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Conserved domains on  [gi|578817888|ref|XP_006717350|]
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polypeptide N-acetylgalactosaminyltransferase 12 isoform X4 [Homo sapiens]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase( domain architecture ID 10301995)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 146-282 3.59e-96

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 cd23471:

Pssm-ID: 483949  Cd Length: 140  Bit Score: 278.99  E-value: 3.59e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 146 PGFFGMLQNKGLTDYCFDYNPPDENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHLCE 225
Cdd:cd23471    1 PGFFGMLKNKGMTNYCFDYNPPDEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTRQPEGCAAVDAGTDFLTMHLCR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 226 ET---APENQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFFKER 282
Cdd:cd23471   81 ENrqaVPENQKFIFREDGSLFHVQTQKCVQAVRNESSGSPAPVLRPCTDSDHQKWFFKER 140
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 2-136 3.34e-75

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: 231.71  E-value: 3.34e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888   2 QSPVDVIRSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPCSHVGHVFP-KQAPYSRNKAL 80
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888  81 A----NSVRAAEVWMDEFKELYYHRNPRARLEPFGDVTERKQLRDKLQCKDFKWFLETVY 136
Cdd:cd02510  240 GtvlrNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 146-282 3.59e-96

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: 278.99  E-value: 3.59e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 146 PGFFGMLQNKGLTDYCFDYNPPDENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHLCE 225
Cdd:cd23471    1 PGFFGMLKNKGMTNYCFDYNPPDEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTRQPEGCAAVDAGTDFLTMHLCR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 226 ET---APENQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFFKER 282
Cdd:cd23471   81 ENrqaVPENQKFIFREDGSLFHVQTQKCVQAVRNESSGSPAPVLRPCTDSDHQKWFFKER 140
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 2-136 3.34e-75

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: 231.71  E-value: 3.34e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888   2 QSPVDVIRSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPCSHVGHVFP-KQAPYSRNKAL 80
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888  81 A----NSVRAAEVWMDEFKELYYHRNPRARLEPFGDVTERKQLRDKLQCKDFKWFLETVY 136
Cdd:cd02510  240 GtvlrNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
148-277 2.07e-22

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 89.90  E-value: 2.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888  148 FFGMLQNKGlTDYCFDYNPPDENqivGHQVILYLCHGMGQNQFFEYTSQKEIRynTHQPEGCIAVEAGMD--TLIMHLCE 225
Cdd:pfam00652   1 ATGRIRNRA-SGKCLDVPGGSSA---GGPVGLYPCHGSNGNQLWTLTGDGTIR--SVASDLCLDVGSTADgaKVVLWPCH 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578817888  226 ETAPeNQKFILQEDGS-LFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKW 277
Cdd:pfam00652  75 PGNG-NQRWRYDEDGTqIRNPQSGKCLDVSGAGTSNGKVILWTCDSGNPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 156-280 3.09e-17

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 75.63  E-value: 3.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888   156 GLTDYCFDYNPPDENqivghqVILYLCHGMGQNQFFEYTSQKEIRynTHQPEGCIAVEAGMDTLI-MHLCEETAPeNQKF 234
Cdd:smart00458   4 GNTGKCLDVNGNKNP------VGLFDCHGTGGNQLWKLTSDGAIR--IKDTDLCLTANGNTGSTVtLYSCDGTND-NQYW 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 578817888   235 ILQEDGSLFHEQSKKCVQAarKESSDSFVPLLRDCTNSDHQKWFFK 280
Cdd:smart00458  75 EVNKDGTIRNPDSGKCLDV--KDGNTGTKVILWTCSGNPNQKWIFE 118
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 9-61 8.95e-04

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


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 37.21  E-value: 8.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578817888    9 RSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPC 61
Cdd:pfam02709  15 PYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG 67
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 146-282 3.59e-96

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: 278.99  E-value: 3.59e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 146 PGFFGMLQNKGLTDYCFDYNPPDENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHLCE 225
Cdd:cd23471    1 PGFFGMLKNKGMTNYCFDYNPPDEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTRQPEGCAAVDAGTDFLTMHLCR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 226 ET---APENQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFFKER 282
Cdd:cd23471   81 ENrqaVPENQKFIFREDGSLFHVQTQKCVQAVRNESSGSPAPVLRPCTDSDHQKWFFKER 140
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 2-136 3.34e-75

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: 231.71  E-value: 3.34e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888   2 QSPVDVIRSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPCSHVGHVFP-KQAPYSRNKAL 80
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888  81 A----NSVRAAEVWMDEFKELYYHRNPRARLEPFGDVTERKQLRDKLQCKDFKWFLETVY 136
Cdd:cd02510  240 GtvlrNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 146-280 4.72e-50

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: 161.35  E-value: 4.72e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 146 PGFFGMLQNKGlTDYCFDYNPPDENqiVGHQVILYLCHGMGQNQFFEYTSQKEIRYNThQPEGCIAVEaGMDTLIMHLCE 225
Cdd:cd23435    1 PGYYGALRNKG-SELCLDVNNPNGQ--GGKPVIMYGCHGLGGNQYFEYTSKGEIRHNI-GKELCLHAS-GSDEVILQHCT 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578817888 226 ET---APENQKFILQEDGSLFHEQSKKCVQAARKEssdsfvPLLRDCTNSD-HQKWFFK 280
Cdd:cd23435   76 SKgkdVPPEQKWLFTQDGTIRNPASGLCLHASGYK------VLLRTCNPSDdSQKWTFI 128
beta-trefoil_Ricin_GALNT4 cd23469
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 146-280 1.33e-27

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: 103.83  E-value: 1.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 146 PGFFGMLQNKGLTDYCFDYNPPDENQiVGHQVILYLCHGMGQNQFFEYTSQKEIRYNThQPEGCIAVEAGMDTLIMHLCE 225
Cdd:cd23469    1 PGWHGAVRSMGISSECLDYNSPEHNP-TGAHLSLFGCHGQGGNQFFEYTSNKEIRFNS-VTELCAEVPDQKNYIGMKHCP 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578817888 226 E---TAPENQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPlLRDCTNSD-HQKWFFK 280
Cdd:cd23469   79 KdgsPVPANIIWHFKEDGTIYHPHSGMCISAYRTPEGRADVQ-MRTCDAGDkNQLWSFE 136
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
148-277 2.07e-22

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 89.90  E-value: 2.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888  148 FFGMLQNKGlTDYCFDYNPPDENqivGHQVILYLCHGMGQNQFFEYTSQKEIRynTHQPEGCIAVEAGMD--TLIMHLCE 225
Cdd:pfam00652   1 ATGRIRNRA-SGKCLDVPGGSSA---GGPVGLYPCHGSNGNQLWTLTGDGTIR--SVASDLCLDVGSTADgaKVVLWPCH 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578817888  226 ETAPeNQKFILQEDGS-LFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKW 277
Cdd:pfam00652  75 PGNG-NQRWRYDEDGTqIRNPQSGKCLDVSGAGTSNGKVILWTCDSGNPNQQW 126
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 149-280 8.25e-21

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1)-like subfamily; The GALNT1-like subfamily includes GALNT1 and GALNT13. They catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT1 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT13 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467311 [Multi-domain]  Cd Length: 127  Bit Score: 85.44  E-value: 8.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 149 FGMLQNKGlTDYCFDYNPPDENQIVGhqviLYLCHGMGQNQFFEYTSQKEIRynthQPEGCIAVEAGMDTLIMHLCEETa 228
Cdd:cd23433    6 LGEIRNVE-TNLCLDTMGRKAGEKVG----LSSCHGQGGNQVFSYTAKGEIR----SDDLCLDASRKGGPVKLEKCHGM- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578817888 229 PENQKFIL-QEDGSLFHEQSKKCVQAARKESSDsfVPLLRDCTNSDHQKWFFK 280
Cdd:cd23433   76 GGNQEWEYdKETKQIRHVNSGLCLTAPNEDDPN--EPVLRPCDGGPSQKWELE 126
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 146-279 3.41e-20

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: 83.91  E-value: 3.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 146 PGFFGMLQNKGlTDYCFD-YN-PPDENQIVGhqviLYLCHGMGQ-NQFFEYTSQKEIRynthQPEGCIAVE-AGMDTLIM 221
Cdd:cd23459    4 VLAYGQVRNPG-TNLCLDtLQrDEDKGYNLG----LYPCQGGLSsNQLFSLSKKGELR----REESCADVQgTEESKVIL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578817888 222 HLCEETAPENQKFILQEDGSLFHEQSKKCVQAARKESSDSfvPLLRDCTNSDHQKWFF 279
Cdd:cd23459   75 ITCHGLEKFNQKWKHTKGGQIVHLASGKCLDAEGLKSGDD--VTLAKCDGSLSQKWTF 130
beta-trefoil_Ricin_GALNT3 cd23468
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 146-279 5.95e-19

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: 80.63  E-value: 5.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 146 PGFFGMLQNKGlTDYCFDYNppdENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNThQPEGCIAVEAGMdtLIMHLC- 224
Cdd:cd23468    2 PLIFGAIKNVG-KELCLDVG---ENNHGGKPLIMYNCHGLGGNQYFEYSTHHEIRHNI-QKELCLHGSQGS--VQLKECt 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 225 ----EETAPENQKFILQEDGSLFHEQSKKCVqaarkeSSDSFVPLLRDCTNSD-HQKWFF 279
Cdd:cd23468   75 ykgrNTAVLPEEKWELQKDQLLYNPALNMCL------SANGENPSLVPCNPSDpFQQWIF 128
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 145-278 8.80e-19

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: 80.18  E-value: 8.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 145 RPGFFGMLQNKGlTDYCFDYNPpdENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQPegCIAVEAgmDTLIMHLC 224
Cdd:cd23442    1 APYFSGQLYNTG-TGYCADYIH--GWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSLQL--CLDVRQ--EQVVLQNC 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578817888 225 EETApENQKFILQEDGSLFHEQSKKCVQAArkESSDSFVPLLRDCTNSDHQKWF 278
Cdd:cd23442   74 TKEK-TSQKWDFQETGRIVHILSGKCIEAV--ESENSKLLFLSPCNGQRNQMWK 124
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 156-280 3.09e-17

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 75.63  E-value: 3.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888   156 GLTDYCFDYNPPDENqivghqVILYLCHGMGQNQFFEYTSQKEIRynTHQPEGCIAVEAGMDTLI-MHLCEETAPeNQKF 234
Cdd:smart00458   4 GNTGKCLDVNGNKNP------VGLFDCHGTGGNQLWKLTSDGAIR--IKDTDLCLTANGNTGSTVtLYSCDGTND-NQYW 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 578817888   235 ILQEDGSLFHEQSKKCVQAarKESSDSFVPLLRDCTNSDHQKWFFK 280
Cdd:smart00458  75 EVNKDGTIRNPDSGKCLDV--KDGNTGTKVILWTCSGNPNQKWIFE 118
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 150-280 4.24e-17

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: 75.48  E-value: 4.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 150 GMLQNKGlTDYCFDynPPDENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNthqpEGCIAVEAGMDTLIMHLCEETaP 229
Cdd:cd23462    6 GEIRNLA-GKLCLD--APGRKKELNKPVGLYPCHGQGGNQYWMLTKDGEIRRD----DLCLDYAGGSGDVTLYPCHGM-K 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578817888 230 ENQKFIL-QEDGSLFHEQSKKCVQAarkeSSDSFVPLLRDCT-NSDHQKWFFK 280
Cdd:cd23462   78 GNQFWIYdEETKQIVHGTSKKCLEL----SDDSSKLVMEPCNgSSPRQQWEFE 126
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 150-281 1.55e-15

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: 71.17  E-value: 1.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 150 GMLQNKGlTDYCFDYNPPDENQIVGhqviLYLCHGMGQNQFFEYTSQKEIRYNthqpEGCIAVEAGMDTLIMHLCEetAP 229
Cdd:cd23437    6 GEIRNLG-TGLCLDTMGHQNGGPVG----LYPCHGMGGNQLFRLNEAGQLAVG----EQCLTASGSGGKVKLRKCN--LG 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578817888 230 ENQKFILQE-DGSLFHEQSKKCVQaarKESSDSFVpLLRDCTN-SDHQKWFFKE 281
Cdd:cd23437   75 ETGKWEYDEaTGQIRHKGTGKCLD---LNEGTNKL-ILQPCDSsSPSQKWEFNE 124
beta-trefoil_Ricin_GALNT6 cd23470
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 146-279 2.02e-15

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: 71.05  E-value: 2.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 146 PGFFGMLQNKGlTDYCFDYNppdENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQpEGCIAVEAG---MDTLIMH 222
Cdd:cd23470    1 PTFYGAIKNEG-TNQCLDVG---ENNRGGKPLIMYSCHGMGGNQYFEYTTHKELRHNIAK-QLCLRVSKGpvqLGECHYK 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578817888 223 LCEETAPENQKFILQEDGSLFHEQSKKCVQAARKEssdsfvPLLRDCTNSD-HQKWFF 279
Cdd:cd23470   76 GKNSQVPPDEEWELTQDHLIRNSGSNMCLTARGKH------PAMAPCNPADpHQLWSF 127
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 158-280 7.97e-15

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: 69.69  E-value: 7.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 158 TDYCFDYNPPDENQIVGhqviLYLCHGMGQNQFFEYTSQKEIRYNthqpEGCIAVEAGMDTLIMHLCEETApENQkfILQ 237
Cdd:cd23466   14 TNQCLDNMARKENEKVG----IFNCHGMGGNQVFSYTANKEIRTD----DLCLDVSKLNGPVMMLKCHHLK-GNQ--LWE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 578817888 238 EDG---SLFHEQSKKCVQAARKEssDSFVPLLRDCTNSDHQKWFFK 280
Cdd:cd23466   83 YDPvklTLLHVNSNQCLDKATEE--DSQVPSIRDCNGSRSQQWLLR 126
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 150-279 1.49e-13

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: 66.22  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 150 GMLQNKgltdyCFDYnpPDENQIVGHQVILYLCHGmGQNQFFEYTSQKEIRyntHQPEGCIAVEAGM----DTLIMHLCE 225
Cdd:cd23418   10 GYGSGR-----CLDV--PGGSTTNGTRLILWDCHG-GANQQFTFTSAGELR---VGGDKCLDAAGGGttngTPVVIWPCN 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578817888 226 ETApeNQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFF 279
Cdd:cd23418   79 GGA--NQKWRFNSDGTIRNVNSGLCLDVAGGGTANGTRLILWSCNGGSNQRWRR 130
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 158-280 5.52e-13

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: 64.66  E-value: 5.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 158 TDYCFDYNPPDENQIVGhqviLYLCHGMGQNQFFEYTSQKEIRYNthqpEGCIAVEAGMDTLIMHLCEETApENQKFILQ 237
Cdd:cd23467   14 TNQCLDNMGRKENEKVG----IFNCHGMGGNQVFSYTADKEIRTD----DLCLDVSRLNGPVVMLKCHHMR-GNQLWEYD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 578817888 238 -EDGSLFHEQSKKCVQAARKEssDSFVPLLRDCTNSDHQKWFFK 280
Cdd:cd23467   85 aERLTLRHVNSNQCLDEPSEE--DKMVPTMKDCSGSRSQQWLLR 126
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 148-280 7.35e-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: 7.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 148 FFGMLQNKGlTDYCFDYNPPDENQIVghqVILYLCHGMGQNQFFEYTSQKEIRYNTHqpegCI-AVEAGMDTLImhLCEE 226
Cdd:cd23460    1 GLGQIKHTE-SGLCLDWAGESNGDKT---VALKPCHGGGGNQFWMYTGDGQIRQDHL----CLtADEGNKVTLR--ECAD 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578817888 227 TAPeNQKFILQEDGS-LFHEQSKKCVQAARKEssdsFVPLLRDCTNSDH-QKWFFK 280
Cdd:cd23460   71 QLP-SQEWSYDEKTGtIRHRSTGLCLTLDANN----DVVILKECDSNSLwQKWIFQ 121
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 172-279 9.14e-08

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: 49.63  E-value: 9.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 172 IVGHQVILYLCHGMGQNQFFEYTSQKEIRynthQPEGCIAVE--AGMDTLIMHLCEETApENQKFILQEDGSLF-HEQSK 248
Cdd:cd23434   18 KAGGTVGLYPCHGTGGNQEWSFTKDGQIK----HDDLCLTVVdrAPGSLVTLQPCREDD-SNQKWEQIENNSKLrHVGSN 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 578817888 249 KCVqAARKESSDSFVplLRDCTNSDH-QKWFF 279
Cdd:cd23434   93 LCL-DSRNAKSGGLT--VETCDPSSGsQQWKF 121
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 174-277 2.89e-07

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


Pssm-ID: 467329 [Multi-domain]  Cd Length: 125  Bit Score: 48.48  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 174 GHQVILYLCHGMGqNQFFEYTSQKEIRYNTHqpegCIAVEAGMDT----LIMHLCEETApeNQKFILQEDGSLFHEQSKK 249
Cdd:cd23451   24 GNPVQIYTCNGTA-AQKWTLGTDGTLRVLGK----CLDVSGGGTAngtlVQLWDCNGTG--AQKWVPRADGTLYNPQSGK 96

                         90       100
                 ....*....|....*....|....*...
gi 578817888 250 CVQAARKESSDSFVPLLRDCTNSDHQKW 277
Cdd:cd23451   97 CLDAPGGSTTDGTQLQLYTCNGTAAQQW 124
beta-trefoil_Ricin_GALNT8-like cd23438
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 148-280 3.46e-07

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: 48.58  E-value: 3.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 148 FFGMLQNKGLTDYCFDYNPpdenqIVGHQVILYLCHGMGQnQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHL---- 223
Cdd:cd23438    4 AYGEMRNSLVTDLCLDQGP-----KENHTAILYPCHGWSP-QLVRYTKDGQLYLGQLGSTASPDTRCLVDDGKSDKpqll 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578817888 224 -CEETAPENQK-FILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNsdhQKWFFK 280
Cdd:cd23438   78 dCSKVKNRLQKyWDFSQGGAIQNRATGRCLEVEEDKLNFGHRLVLQTCSG---QKWNIK 133
beta-trefoil_Ricin_GALNT18 cd23475
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 149-277 1.25e-06

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: 46.84  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 149 FGMLQNKGLTDYCFDYNPPDENqivghQVILYLCHGMG-QNQFfeYTSQKEIRYNTHQP------EGCIAVEAGMDTLIM 221
Cdd:cd23475   10 YGVLQNSLKTDLCLDQGPDTDN-----IPIMYICHGMTpQNVY--YTSNQQLHVGILSPtiddddNRCLVDVNSRPRLIE 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817888 222 hlCEETAPENQKFILQ--EDGSLFHEQSKKCVQAarKESSDS---FVPLLRDCTNsdhQKW 277
Cdd:cd23475   83 --CSYAKAKRMKLYWLftQGGSIQNKKSKRCLEL--QENADNefgYQLVLQKCSG---QRW 136
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 149-277 4.37e-06

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


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 45.44  E-value: 4.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 149 FGMLQNKGlTDYCFDynPPDENQIVGHQVILYLCHGmGQNQFFEYTSQKEIRY-----NTHQpegCIAVEAGMDT----L 219
Cdd:cd00161    2 TYRIVNAA-SGKCLD--VAGGSTANGAPVQQWTCNG-GANQQWTLTPVGDGYYtirnvASGK---CLDVAGGSTAnganV 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817888 220 IMHLCEETApeNQKFILQEDGS----LFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKW 277
Cdd:cd00161   75 QQWTCNGGD--NQQWRLEPVGDgyyrIVNKHSGKCLDVSGGSTANGANVQQWTCNGGANQQW 134
beta-trefoil_Ricin_GALNT8 cd23472
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 136-277 2.64e-05

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: 43.27  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 136 YPELhVPEDRPGFFGMLQNKGLTDYCFDYNPpdenqIVGHQVILYLCHGMGQnQFFEYTSQKEI--------RYNTHQpe 207
Cdd:cd23472    1 YPVL-MPIQTIVGYGTMKNSLNENICIDQGP-----VPGNTPIMYGCHGYSP-QFVYYHLTGELyvgglkadIYASDR-- 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817888 208 gCIAVEAGMDTLIMHLCEETAPE--NQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNsdhQKW 277
Cdd:cd23472   72 -CLTDPGEGWKPELVSCQDATLKglNMYWDFKQGTAIINRKTKRCLEISLDKTPSYYTLILQTCTG---QKW 139
beta-trefoil_Ricin_GALNT17 cd23474
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 149-280 4.60e-05

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: 42.58  E-value: 4.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 149 FGMLQNKGLTDYCFDYNPPdENqivgHQVILYLCHGMGQnQFFEYTSQKEIRY-----NTHQPEGCIAVEAGMDTLIMHL 223
Cdd:cd23474   10 YGELRNNKAKDVCLDQGPP-EN----HTAILYPCHGWGP-QLARYTKEGYLHLgalgtTTLLPDTRCLVDNKKSRFPQLL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817888 224 -CEETAPENQK---FIlqEDGSLFHEQSKKCVQAARKeSSDSFVPLLRDCTNsdhQKWFFK 280
Cdd:cd23474   84 dCDKVKSILHKrwnFI--QNGAIMNLGTGRCLEVENR-GNFGIDLILRSCTG---QRWTIK 138
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 158-233 2.55e-04

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10)-like subfamily; The GALNT10-like subfamily includes GALNT10 and GALNTL6. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467317 [Multi-domain]  Cd Length: 126  Bit Score: 40.02  E-value: 2.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578817888 158 TDYCFDynppDENQIVGHQVILYLCHGMGQNQFFEY-TSQKEIRYNTHQpeGCIAVEAGMDTLIMHLCEETAPeNQK 233
Cdd:cd23439   54 RKVCFD----VSSHTPGAPVILYACHGMKGNQLWKYrPNTKQLYHPVSG--LCLDADPGSGKVFMNHCDESSD-TQK 123
beta-trefoil_Ricin_GALNT9 cd23473
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 149-280 3.02e-04

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: 40.33  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 149 FGMLQNKGLTDYCFDYNPPDENQivghqVILYLCHGMgQNQFFEYTSQKEIRYN-----THQPEG-CIAVEAGMDTLIMH 222
Cdd:cd23473   10 YGEVRNSKASGYCLDQGSEEDDK-----AILYPCHGM-SSQLVRYSTEGLLQLGplgstAFLPDTkCLVDDGRGRTPTLK 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 223 LCEETAPENQKFI-LQEDGSLFHEQSKKCVQAA-RKESSDSFVPLLRDCTNsdhQKWFFK 280
Cdd:cd23473   84 KCEDVARPAQRLWdFTQNGPIISRDTGRCLEVEmSKDANFGLRLVVQRCSG---QKWMIR 140
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 9-61 8.95e-04

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


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 37.21  E-value: 8.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578817888    9 RSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPC 61
Cdd:pfam02709  15 PYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG 67
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 174-277 1.00e-03

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts 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: 467336 [Multi-domain]  Cd Length: 135  Bit Score: 38.46  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 174 GHQVILYLCHGmGQNQFFEYTSQK----EIRYNTHQPegCIAVEAG--MDTLIMHL--CEETApeNQKFILQEDGSLFHE 245
Cdd:cd23458   24 GANIQQWDCGS-GSNQQWTLVEIDngyyRIKASHSGK--CLDVAGGstANGANIQQwdCVGGA--NQQWKLQDLGNGYFE 98

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 578817888 246 ----QSKKCVQAARKESSDSFVPLLRDCTNSDHQKW 277
Cdd:cd23458   99 lkarHSGKCLDVAGGSTANGASIQQWTCNGNDNQRF 134
beta-trefoil_Ricin_GALNT5 cd23436
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 150-279 2.92e-03

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


Pssm-ID: 467314  Cd Length: 132  Bit Score: 37.08  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 150 GMLQNKGlTDYCFDYNPPDenqivghqVILYLCHGMGQNQFFEYTSQKEIRynthQPEGCIAVEAGMDTLIMHLCEETAP 229
Cdd:cd23436    7 GLLVNVA-LRKCIAIENTT--------LTLQDCDLNNKSQHFNYTWLRLIR----QGELCLAPVEAEGALTLHPCDNTNN 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 230 eNQKFI---------LQEDGSLFHEQSKKCVQAARKessdSFVPLLRDCTNSD-HQKWFF 279
Cdd:cd23436   74 -GLRWLhksliafpeLMDHIMLEHQSQPTCLEADPS----QKILRLNACDSFKrYQKWRF 128
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
 156-277 4.01e-03

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: 36.72  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817888 156 GLTDYCFDynPPDENQIVGHQVILYLCHGMGQnQFFEYTSQKEIRYNTHqpegCI-AVEAGMD---TLIMHLCEETApeN 231
Cdd:cd23452    8 GLANKCID--VPNSSTTDGAPLQLWDCNGTNA-QKWTFASDGTLRALGK----CLdVAWGGTDngtAVQLWTCSGNP--A 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 578817888 232 QKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKW 277
Cdd:cd23452   79 QQFVLSGAGDLVNPQANKCVDVSGGNSGNGTRLQLWECSGNANQKW 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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