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Conserved domains on  [gi|38327556|ref|NP_068580|]
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polypeptide N-acetylgalactosaminyltransferase 9 isoform B [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 90-234 5.80e-117

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 cd23473:

Pssm-ID: 483949  Cd Length: 145  Bit Score: 330.00  E-value: 5.80e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  90 MRVYNNTLTYGEVRNSKASAYCLDQGAEDGDRAILYPCHGMSSQLVRYSADGLLQLGPLGSTAFLPDSKCLVDDGTGRMP 169
Cdd:cd23473   1 MRIYNNTITYGEVRNSKASGYCLDQGSEEDDKAILYPCHGMSSQLVRYSTEGLLQLGPLGSTAFLPDTKCLVDDGRGRTP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38327556 170 TLKKCEDVARPTQRLWDFTQSGPIVSRATGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIKH 234
Cdd:cd23473  81 TLKKCEDVARPAQRLWDFTQNGPIISRDTGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIKH 145
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 1-87 1.41e-37

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.


The actual alignment was detected with superfamily member cd02510:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 299  Bit Score: 133.10  E-value: 1.41e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556   1 MEVLPCSRVAHIERT-RKPYNNDIDY-YAKRNALRAAEVWMDDFKSHVYMAWNIPMsnpGVDFGDVSERLALRQRLKCRS 78
Cdd:cd02510 214 IEIVPCSRVGHIFRRkRKPYTFPGGSgTVLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKS 290


                ....*....
gi 38327556  79 FKWYLENVY 87
Cdd:cd02510 291 FKWYLENVY 299
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_GALNT9 cd23473
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 90-234 5.80e-117

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 9 (GALNT9) and similar proteins; GALNT9 (EC 2.4.1.41), also called polypeptide GalNAc transferase 9, GalNAc-T9, pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9, 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. GALNT9 does not glycosylate apomucin or SDC3. GALNT9 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: 467351  Cd Length: 145  Bit Score: 330.00  E-value: 5.80e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  90 MRVYNNTLTYGEVRNSKASAYCLDQGAEDGDRAILYPCHGMSSQLVRYSADGLLQLGPLGSTAFLPDSKCLVDDGTGRMP 169
Cdd:cd23473   1 MRIYNNTITYGEVRNSKASGYCLDQGSEEDDKAILYPCHGMSSQLVRYSTEGLLQLGPLGSTAFLPDTKCLVDDGRGRTP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38327556 170 TLKKCEDVARPTQRLWDFTQSGPIVSRATGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIKH 234
Cdd:cd23473  81 TLKKCEDVARPAQRLWDFTQNGPIISRDTGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIKH 145
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 1-87 1.41e-37

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: 133.10  E-value: 1.41e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556   1 MEVLPCSRVAHIERT-RKPYNNDIDY-YAKRNALRAAEVWMDDFKSHVYMAWNIPMsnpGVDFGDVSERLALRQRLKCRS 78
Cdd:cd02510 214 IEIVPCSRVGHIFRRkRKPYTFPGGSgTVLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKS 290


                ....*....
gi 38327556  79 FKWYLENVY 87
Cdd:cd02510 291 FKWYLENVY 299
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
98-226 1.12e-19

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 81.42  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556    98 TYGEVRNsKASAYCLD--QGAEDGDRAILYPCHGM-SSQLVRYSADGLLQLGPlgstaflpDSKCL--VDDGTGRMPTLK 172
Cdd:pfam00652   1 ATGRIRN-RASGKCLDvpGGSSAGGPVGLYPCHGSnGNQLWTLTGDGTIRSVA--------SDLCLdvGSTADGAKVVLW 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 38327556   173 KCeDVARPTQRlWDFTQSG-PIVSRATGRCLEVEMSKDANFglRLVVQRC----SGQKW 226
Cdd:pfam00652  72 PC-HPGNGNQR-WRYDEDGtQIRNPQSGKCLDVSGAGTSNG--KVILWTCdsgnPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 105-226 1.08e-09

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 54.44  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556    105 SKASAYCLDQGAEDGdRAILYPCHGMSS-QLVRYSADGLLQlgplgstaFLPDSKCL-VDDGTGRMPTLKKCEDVArPTQ 182
Cdd:smart00458   3 SGNTGKCLDVNGNKN-PVGLFDCHGTGGnQLWKLTSDGAIR--------IKDTDLCLtANGNTGSTVTLYSCDGTN-DNQ 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 38327556    183 RlWDFTQSGPIVSRATGRCLEVemsKDANFGLRLVVQRCSG---QKW 226
Cdd:smart00458  73 Y-WEVNKDGTIRNPDSGKCLDV---KDGNTGTKVILWTCSGnpnQKW 115
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_GALNT9 cd23473
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 90-234 5.80e-117

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 9 (GALNT9) and similar proteins; GALNT9 (EC 2.4.1.41), also called polypeptide GalNAc transferase 9, GalNAc-T9, pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9, 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. GALNT9 does not glycosylate apomucin or SDC3. GALNT9 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: 467351  Cd Length: 145  Bit Score: 330.00  E-value: 5.80e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  90 MRVYNNTLTYGEVRNSKASAYCLDQGAEDGDRAILYPCHGMSSQLVRYSADGLLQLGPLGSTAFLPDSKCLVDDGTGRMP 169
Cdd:cd23473   1 MRIYNNTITYGEVRNSKASGYCLDQGSEEDDKAILYPCHGMSSQLVRYSTEGLLQLGPLGSTAFLPDTKCLVDDGRGRTP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38327556 170 TLKKCEDVARPTQRLWDFTQSGPIVSRATGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIKH 234
Cdd:cd23473  81 TLKKCEDVARPAQRLWDFTQNGPIISRDTGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIKH 145
beta-trefoil_Ricin_GALNT8-like cd23438
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 95-230 2.90e-80

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8)-like subfamily; The GALNT8-like subfamily includes GALNT8, GALNT9, GALNT17 and GALNT18. 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. GALNT9 does not glycosylate apomucin or SDC3. 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 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: 467316  Cd Length: 134  Bit Score: 236.56  E-value: 2.90e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  95 NTLTYGEVRNSKASAYCLDQGAEDGDRAILYPCHGMSSQLVRYSADGLLQLGPLGSTAFlPDSKCLVDDGTGRMPTLKKC 174
Cdd:cd23438   1 NTVAYGEMRNSLVTDLCLDQGPKENHTAILYPCHGWSPQLVRYTKDGQLYLGQLGSTAS-PDTRCLVDDGKSDKPQLLDC 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 38327556 175 EDVARPTQRLWDFTQSGPIVSRATGRCLEVEMSKDaNFGLRLVVQRCSGQKWMIRN 230
Cdd:cd23438  80 SKVKNRLQKYWDFSQGGAIQNRATGRCLEVEEDKL-NFGHRLVLQTCSGQKWNIKN 134
beta-trefoil_Ricin_GALNT17 cd23474
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 90-233 3.19e-61

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: 188.57  E-value: 3.19e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  90 MRVYNNTLTYGEVRNSKASAYCLDQGAEDGDRAILYPCHGMSSQLVRYSADGLLQLGPLGSTAFLPDSKCLVDDGTGRMP 169
Cdd:cd23474   1 MRRYNNTVAYGELRNNKAKDVCLDQGPPENHTAILYPCHGWGPQLARYTKEGYLHLGALGTTTLLPDTRCLVDNKKSRFP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38327556 170 TLKKCEDVARPTQRLWDFTQSGPIVSRATGRCLEVEMSKdaNFGLRLVVQRCSGQKWMIRNWIK 233
Cdd:cd23474  81 QLLDCDKVKSILHKRWNFIQNGAIMNLGTGRCLEVENRG--NFGIDLILRSCTGQRWTIKNFIK 142
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 1-87 1.41e-37

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: 133.10  E-value: 1.41e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556   1 MEVLPCSRVAHIERT-RKPYNNDIDY-YAKRNALRAAEVWMDDFKSHVYMAWNIPMsnpGVDFGDVSERLALRQRLKCRS 78
Cdd:cd02510 214 IEIVPCSRVGHIFRRkRKPYTFPGGSgTVLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKS 290


                ....*....
gi 38327556  79 FKWYLENVY 87
Cdd:cd02510 291 FKWYLENVY 299
beta-trefoil_Ricin_GALNT18 cd23475
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 90-230 4.04e-37

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 18 (GALNT18) and similar proteins; GALNT18 (EC 2.4.1.41), also called polypeptide GalNAc transferase 18, GalNAc-T18, polypeptide GalNAc transferase-like protein 4, GalNAc-T-like protein 4, pp-GaNTase-like protein 4, polypeptide N-acetylgalactosaminyltransferase-like protein 4, protein-UDP acetylgalactosaminyltransferase-like protein 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. GALNT18 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: 467353  Cd Length: 142  Bit Score: 127.35  E-value: 4.04e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  90 MRVYNNTLTYGEVRNSKASAYCLDQGAEDGDRAILYPCHGMSSQLVRYSADGLLQLGPLGSTAFLPDSKCLVDdgTGRMP 169
Cdd:cd23475   1 MRMYTDTIAYGVLQNSLKTDLCLDQGPDTDNIPIMYICHGMTPQNVYYTSNQQLHVGILSPTIDDDDNRCLVD--VNSRP 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38327556 170 TLKKCEDVARPTQRL-WDFTQSGPIVSRATGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRN 230
Cdd:cd23475  79 RLIECSYAKAKRMKLyWLFTQGGSIQNKKSKRCLELQENADNEFGYQLVLQKCSGQRWTITN 140
beta-trefoil_Ricin_GALNT8 cd23472
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 87-233 6.80e-32

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8) and similar proteins; GALNT8 (EC 2.4.1.41), also called polypeptide GalNAc transferase 8, GalNAc-T8, pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8, 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. GALNT8 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: 467350  Cd Length: 146  Bit Score: 113.76  E-value: 6.80e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  87 YPEMRVYNNTLTYGEVRNSKASAYCLDQGAEDGDRAILYPCHGMSSQLVRYSADGLLQLGPLGSTAFLPDsKCLVDDGTG 166
Cdd:cd23472   1 YPVLMPIQTIVGYGTMKNSLNENICIDQGPVPGNTPIMYGCHGYSPQFVYYHLTGELYVGGLKADIYASD-RCLTDPGEG 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38327556 167 RMPTLKKCEDVARPTQRL-WDFTQSGPIVSRATGRCLEVEMSKDANFGLrLVVQRCSGQKWMIRNWIK 233
Cdd:cd23472  80 WKPELVSCQDATLKGLNMyWDFKQGTAIINRKTKRCLEISLDKTPSYYT-LILQTCTGQKWEIQHVLM 146
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
98-226 1.12e-19

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 81.42  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556    98 TYGEVRNsKASAYCLD--QGAEDGDRAILYPCHGM-SSQLVRYSADGLLQLGPlgstaflpDSKCL--VDDGTGRMPTLK 172
Cdd:pfam00652   1 ATGRIRN-RASGKCLDvpGGSSAGGPVGLYPCHGSnGNQLWTLTGDGTIRSVA--------SDLCLdvGSTADGAKVVLW 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 38327556   173 KCeDVARPTQRlWDFTQSG-PIVSRATGRCLEVEMSKDANFglRLVVQRC----SGQKW 226
Cdd:pfam00652  72 PC-HPGNGNQR-WRYDEDGtQIRNPQSGKCLDVSGAGTSNG--KVILWTCdsgnPNQQW 126
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 99-230 6.65e-19

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467315 [Multi-domain]  Cd Length: 124  Bit Score: 79.26  E-value: 6.65e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  99 YGEVRNsKASAYCLD-QGAEDGDRAILYPCHGM-SSQLVRYSADGLLQLGplgstaflpdSKCLVDDGTGRMPTLKKCEd 176
Cdd:cd23437   5 WGEIRN-LGTGLCLDtMGHQNGGPVGLYPCHGMgGNQLFRLNEAGQLAVG----------EQCLTASGSGGKVKLRKCN- 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38327556 177 vARPTQRlWDFTQS-GPIVSRATGRCLEVEMSKDanfglRLVVQRCSG----QKWMIRN 230
Cdd:cd23437  73 -LGETGK-WEYDEAtGQIRHKGTGKCLDLNEGTN-----KLILQPCDSsspsQKWEFNE 124
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 105-226 4.61e-14

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: 66.60  E-value: 4.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 105 SKASAYCLD---QGAEDGDRAILYPCHGMSSQLVRYSADGLLQLGplgstaflpDSKCLVDDGTGRMP----TLKKCEdv 177
Cdd:cd23418  10 GYGSGRCLDvpgGSTTNGTRLILWDCHGGANQQFTFTSAGELRVG---------GDKCLDAAGGGTTNgtpvVIWPCN-- 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 38327556 178 ARPTQRlWDFTQSGPIVSRATGRCLEVEMSKDANfGLRLVVQRCSG---QKW 226
Cdd:cd23418  79 GGANQK-WRFNSDGTIRNVNSGLCLDVAGGGTAN-GTRLILWSCNGgsnQRW 128
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 99-229 3.76e-11

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: 58.61  E-value: 3.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  99 YGEVRNsKASAYCLD-QGAEDGDRAI-LYPCHG-MSSQLVRYSADGLLQlgplgstaflPDSKCLVDDgTGRMPTLKKCE 175
Cdd:cd23460   2 LGQIKH-TESGLCLDwAGESNGDKTVaLKPCHGgGGNQFWMYTGDGQIR----------QDHLCLTAD-EGNKVTLRECA 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38327556 176 DVaRPTQRlWDFTQS-GPIVSRATGRCLEVEMSKDanfglRLVVQRCSG----QKWMIR 229
Cdd:cd23460  70 DQ-LPSQE-WSYDEKtGTIRHRSTGLCLTLDANND-----VVILKECDSnslwQKWIFQ 121
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 100-230 1.20e-10

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: 57.32  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 100 GEVRNSKaSAYCLDQ-GAEDGDRAILYPCHGM-SSQLVRYSADGLLQlgplgstaflPDSKCLvDDGTGRMP-TLKKCeD 176
Cdd:cd23433   7 GEIRNVE-TNLCLDTmGRKAGEKVGLSSCHGQgGNQVFSYTAKGEIR----------SDDLCL-DASRKGGPvKLEKC-H 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38327556 177 VARPTQrLWDF-TQSGPIVSRATGRCLEVEMSKDANfglRLVVQRCSG---QKWMIRN 230
Cdd:cd23433  74 GMGGNQ-EWEYdKETKQIRHVNSGLCLTAPNEDDPN---EPVLRPCDGgpsQKWELEG 127
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 95-226 1.78e-10

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: 56.94  E-value: 1.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  95 NTLTYGEVRNSKaSAYCLD--QGAEDGDRAI-LYPCHGM--SSQLVRYSADGLLQlgplgstaflPDSKCL-VDDGTGRM 168
Cdd:cd23459   3 DVLAYGQVRNPG-TNLCLDtlQRDEDKGYNLgLYPCQGGlsSNQLFSLSKKGELR----------REESCAdVQGTEESK 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38327556 169 PTLKKCEDVARPTQRlWDFTQSGPIVSRATGRCLEVEMSKDanfGLRLVVQRCSG---QKW 226
Cdd:cd23459  72 VILITCHGLEKFNQK-WKHTKGGQIVHLASGKCLDAEGLKS---GDDVTLAKCDGslsQKW 128
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 98-226 2.91e-10

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: 56.61  E-value: 2.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  98 TYGEVRNsKASAYCLD---QGAEDGDRAILYPCHGMSSQL--VRYSADGLLQLGPLGStaflpdSKCL-VDDGT---GRM 168
Cdd:cd00161   1 GTYRIVN-AASGKCLDvagGSTANGAPVQQWTCNGGANQQwtLTPVGDGYYTIRNVAS------GKCLdVAGGStanGAN 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38327556 169 PTLKKCEDvaRPTQRlWDFTQSGP----IVSRATGRCLEVEMSKDANfGLRLVVQRCSG---QKW 226
Cdd:cd00161  74 VQQWTCNG--GDNQQ-WRLEPVGDgyyrIVNKHSGKCLDVSGGSTAN-GANVQQWTCNGganQQW 134
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 95-226 4.27e-10

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467340 [Multi-domain]  Cd Length: 126  Bit Score: 55.83  E-value: 4.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  95 NTLTYGEVRNSkASAYCLDQGAEDGD---RAILYPCHGMS-SQLVRYSADGLLQLgplgstaflpDSKCLVDDGTGRMPT 170
Cdd:cd23462   1 EALAYGEIRNL-AGKLCLDAPGRKKElnkPVGLYPCHGQGgNQYWMLTKDGEIRR----------DDLCLDYAGGSGDVT 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38327556 171 LKKCEDvARPTQrLWDFT-QSGPIVSRATGRCLEVemskdANFGLRLVVQRCSG----QKW 226
Cdd:cd23462  70 LYPCHG-MKGNQ-FWIYDeETKQIVHGTSKKCLEL-----SDDSSKLVMEPCNGssprQQW 123
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 105-226 1.08e-09

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 54.44  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556    105 SKASAYCLDQGAEDGdRAILYPCHGMSS-QLVRYSADGLLQlgplgstaFLPDSKCL-VDDGTGRMPTLKKCEDVArPTQ 182
Cdd:smart00458   3 SGNTGKCLDVNGNKN-PVGLFDCHGTGGnQLWKLTSDGAIR--------IKDTDLCLtANGNTGSTVTLYSCDGTN-DNQ 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 38327556    183 RlWDFTQSGPIVSRATGRCLEVemsKDANFGLRLVVQRCSG---QKW 226
Cdd:smart00458  73 Y-WEVNKDGTIRNPDSGKCLDV---KDGNTGTKVILWTCSGnpnQKW 115
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 99-228 2.04e-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: 51.18  E-value: 2.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  99 YGEVRNsKASAYCLDQGAEDGD---RAILYPCHGM-SSQLVRYSADGLLQLgplgSTAFlpdSKCLVDDGtGRMPTLKKC 174
Cdd:cd23435   4 YGALRN-KGSELCLDVNNPNGQggkPVIMYGCHGLgGNQYFEYTSKGEIRH----NIGK---ELCLHASG-SDEVILQHC 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 175 E--DVARPTQRLWDFTQSGPIVSRATGRCLEVEMSKdanfglrLVVQRCSG----QKWMI 228
Cdd:cd23435  75 TskGKDVPPEQKWLFTQDGTIRNPASGLCLHASGYK-------VLLRTCNPsddsQKWTF 127
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 100-226 5.44e-06

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


Pssm-ID: 467329 [Multi-domain]  Cd Length: 125  Bit Score: 44.25  E-value: 5.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 100 GEVRNSkASAYCLD---QGAEDGDRAILYPCHGMSSQLVRYSADG-LLQLGplgstaflpdsKCLVDDGTGRMPT----L 171
Cdd:cd23451   3 GPVRLA-NAGKCLDvpgSSTADGNPVQIYTCNGTAAQKWTLGTDGtLRVLG-----------KCLDVSGGGTANGtlvqL 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38327556 172 KKCEDVarPTQRlWDFTQSGPIVSRATGRCLEVEMSKDANfGLRLVVQRCSG---QKW 226
Cdd:cd23451  71 WDCNGT--GAQK-WVPRADGTLYNPQSGKCLDAPGGSTTD-GTQLQLYTCNGtaaQQW 124
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 111-226 1.47e-05

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: 43.08  E-value: 1.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 111 CLDQ-GAEDGDRAILYPCHGM-SSQLVRYSADGLLQlgplgstaflPDSKCL-VDDGTGRMP-TLKKCEDVARPTQrlWD 186
Cdd:cd23434  11 CLDTlGHKAGGTVGLYPCHGTgGNQEWSFTKDGQIK----------HDDLCLtVVDRAPGSLvTLQPCREDDSNQK--WE 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 38327556 187 FTQSGP-IVSRATGRCLEvemSKDANfGLRLVVQRCSG----QKW 226
Cdd:cd23434  79 QIENNSkLRHVGSNLCLD---SRNAK-SGGLTVETCDPssgsQQW 119
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 100-226 3.01e-05

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: 42.43  E-value: 3.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 100 GEVRNsKASAYCLD---QGAEDGDRAILYPCHGMS-SQLVRYSADGLLQLGPLGstaflpdsKCLvdDGTGRMPTLKKCE 175
Cdd:cd23442   6 GQLYN-TGTGYCADyihGWRLAGGPVELSPCSGQNgNQLFEYTSDKEIRFGSLQ--------LCL--DVRQEQVVLQNCT 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 38327556 176 DVArpTQRLWDFTQSGPIVSRATGRCLEVeMSKDANFGLRLvvQRCSG---QKW 226
Cdd:cd23442  75 KEK--TSQKWDFQETGRIVHILSGKCIEA-VESENSKLLFL--SPCNGqrnQMW 123
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
 101-226 5.54e-05

ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine protease I (RPI) and similar proteins; RPI, also called serine protease 1, is a major serine protease exhibiting lytic activity toward living yeast cells. It has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI. RPI contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467330 [Multi-domain]  Cd Length: 125  Bit Score: 41.73  E-value: 5.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 101 EVRNSKASaycldqgaeDGDRAILYPCHGMSSQLVRYSADGLLQLGplgstaflpdSKCL------VDDGTGRMptLKKC 174
Cdd:cd23452  15 DVPNSSTT---------DGAPLQLWDCNGTNAQKWTFASDGTLRAL----------GKCLdvawggTDNGTAVQ--LWTC 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 38327556 175 EdvARPTQRlWDFTQSGPIVSRATGRCLEVEMSKDANfGLRLVVQRCSG---QKW 226
Cdd:cd23452  74 S--GNPAQQ-FVLSGAGDLVNPQANKCVDVSGGNSGN-GTRLQLWECSGnanQKW 124
beta-trefoil_Ricin_GALNT3 cd23468
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 95-202 1.39e-04

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: 40.57  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  95 NTLTYGEVRNSKASAyCLDQGAED--GDRAILYPCHGM-SSQLVRYSADGLLQLGplgstafLPDSKCLvdDGTGRMPTL 171
Cdd:cd23468   1 NPLIFGAIKNVGKEL-CLDVGENNhgGKPLIMYNCHGLgGNQYFEYSTHHEIRHN-------IQKELCL--HGSQGSVQL 70

                        90       100       110
                ....*....|....*....|....*....|....*
gi 38327556 172 KKC----EDVARPTQRLWDFTQSGPIVSRATGRCL 202
Cdd:cd23468  71 KECtykgRNTAVLPEEKWELQKDQLLYNPALNMCL 105
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 95-226 2.03e-04

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


Pssm-ID: 467319 [Multi-domain]  Cd Length: 122  Bit Score: 40.08  E-value: 2.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  95 NTLTYGEVRNSKAsayCLDQGAEDGDRA---ILYPCHG-MSSQLVRYSADGLLQLgplgstaflpDSKCLV--DDGTGRM 168
Cdd:cd23441   1 NELAYGQIKQGNL---CLDSDEQLFQGPallILAPCSNsSDSQEWSFTKDGQLQT----------QGLCLTvdSSSKDLP 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38327556 169 PTLKKCEDvaRPTQRlWDFTqSGPIVSRATGRCLEVEMSKdanfglRLVVQRCS----GQKW 226
Cdd:cd23441  68 VVLETCSD--DPKQK-WTRT-GRQLVHSESGLCLDSRKKK------GLVVSPCRsgapSQKW 119
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 111-226 2.26e-04

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket.


Pssm-ID: 467294 [Multi-domain]  Cd Length: 120  Bit Score: 39.72  E-value: 2.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 111 CLDqgAEDGDRAILYPCHGMSSQL--VRYSADGLLQLGPLGStaflpdSKCLVDDGTGRMpTLKKCEDVARptQRlWDFT 188
Cdd:cd23415  13 CLD--SNAGGNVYTGPCNGGPYQRwtWSGVGDGTVTLRNAAT------GRCLDSNGNGGV-YTLPCNGGSY--QR-WRVT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 38327556 189 QSGP----IVSRATGRCLevemskDANFGLRLVVQRCSG---QKW 226
Cdd:cd23415  81 STSGggvtLRNVATGRCL------DSNGSGGVYTRPCNGgsyQRW 119
beta-trefoil_Ricin_AglA cd23425
ricin B-type lectin domain, beta-trefoil fold, found in alpha-galactosidase A (AglA) and ...
 107-205 2.55e-04

ricin B-type lectin domain, beta-trefoil fold, found in alpha-galactosidase A (AglA) and similar proteins; AglA (EC 3.2.1.22), also called melibiase A, hydrolyzes a variety of simple alpha-D-galactosides as well as more complex molecules such as oligosaccharides and polysaccharides. It belongs to the glycosyl hydrolase 27 (GH27) family. AglA contains an N-terminal GH27 catalytic domain, an alpha galactosidase C-terminal beta sandwich domain in the middle region, and a carbohydrate-binding domain at the C-terminus. The carbohydrate-binding domain is also known as a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.


Pssm-ID: 467303 [Multi-domain]  Cd Length: 116  Bit Score: 39.35  E-value: 2.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 107 ASAYCLdqgAEDGDRAILYPCHGMSSQLVRYSADGLLQlgPLGSTaflpdSKCLVDDGTGrmptLKKCEDVARPTQRlWD 186
Cdd:cd23425  11 ASGNCL---TADAAEVKFQTCDGSDSQIWQVRKSGILR--NLSNT-----GQCLTADGAN----VSLSPCDTSTSQN-WS 75

                        90
                ....*....|....*....
gi 38327556 187 FTQSGPIVSRATGRCLEVE 205
Cdd:cd23425  76 YEISGNLVNKKTGLCLTEG 94
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 99-226 2.98e-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: 39.78  E-value: 2.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  99 YGEVRNSKASAYCLDQGAED-----GDRAILYPCHGM-SSQLVRYSAdgllqLGPLGSTAFLPDSKCLVDDGTGRMpTLK 172
Cdd:cd23471   4 FGMLKNKGMTNYCFDYNPPDehqiaGHQVILYQCHGMgQNQFFEYTS-----QNEIRYNTRQPEGCAAVDAGTDFL-TMH 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 173 KCED--VARPTQRLWDFTQSGPIVSRATGRCLE-VEMSKDANFGlrLVVQRCSG---QKW 226
Cdd:cd23471  78 LCREnrQAVPENQKFIFREDGSLFHVQTQKCVQaVRNESSGSPA--PVLRPCTDsdhQKW 135
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 98-230 3.64e-04

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: 39.26  E-value: 3.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  98 TYGEVRNSKASAyCLDQGA-EDGDRAILYPCHGM-SSQLVRYSADGLLQlgplgstaflPDSKCL-VDDGTGRMpTLKKC 174
Cdd:cd23466   5 SLGEIRNVETNQ-CLDNMArKENEKVGIFNCHGMgGNQVFSYTANKEIR----------TDDLCLdVSKLNGPV-MMLKC 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 175 EDVArpTQRLWDFTQSG-PIVSRATGRCLEVEMSKDANFGlrlVVQRCSG---QKWMIRN 230
Cdd:cd23466  73 HHLK--GNQLWEYDPVKlTLLHVNSNQCLDKATEEDSQVP---SIRDCNGsrsQQWLLRN 127
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 100-187 9.87e-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: 38.12  E-value: 9.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 100 GEVRNSKasaYCLDqGAEDGDRAILYPCHGMS-SQLVRYSA-DGLLQLGPLGstaflpdsKCL-VDDGTGRMpTLKKCED 176
Cdd:cd23462  50 GEIRRDD---LCLD-YAGGSGDVTLYPCHGMKgNQFWIYDEeTKQIVHGTSK--------KCLeLSDDSSKL-VMEPCNG 116

                        90
                ....*....|.
gi 38327556 177 VArPTQRlWDF 187
Cdd:cd23462 117 SS-PRQQ-WEF 125
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 98-230 1.36e-03

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: 37.70  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  98 TYGEVRNSKASAyCLDQ-GAEDGDRAILYPCHGM-SSQLVRYSADGLLQlgplgstaflPDSKCLVDDGTGRMPTLKKCE 175
Cdd:cd23467   5 SLGEIRNVETNQ-CLDNmGRKENEKVGIFNCHGMgGNQVFSYTADKEIR----------TDDLCLDVSRLNGPVVMLKCH 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38327556 176 DVaRPTQrLWDFTQSGPIVSRA-TGRCLEVEMSKDAnfgLRLVVQRCSG---QKWMIRN 230
Cdd:cd23467  74 HM-RGNQ-LWEYDAERLTLRHVnSNQCLDEPSEEDK---MVPTMKDCSGsrsQQWLLRN 127
beta-trefoil_Ricin_GALNT6 cd23470
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 99-202 2.89e-03

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: 36.77  E-value: 2.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  99 YGEVRNsKASAYCLDQGAED--GDRAILYPCHGM-SSQLVRYSADGLLQLGpLGSTAFLPDSKCLVDDGTGRMptlkKCE 175
Cdd:cd23470   4 YGAIKN-EGTNQCLDVGENNrgGKPLIMYSCHGMgGNQYFEYTTHKELRHN-IAKQLCLRVSKGPVQLGECHY----KGK 77

                        90       100
                ....*....|....*....|....*..
gi 38327556 176 DVARPTQRLWDFTQSGPIVSRATGRCL 202
Cdd:cd23470  78 NSQVPPDEEWELTQDHLIRNSGSNMCL 104
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 95-226 3.11e-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: 36.59  E-value: 3.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556  95 NTLTYGEVRNSkASAYCLdqGAED-----GDRAILYPCHGMS-SQLVRYSADGLLQLGPLGstaflpdskCL-VDDGTGR 167
Cdd:cd23440   1 KVIRKGQLKHA-GSGLCL--VAEDevsqkGSLLVLRPCSRNDkKQLWYYTEDGELRLANLL---------CLdSSETSSD 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38327556 168 MPTLKKCEDvARPTQRlWDFTQSGPIVSRATGRCLeveMSKDANFGLRLVVQRCSG---QKW 226
Cdd:cd23440  69 FPRLMKCHG-SGGSQQ-WRFKKDNRLYNPASGQCL---AASKNGTSGYVTMDICSDspsQKW 125
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 158-231 3.14e-03

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket.


Pssm-ID: 467294 [Multi-domain]  Cd Length: 120  Bit Score: 36.64  E-value: 3.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 158 KCLVDDGTGRmPTLKKCedVARPTQRlWDFTQSGP----IVSRATGRCLevemskDANFGLRLVVQRCSG---QKWMIRN 230
Cdd:cd23415  12 RCLDSNAGGN-VYTGPC--NGGPYQR-WTWSGVGDgtvtLRNAATGRCL------DSNGNGGVYTLPCNGgsyQRWRVTS 81


                .
gi 38327556 231 W 231
Cdd:cd23415  82 T 82
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
184-229 3.97e-03

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 35.43  E-value: 3.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 38327556   184 LWDFTQSGP-----IVSRATGRCLEVEMSKDANfGLRLVVQRCSG---QKWMIR 229
Cdd:pfam14200   4 QWRFGGTVGdgyytIVNVASGKYLDVAGGSTAN-GANVQQWTDNGndnQQWRIV 56
beta-trefoil_Ricin_VPS13D cd23453
ricin B-type lectin domain, beta-trefoil fold, found in vacuolar protein sorting-associated ...
 117-215 5.32e-03

ricin B-type lectin domain, beta-trefoil fold, found in vacuolar protein sorting-associated protein 13D (VPS13D) and similar proteins; VPS13D is a ubiquitin-binding protein that is required for the regulation of mitochondrial size and clearance. It promotes mitochondrial clearance by mitochondrial autophagy (mitophagy), also possibly by positively regulating mitochondrial fission. Mitophagy plays an important role in regulating cell health and mitochondrial size and homeostasis. Mutations in VPS13D lead to a new recessive ataxia with spasticity and mitochondrial defects. VPS13D contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467331  Cd Length: 159  Bit Score: 36.52  E-value: 5.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327556 117 EDGDRailypchgmsSQLVRYSADGLLQlgPLGSTA-------FLPDSKCLVDDGTGRMPTLKKCED--VARPTQR---- 183
Cdd:cd23453  27 EPGKR----------SQLWRMTSTGMLQ--HEGSSPprdprksSRSLANCLVLDIAELAPTPNKYVPlvLRKPDERrkst 94

                        90       100       110
                ....*....|....*....|....*....|...
gi 38327556 184 -LWDFTQSGPIVSRATGRCLEvemSKDANFGLR 215
Cdd:cd23453  95 qTWRFTDDGRLVCGLPGLCVQ---ARGGVSGLK 124
 
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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