 191 PTASVILCFHDEaWSTLLRTVHSILDTVPRAFlkEIILVDDLSQQGQLksalsEYVARLE--GVKLLRSNKRLGAIRARM 268
Cdd:COG1216    3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTA-----ELLAALAfpRVRVIRNPENLGFAAARN 74

                         90       100       110
                 ....*....|....*....|....*....|
gi 975830122 269 LGATRATGDVLVFMDAHCECHPGWLEPLLS 298
Cdd:COG1216   75 LGLRAAGGDYLLFLDDDTVVEPDWLERLLA 104
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 195-308 2.14e-14

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: 71.00  E-value: 2.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 195 VILCFHDEAwSTLLRTVHSILDTVPRAFlkEIILVDDLSQQGQLKsALSEYVARLEGVKLLRSNKRLGAIRARMLGATRA 274
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTLE-ILEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76

                         90       100       110
                 ....*....|....*....|....*....|....
gi 975830122 275 TGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVV 308
Cdd:cd00761   77 RGEYILFLDADDLLLPDWLERLVAELLADPEADA 110
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
505-592 5.61e-12

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 63.32  E-value: 5.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122  505 FSGKLHNTGLGLCADCQAeGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQhLCFAVRQE----QVILQNCTEEGl 580
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPG-GSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVASD-LCLDVGSTadgaKVVLWPCHPGN- 77

                          90
                  ....*....|..
gi 975830122  581 aiHQQHWDFQED 592
Cdd:pfam00652  78 --GNQRWRYDED 87
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 503-592 2.13e-08

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: 53.10  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 503 PSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQHLCFAVRQEQ-VILQNCTEEGLA 581
Cdd:cd23435    1 PGYYGALRNKGSELCLDVNNPNGQGGKPVIMYGCHGLGGNQYFEYTSKGEIRHNIGKELCLHASGSDeVILQHCTSKGKD 80

                         90
                 ....*....|..
gi 975830122 582 I-HQQHWDFQED 592
Cdd:cd23435   81 VpPEQKWLFTQD 92
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 195-308 2.42e-08

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


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 54.12  E-value: 2.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 195 VILCFHDEAwsTLLRTVHSILDTVPRAFLKEIILVDDLSQQGQLKSALsEYVARLEGVKLLRSNKRLG---AIRArmlGA 271
Cdd:cd04179    2 VIPAYNEEE--NIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIAR-ELAARVPRVRVIRLSRNFGkgaAVRA---GF 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 975830122 272 TRATGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVV 308
Cdd:cd04179   76 KAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVV 112
beta-trefoil_Ricin_GALNT3 cd23468
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 503-599 1.10e-07

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: 50.97  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 503 PSFSGKLHNTGLGLCADCqAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQHLCFAVRQEQVILQNCTEEG--- 579
Cdd:cd23468    2 PLIFGAIKNVGKELCLDV-GENNHGGKPLIMYNCHGLGGNQYFEYSTHHEIRHNIQKELCLHGSQGSVQLKECTYKGrnt 80

                         90       100
                 ....*....|....*....|
gi 975830122 580 LAIHQQHWDFQEDENRANSA 599
Cdd:cd23468   81 AVLPEEKWELQKDQLLYNPA 100
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 192-403 1.32e-06

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: 49.92  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 192 TASVILCFHDEAwSTLLRTVHSILDTVPRAFLKEIILVDDLSQQGQlKSALSEYVARLEGVKLLRSNKRLGAIrARMLGA 271
Cdd:cd02525    1 FVSIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTDGT-REIVQEYAAKDPRIRLIDNPKRIQSA-GLNIGI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 272 TRATGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVVSPVIDVIdwktfqyyPSKDLQRGVLDwkldfhweplpehvrkA 351
Cdd:cd02525   78 RNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETI--------GESKFQKAIAV----------------A 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 975830122 352 LQSP----ISPIRSPVVPGEVV------AMDRHYFQNTGAYDSlmSLRGGENLELS-------FKAWLC 403
Cdd:cd02525  134 QSSPlgsgGSAYRGGAVKIGYVdtvhhgAYRREVFEKVGGFDE--SLVRNEDAELNyrlrkagYKIWLS 200
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 195-308 5.08e-06

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: 47.95  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 195 VILCFHDEawSTLLRTVHSILDTVPRAFLK--EIILVDDLSQQGQLKSALSEYVARLEGVKLLRSNKRLG---AIRARML 269
Cdd:cd04188    2 VIPAYNEE--KRLPPTLEEAVEYLEERPSFsyEIIVVDDGSKDGTAEVARKLARKNPALIRVLTLPKNRGkggAVRAGML 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 975830122 270 gatRATGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVV 308
Cdd:cd04188   80 ---AARGDYILFADADLATPFEELEKLEEALKTSGYDIA 115
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 195-439 9.52e-06

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 47.37  E-value: 9.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122  195 VILCFHDEawSTLLRTVHSILDTV-PRAflkEIILVDDLSQQGQLKSALsEYVARLEGVKL--LRSNKRLG---AIRARM 268
Cdd:pfam13641   7 VVPAFNED--SVLGRVLEAILAQPyPPV---EVVVVVNPSDAETLDVAE-EIAARFPDVRLrvIRNARLLGptgKSRGLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122  269 LGATRATGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVVSpviDVIDWKTFQYYPSkdlQRGVLDWKLDFHWEPLPEHV 348
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVG---TPVFSLNRSTMLS---ALGALEFALRHLRMMSLRLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122  349 RKALqsPISpirspvvpGEVVAMDRHYFQNTGAYDSLMSLrgGENLELSFKAWLCGGSVEILPCSRVGHIyqnqdshSPL 428
Cdd:pfam13641 155 LGVL--PLS--------GAGSAIRREVLKELGLFDPFFLL--GDDKSLGRRLRRHGWRVAYAPDAAVRTV-------FPT 215

                         250
                  ....*....|.
gi 975830122  429 DQEATLRNRVR 439
Cdd:pfam13641 216 YLAASIKQRAR 226
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 186-284 1.06e-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: 47.19  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 186 PQDSLPTASVILCFHDEAwSTLLRTVHSILDTVPRAFLKEIILVDDLSQQGQLkSALSEYVARleGVKLLRSNKRLGAIR 265
Cdd:cd06439   24 DPAYLPTVTIIIPAYNEE-AVIEAKLENLLALDYPRDRLEIIVVSDGSTDGTA-EIAREYADK--GVKLLRFPERRGKAA 99

                         90
                 ....*....|....*....
gi 975830122 266 ARMLGATRATGDVLVFMDA 284
Cdd:cd06439  100 ALNRALALATGEIVVFTDA 118
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 195-294 3.18e-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: 44.91  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 195 VILCFHDEAwSTLLRTVHSILD-TVPRaflKEIILVDDLSQQGQLKSALSEYVARLEGVKLLRSNKRLG---AIRArmlG 270
Cdd:cd06423    1 IIVPAYNEE-AVIERTIESLLAlDYPK---LEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGkagALNA---G 73

                         90       100
                 ....*....|....*....|....
gi 975830122 271 ATRATGDVLVFMDAHCECHPGWLE 294
Cdd:cd06423   74 LRHAKGDIVVVLDADTILEPDALK 97
beta-trefoil_Ricin_GALNT6 cd23470
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 503-600 6.85e-05

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: 42.93  E-value: 6.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 503 PSFSGKLHNTGLGLCADCqAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQHLCFAVRQEQVILQNCTEEGLAI 582
Cdd:cd23470    1 PTFYGAIKNEGTNQCLDV-GENNRGGKPLIMYSCHGMGGNQYFEYTTHKELRHNIAKQLCLRVSKGPVQLGECHYKGKNS 79

                         90       100
                 ....*....|....*....|.
gi 975830122 583 H---QQHWDFQEDENRANSAA 600
Cdd:cd23470   80 QvppDEEWELTQDHLIRNSGS 100
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 195-335 1.23e-04

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 43.82  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 195 VILCFHDEAwSTLLRTVHSI--LDTVPRAFlkEIILVDDLS--QQGQLKSAlseyvARLEG---VKLLRSNKRLGAIRAR 267
Cdd:cd04192    1 VVIAARNEA-ENLPRLLQSLsaLDYPKEKF--EVILVDDHStdGTVQILEF-----AAAKPnfqLKILNNSRVSISGKKN 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 975830122 268 ML--GATRATGDVLVFMDAHCECHPGWLEPLLSRIAGDRSRVVS-PVIdvidwktfqYYPSKDL--QRGVLDW 335
Cdd:cd04192   73 ALttAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAgPVI---------YFKGKSLlaKFQRLDW 136
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 506-589 1.44e-04

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


Pssm-ID: 467319 [Multi-domain]  Cd Length: 122  Bit Score: 41.62  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 506 SGKLHNTGLGLCADCQAEGdilgCPMVLAPCSDSRQQQYLqHTSRKEIHFGSpqHLCFAVRQE-QVILQNCTEEGLAihq 584
Cdd:cd23441   47 DGQLQTQGLCLTVDSSSKD----LPVVLETCSDDPKQKWT-RTGRQLVHSES--GLCLDSRKKkGLVVSPCRSGAPS--- 116


                 ....*
gi 975830122 585 QHWDF 589
Cdd:cd23441  117 QKWDF 121
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 207-284 2.33e-04

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


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 42.46  E-value: 2.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 975830122 207 LLRTVHSILDTVPRAFlkEIILVDDLSQQGQLKsALSEYVARLEGVKLLRSNKRLGAIRARMLGATRATGDVLVFMDA 284
Cdd:cd04187   15 LYERLKAVLESLGYDY--EIIFVDDGSTDRTLE-ILRELAARDPRVKVIRLSRNFGQQAALLAGLDHARGDAVITMDA 89
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 503-592 3.63e-04

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


Pssm-ID: 467349  Cd Length: 140  Bit Score: 40.93  E-value: 3.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 503 PSFSGKLHNTGL-GLCADCQA--EGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQ-HLCFAVR--QEQVILQNCT 576
Cdd:cd23471    1 PGFFGMLKNKGMtNYCFDYNPpdEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTRQpEGCAAVDagTDFLTMHLCR 80

                         90
                 ....*....|....*..
gi 975830122 577 EEGLAI-HQQHWDFQED 592
Cdd:cd23471   81 ENRQAVpENQKFIFRED 97
beta-trefoil_Ricin_GALNT4 cd23469
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 503-592 3.86e-04

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: 41.04  E-value: 3.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 503 PSFSGKLHNTGL-GLCADCQA-EGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQHLCFAVRQEQ--VILQNCTEE 578
Cdd:cd23469    1 PGWHGAVRSMGIsSECLDYNSpEHNPTGAHLSLFGCHGQGGNQFFEYTSNKEIRFNSVTELCAEVPDQKnyIGMKHCPKD 80

                         90
                 ....*....|....*
gi 975830122 579 GLAIHQQ-HWDFQED 592
Cdd:cd23469   81 GSPVPANiIWHFKED 95
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 501-593 3.99e-04

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: 41.10  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 501 PRPSFsGKLHNTGLGLCADcqAEGDILGCPMVLAPCSDSR------QQQYLQHTSRKEIHFGSPQH---LCF-AVRQEQ- 569
Cdd:cd23476    3 PAAAW-GEIRNVGTGLCAD--TKHGALGSPLRLEGCVKGRgeaawnNGQVFTFGWREDIRPGDPQHtkkFCFdAISHNSp 79

                         90       100
                 ....*....|....*....|....
gi 975830122 570 VILQNCteEGLAiHQQHWDFQEDE 593
Cdd:cd23476   80 VTLYDC--HGMK-GNQLWRYRKDK 100
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 225-301 4.11e-04

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


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 42.14  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 225 EIILVDDLSQQGQLKsALSEYVARLEGVKLLRSNKRLGAIRARMLGATRATGDVLVFMDA---HcecHPGWLEPLLSRIA 301
Cdd:cd06442   29 EIIVVDDNSPDGTAE-IVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDAdlsH---PPEYIPELLEAQL 104
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 194-294 6.41e-04

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 41.40  E-value: 6.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 194 SVILCFHDEAwSTLLRTVHSILDTVPRAFlkEIILVDDLSQQGqlksalSEYVARLEGVKLLRSNKrlGaiRARML--GA 271
Cdd:cd02522    2 SIIIPTLNEA-ENLPRLLASLRRLNPLPL--EIIVVDGGSTDG------TVAIARSAGVVVISSPK--G--RARQMnaGA 68

                         90       100
                 ....*....|....*....|...
gi 975830122 272 TRATGDVLVFMDAHCECHPGWLE 294
Cdd:cd02522   69 AAARGDWLLFLHADTRLPPDWDA 91
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 506-595 6.91e-04

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: 40.04  E-value: 6.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 506 SGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGspqHLC--FAVRQEQVILQNCteeglaiH 583
Cdd:cd23462    5 YGEIRNLAGKLCLDAPGRKKELNKPVGLYPCHGQGGNQYWMLTKDGEIRRD---DLCldYAGGSGDVTLYPC-------H 74

                         90
                 ....*....|....*.
gi 975830122 584 Q----QHWDFQEDENR 595
Cdd:cd23462   75 GmkgnQFWIYDEETKQ 90
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 225-354 2.59e-03

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 40.41  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 225 EIILVDDLSQQGQLKSAlSEYVARLEGVKLLrSNKRLGAIRARMLGATRATGDVLVFMDAHCECHPGWLEPLLSRIAGDR 304
Cdd:PRK10073  37 EIIIVNDGSTDNSVEIA-KHYAENYPHVRLL-HQANAGVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDD 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 975830122 305 SRVVSPVIDVIDWK---TFQYYPSKDLQR-GVLDWkldfhweplPEHVRKALQS 354
Cdd:PRK10073 115 LDVAQCNADWCFRDtgeTWQSIPSDRLRStGVLSG---------PDWLRMALSS 159
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 508-598 2.66e-03

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


Pssm-ID: 467334 [Multi-domain]  Cd Length: 122  Bit Score: 38.11  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 508 KLHNTGLGLCADCQaEGDILGCPMVLAPCSDSRQQQ-YLQHTSRkeIHFGSPQHLCFAVRQE-----QVILQNCTEEgla 581
Cdd:cd23456    4 QLKSQASGLCLDVS-GGATNGANVVVYDCNNSNSQKwYYDATGR--LHSKANPGKCLDAGGEnsngaNVVLWACNDS--- 77

                         90
                 ....*....|....*....
gi 975830122 582 IHQQhWDFQED--ENRANS 598
Cdd:cd23456   78 ANQR-WDFDGNfiRSRNNT 95
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 507-592 5.00e-03

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: 37.36  E-value: 5.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830122 507 GKLHNTGLGLCAdcQAEGDIL--GCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpqHLCFAV---RQEQVILQNCTEEGLA 581
Cdd:cd23440    6 GQLKHAGSGLCL--VAEDEVSqkGSLLVLRPCSRNDKKQLWYYTEDGELRLAN--LLCLDSsetSSDFPRLMKCHGSGGS 81

                         90
                 ....*....|.
gi 975830122 582 ihqQHWDFQED 592
Cdd:cd23440   82 ---QQWRFKKD 89
 
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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