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Conserved domains on  [gi|975830131|ref|NP_001305981|]
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polypeptide N-acetylgalactosaminyltransferase 15 isoform 3 [Homo sapiens]

Protein Classification

RICIN domain-containing protein( domain architecture ID 12006040)

RICIN domain-containing protein may have carbohydrate-binding function; similar to Salmonella enterica lipoprotein EnvE

Gene Ontology:  GO:0030246
PubMed:  8844840|35536958

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 32-159 1.12e-60

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: 183.80  E-value: 1.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  32 RPSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpQHLCFAVRQEQVILQNCTEEgla 111
Cdd:cd23442    1 APYFSGQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGS-LQLCLDVRQEQVVLQNCTKE--- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 975830131 112 IHQQHWDFQENGMIVHILSGKCMEAVVQENNKDLYLRPCDGKARQQWR 159
Cdd:cd23442   77 KTSQKWDFQETGRIVHILSGKCIEAVESENSKLLFLSPCNGQRNQMWK 124
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 1-23 1.44e-05

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: 43.73  E-value: 1.44e-05
                         10        20
                 ....*....|....*....|...
gi 975830131   1 MERLQLQRRLGCRTFHWFLANVY 23
Cdd:cd02510  277 SERKALRERLKCKSFKWYLENVY 299
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 32-159 1.12e-60

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: 183.80  E-value: 1.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  32 RPSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpQHLCFAVRQEQVILQNCTEEgla 111
Cdd:cd23442    1 APYFSGQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGS-LQLCLDVRQEQVVLQNCTKE--- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 975830131 112 IHQQHWDFQENGMIVHILSGKCMEAVVQENNKDLYLRPCDGKARQQWR 159
Cdd:cd23442   77 KTSQKWDFQETGRIVHILSGKCIEAVESENSKLLFLSPCNGQRNQMWK 124
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
35-158 6.78e-23

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 87.97  E-value: 6.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131   35 FSGKLHNTGLGLCADCQAeGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQhLCFAVRQE----QVILQNCTEEGl 110
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPG-GSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVASD-LCLDVGSTadgaKVVLWPCHPGN- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 975830131  111 aiHQQHWDFQENG-MIVHILSGKCMEAVVQEN-NKDLYLRPCD-GKARQQW 158
Cdd:pfam00652  78 --GNQRWRYDEDGtQIRNPQSGKCLDVSGAGTsNGKVILWTCDsGNPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 43-160 2.56e-11

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 57.52  E-value: 2.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131    43 GLGLCADCQAEGDilgcPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQhLCFAVRQ---EQVILQNCTEEGLAihqQHWDF 119
Cdd:smart00458   5 NTGKCLDVNGNKN----PVGLFDCHGTGGNQLWKLTSDGAIRIKDTD-LCLTANGntgSTVTLYSCDGTNDN---QYWEV 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 975830131   120 QENGMIVHILSGKCMEAVVQENNKDLYLRPCDGKARQQWRF 160
Cdd:smart00458  77 NKDGTIRNPDSGKCLDVKDGNTGTKVILWTCSGNPNQKWIF 117
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 1-23 1.44e-05

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: 43.73  E-value: 1.44e-05
                         10        20
                 ....*....|....*....|...
gi 975830131   1 MERLQLQRRLGCRTFHWFLANVY 23
Cdd:cd02510  277 SERKALRERLKCKSFKWYLENVY 299
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 32-159 1.12e-60

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: 183.80  E-value: 1.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  32 RPSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpQHLCFAVRQEQVILQNCTEEgla 111
Cdd:cd23442    1 APYFSGQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGS-LQLCLDVRQEQVVLQNCTKE--- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 975830131 112 IHQQHWDFQENGMIVHILSGKCMEAVVQENNKDLYLRPCDGKARQQWR 159
Cdd:cd23442   77 KTSQKWDFQETGRIVHILSGKCIEAVESENSKLLFLSPCNGQRNQMWK 124
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
35-158 6.78e-23

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 87.97  E-value: 6.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131   35 FSGKLHNTGLGLCADCQAeGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQhLCFAVRQE----QVILQNCTEEGl 110
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPG-GSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVASD-LCLDVGSTadgaKVVLWPCHPGN- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 975830131  111 aiHQQHWDFQENG-MIVHILSGKCMEAVVQEN-NKDLYLRPCD-GKARQQW 158
Cdd:pfam00652  78 --GNQRWRYDEDGtQIRNPQSGKCLDVSGAGTsNGKVILWTCDsGNPNQQW 126
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 33-161 1.69e-18

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: 76.60  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  33 PSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQHLCFAVRQEQ-VILQNCTEEGLA 111
Cdd:cd23435    1 PGYYGALRNKGSELCLDVNNPNGQGGKPVIMYGCHGLGGNQYFEYTSKGEIRHNIGKELCLHASGSDeVILQHCTSKGKD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 975830131 112 I-HQQHWDFQENGMIVHILSGKCMEAvvqeNNKDLYLRPCDGKAR-QQWRFD 161
Cdd:cd23435   81 VpPEQKWLFTQDGTIRNPASGLCLHA----SGYKVLLRTCNPSDDsQKWTFI 128
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 36-161 5.40e-15

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: 67.39  E-value: 5.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  36 SGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGspqHLC--FAVRQEQVILQNCteeglaiH 113
Cdd:cd23462    5 YGEIRNLAGKLCLDAPGRKKELNKPVGLYPCHGQGGNQYWMLTKDGEIRRD---DLCldYAGGSGDVTLYPC-------H 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 975830131 114 Q----QHWDF-QENGMIVHILSGKCMEavVQENNKDLYLRPCDGKA-RQQWRFD 161
Cdd:cd23462   75 GmkgnQFWIYdEETKQIVHGTSKKCLE--LSDDSSKLVMEPCNGSSpRQQWEFE 126
beta-trefoil_Ricin_GALNT4 cd23469
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 33-161 4.98e-13

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: 62.61  E-value: 4.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  33 PSFSGKLHNTGL-GLCADCQA-EGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQHLCFAVRQEQ--VILQNCTEE 108
Cdd:cd23469    1 PGWHGAVRSMGIsSECLDYNSpEHNPTGAHLSLFGCHGQGGNQFFEYTSNKEIRFNSVTELCAEVPDQKnyIGMKHCPKD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 975830131 109 GLAIHQQ-HWDFQENGMIVHILSGKCMEAV-VQENNKDLYLRPCD-GKARQQWRFD 161
Cdd:cd23469   81 GSPVPANiIWHFKEDGTIYHPHSGMCISAYrTPEGRADVQMRTCDaGDKNQLWSFE 136
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 33-162 6.15e-13

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: 62.51  E-value: 6.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  33 PSFSGKLHNTGL-GLCADCQA--EGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQ-HLCFAVR--QEQVILQNCT 106
Cdd:cd23471    1 PGFFGMLKNKGMtNYCFDYNPpdEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTRQpEGCAAVDagTDFLTMHLCR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 975830131 107 EEGLAI-HQQHWDFQENGMIVHILSGKCMEAVVQENNKDL--YLRPCDGKARQQWRFDQ 162
Cdd:cd23471   81 ENRQAVpENQKFIFREDGSLFHVQTQKCVQAVRNESSGSPapVLRPCTDSDHQKWFFKE 139
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 43-160 2.56e-11

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 57.52  E-value: 2.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131    43 GLGLCADCQAEGDilgcPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQhLCFAVRQ---EQVILQNCTEEGLAihqQHWDF 119
Cdd:smart00458   5 NTGKCLDVNGNKN----PVGLFDCHGTGGNQLWKLTSDGAIRIKDTD-LCLTANGntgSTVTLYSCDGTNDN---QYWEV 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 975830131   120 QENGMIVHILSGKCMEAVVQENNKDLYLRPCDGKARQQWRF 160
Cdd:smart00458  77 NKDGTIRNPDSGKCLDVKDGNTGTKVILWTCSGNPNQKWIF 117
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 31-165 3.72e-11

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10) and similar proteins; GALNT10 (EC 2.4.1.41), also called polypeptide GalNAc transferase 10, GalNAc-T10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. GALNT10 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467354  Cd Length: 150  Bit Score: 58.05  E-value: 3.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  31 PRPSFsGKLHNTGLGLCADcqAEGDILGCPMVLAPCSDSR------QQQYLQHTSRKEIHFGSPQH---LCF-AVRQEQ- 99
Cdd:cd23476    3 PAAAW-GEIRNVGTGLCAD--TKHGALGSPLRLEGCVKGRgeaawnNGQVFTFGWREDIRPGDPQHtkkFCFdAISHNSp 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 975830131 100 VILQNCteEGLAiHQQHWDFQENGMIVHILSGKCMEAvvQENNKDLYLRPCDGKA-RQQWRFDQINA 165
Cdd:cd23476   80 VTLYDC--HGMK-GNQLWRYRKDKTLYHPVSNSCMDC--SESDHRIFMNTCNPSSpTQQWLFEHTNS 141
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 37-160 5.49e-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: 56.68  E-value: 5.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  37 GKLHNTGLGLCADCQAEGDILGCPmVLAPCSDSRQQQYLQHTSRKEIHFGspqHLCFAVRQ-EQVILQNCTEEGLAihqQ 115
Cdd:cd23460    3 GQIKHTESGLCLDWAGESNGDKTV-ALKPCHGGGGNQFWMYTGDGQIRQD---HLCLTADEgNKVTLRECADQLPS---Q 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 975830131 116 HWDFQENGM-IVHILSGKCMEavVQENNKDLYLRPCDGKA-RQQWRF 160
Cdd:cd23460   76 EWSYDEKTGtIRHRSTGLCLT--LDANNDVVILKECDSNSlWQKWIF 120
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 37-160 1.00e-10

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: 56.23  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  37 GKLHNTGLGLCAdcQAEGDIL--GCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpqHLCFAV---RQEQVILQNCTEEGLA 111
Cdd:cd23440    6 GQLKHAGSGLCL--VAEDEVSqkGSLLVLRPCSRNDKKQLWYYTEDGELRLAN--LLCLDSsetSSDFPRLMKCHGSGGS 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 975830131 112 ihqQHWDFQENGMIVHILSGKCMEAVVQENNKDLYLRPCDGKARQQWRF 160
Cdd:cd23440   82 ---QQWRFKKDNRLYNPASGQCLAASKNGTSGYVTMDICSDSPSQKWVF 127
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 35-160 1.24e-10

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: 55.76  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  35 FSGKLHNTGLGLCADCQAEGDilGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpqhLCFAVR--QEQVILQNCTEEGlai 112
Cdd:cd23437    4 AWGEIRNLGTGLCLDTMGHQN--GGPVGLYPCHGMGGNQLFRLNEAGQLAVGE---QCLTASgsGGKVKLRKCNLGE--- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 975830131 113 hQQHWDFQE-NGMIVHILSGKCMEavVQENNKDLYLRPCDG-KARQQWRF 160
Cdd:cd23437   76 -TGKWEYDEaTGQIRHKGTGKCLD--LNEGTNKLILQPCDSsSPSQKWEF 122
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 36-160 3.88e-10

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


Pssm-ID: 467317 [Multi-domain]  Cd Length: 126  Bit Score: 54.66  E-value: 3.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  36 SGKLHNTGLGLCADCQAEGdiLGCPMVLAPCSDSRQQ--QYLQHTSRKEIHFGSPQHlCF----AVRQEQVILQNCteeg 109
Cdd:cd23439    2 SGEIRNVGSGLCIDTKHGG--ENDEVRLSKCVKDGGGgeQQFELTWHEDIRPKKRKV-CFdvssHTPGAPVILYAC---- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 975830131 110 laiHQ----QHWDFQEN-GMIVHILSGKCMEAVvqENNKDLYLRPCD-GKARQQWRF 160
Cdd:cd23439   75 ---HGmkgnQLWKYRPNtKQLYHPVSGLCLDAD--PGSGKVFMNHCDeSSDTQKWTW 126
beta-trefoil_Ricin_GALNTL6 cd23477
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 30-165 2.28e-09

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase-like 6 (GALNTL6) and similar proteins; GALNTL6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 17, GalNAc-T17, pp-GaNTase 17, protein-UDP acetylgalactosaminyltransferase 17, putative polypeptide N-acetylgalactosaminyltransferase 17, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNTL6 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467355  Cd Length: 148  Bit Score: 53.02  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  30 EPRPSFSGKLHNTGLGLCADCQ--AEGDILGCPMVLAPCSDS--RQQQYLQHTSRKEIHFGSPQH---LCF-AVRQEQ-V 100
Cdd:cd23477    1 EPPPAAWGEIRNVAANLCVDSKhgATGTELRLDICVKDGSERtwSHEQLFTFGWREDIRPGEPLHtrkFCFdAISHNSpV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 975830131 101 ILQNCteEGLAiHQQHWDFQENGMIVHILSGKCMEAvvQENNKDLYLRPCDGK-ARQQWRFDQINA 165
Cdd:cd23477   81 TLYDC--HGMK-GNQLWSYRKDKTLFHPVSNSCMDC--NPADKKIFMNRCDPLsETQQWIFEHTNM 141
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 99-161 4.89e-09

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: 51.94  E-value: 4.89e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 975830131  99 QVILQNCTEEGLAihQQHWDFQENGMIVHILSGKCMEAVVQENNKDLYLRPCDGKARQQWRFD 161
Cdd:cd23459   71 KVILITCHGLEKF--NQKWKHTKGGQIVHLASGKCLDAEGLKSGDDVTLAKCDGSLSQKWTFE 131
beta-trefoil_Ricin_GALNT3 cd23468
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 33-160 6.55e-09

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: 51.35  E-value: 6.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  33 PSFSGKLHNTGLGLCADCqAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQHLCFAVRQEQVILQNCTEEG--- 109
Cdd:cd23468    2 PLIFGAIKNVGKELCLDV-GENNHGGKPLIMYNCHGLGGNQYFEYSTHHEIRHNIQKELCLHGSQGSVQLKECTYKGrnt 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 975830131 110 LAIHQQHWDFQENGMIVHILSGKCMEA------VVQENNKDLYlrpcdgkarQQWRF 160
Cdd:cd23468   81 AVLPEEKWELQKDQLLYNPALNMCLSAngenpsLVPCNPSDPF---------QQWIF 128
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 36-158 8.15e-09

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: 51.22  E-value: 8.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  36 SGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQ-YLQHTSRKEIHFGSPQH-LCFAVRQ------EQVILQNCTe 107
Cdd:cd00161    2 TYRIVNAASGKCLDVAGGSTANGAPVQQWTCNGGANQQwTLTPVGDGYYTIRNVASgKCLDVAGgstangANVQQWTCN- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 975830131 108 eGLAihQQHWDFQENG----MIVHILSGKCMEAV--VQENNKDLYLRPCDGKARQQW 158
Cdd:cd00161   81 -GGD--NQQWRLEPVGdgyyRIVNKHSGKCLDVSggSTANGANVQQWTCNGGANQQW 134
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 46-160 1.51e-08

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: 50.48  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  46 LCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpqhLCFAVRQEQ----VILQNCTEEGlaihQQHWDFQE 121
Cdd:cd23441   13 LCLDSDEQLFQGPALLILAPCSNSSDSQEWSFTKDGQLQTQG---LCLTVDSSSkdlpVVLETCSDDP----KQKWTRTG 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 975830131 122 nGMIVHILSGKCMEAVVQennKDLYLRPC-DGKARQQWRF 160
Cdd:cd23441   86 -RQLVHSESGLCLDSRKK---KGLVVSPCrSGAPSQKWDF 121
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 37-160 1.70e-07

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: 47.69  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  37 GKLHNTGLGLCADC--QAEGDILGcpmvLAPCSDSRQQQYLQHTSRKEIHFGSpqhLCFAVRQ--EQVILQNCTEEGLai 112
Cdd:cd23433    7 GEIRNVETNLCLDTmgRKAGEKVG----LSSCHGQGGNQVFSYTAKGEIRSDD---LCLDASRkgGPVKLEKCHGMGG-- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 975830131 113 hQQHWDF-QENGMIVHILSGKCMEAVVQENNKDLYLRPCDGKARQQWRF 160
Cdd:cd23433   78 -NQEWEYdKETKQIRHVNSGLCLTAPNEDDPNEPVLRPCDGGPSQKWEL 125
beta-trefoil_Ricin_GALNT6 cd23470
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 33-160 3.54e-07

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: 46.79  E-value: 3.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  33 PSFSGKLHNTGLGLCADCqAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQHLCFAVRQEQVILQNCTEEGLAI 112
Cdd:cd23470    1 PTFYGAIKNEGTNQCLDV-GENNRGGKPLIMYSCHGMGGNQYFEYTTHKELRHNIAKQLCLRVSKGPVQLGECHYKGKNS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 975830131 113 H---QQHWDFQENGMIVHILSGKCMEAvvqeNNKDLYLRPCD-GKARQQWRF 160
Cdd:cd23470   80 QvppDEEWELTQDHLIRNSGSNMCLTA----RGKHPAMAPCNpADPHQLWSF 127
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 36-160 1.86e-06

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: 45.03  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  36 SGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpqhLCFAV------RQEQVILQNCTEEG 109
Cdd:cd23418    5 GGQIRGYGSGRCLDVPGGSTTNGTRLILWDCHGGANQQFTFTSAGELRVGGD---KCLDAagggttNGTPVVIWPCNGGA 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 975830131 110 LaihqQHWDFQENGMIVHILSGKCMEAV--VQENNKDLYLRPCDGKARQQWRF 160
Cdd:cd23418   82 N----QKWRFNSDGTIRNVNSGLCLDVAggGTANGTRLILWSCNGGSNQRWRR 130
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 99-162 7.10e-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: 43.51  E-value: 7.10e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  99 QVILQNCTEEGlaihQQHWDFQENG----MIVHILSGKCMEAV--VQENNKDLYLRPCDGKARQQWRFDQ 162
Cdd:cd00161   26 PVQQWTCNGGA----NQQWTLTPVGdgyyTIRNVASGKCLDVAggSTANGANVQQWTCNGGDNQQWRLEP 91
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 1-23 1.44e-05

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: 43.73  E-value: 1.44e-05
                         10        20
                 ....*....|....*....|...
gi 975830131   1 MERLQLQRRLGCRTFHWFLANVY 23
Cdd:cd02510  277 SERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 90-160 4.47e-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: 40.77  E-value: 4.47e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 975830131  90 HLCFAV----RQEQVILQNCTEEGlaiHQQHWDFQENG-MIVHILSGKCMeAVVQENNKDLYLRPCDGK-ARQQWRF 160
Cdd:cd23434   49 DLCLTVvdraPGSLVTLQPCREDD---SNQKWEQIENNsKLRHVGSNLCL-DSRNAKSGGLTVETCDPSsGSQQWKF 121
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 99-161 6.77e-05

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


Pssm-ID: 467334 [Multi-domain]  Cd Length: 122  Bit Score: 40.42  E-value: 6.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 975830131  99 QVILQNCTEEglaiHQQHWDFQENGMIVHIL-SGKCMEAV-VQENNKDLYLRPCDGKARQQWRFD 161
Cdd:cd23456   25 NVVVYDCNNS----NSQKWYYDATGRLHSKAnPGKCLDAGgENSNGANVVLWACNDSANQRWDFD 85
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 35-159 9.47e-05

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: 40.01  E-value: 9.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  35 FSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYlQHTSRKEIHFgspQHLCFAVRQ------EQVILQNCTEE 108
Cdd:cd23451    1 GTGPVRLANAGKCLDVPGSSTADGNPVQIYTCNGTAAQKW-TLGTDGTLRV---LGKCLDVSGggtangTLVQLWDCNGT 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 975830131 109 GlaiHQQhWDFQENGMIVHILSGKCMEA--VVQENNKDLYLRPCDGKARQQWR 159
Cdd:cd23451   77 G---AQK-WVPRADGTLYNPQSGKCLDApgGSTTDGTQLQLYTCNGTAAQQWT 125
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 89-159 3.17e-04

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 38.73  E-value: 3.17e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 975830131  89 QHLCFAVRQE--QVILQNCTEEGLAihqQHWDFQENGMIVHILSGKCMEAVVQENNKDLYLRPCDGK-ARQQWR 159
Cdd:cd23385   10 LGKCLAARSSssKVSLSTCNPNSPN---QQWKWTSGHRLFNVGTGKCLGVSSSSPSSPLRLFECDSEdELQKWK 80
beta-trefoil_Ricin_ebulin-like_rpt2 cd23490
second ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and ...
 66-161 4.18e-04

second ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and similar proteins; This subfamily includes Sambucus ebulus ebulin I and Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf. Ebulin l is a type II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus. It is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. It is considered a nontoxic type II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type II RIP like ricin. Ebulin l binds an A-chain substrate analogue, pteroic acid. It binds bind galactose and lactose in subdomain 1alpha in a similar manner to that of ricin. In contrast, it binds only the monosaccharide galactose, and not the disaccharide lactose in subdomain 2gamma. SNAV is a non-toxic GalNAc-specific type II RIP which strongly inhibits mammalian protein synthesis but does not affect plant nor bacterial protein synthesis. SNAI is Neu5Ac(alpha2-6)Gal/GalNAc specific agglutinin. It also acts as a type II RIP that strongly inhibits mammalian but not plant ribosomes. SNAI' is another NeuAc(alpha2,6)Gal/GalNAc binding type II RIP from elderberry (Sambucus nigra) bark. It is a minor bark protein which closely resembles the major Neu5Ac(alpha2,6)Gal/GalNAc binding type II RIP, SNAI, with respect to its carbohydrate-binding specificity and ribosome-inactivating activity but has a different molecular structure due to a single cysteine residue present in the B chain of SNAI but absent from SNAI'. SNAIf is fruit specific SNAI. It functions as fetuin-binding fruit lectin. Like Ebulin l, SNAV, SNAI, SNAI' and SNAIf consist of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain. It may also be responsible for cell agglutination (lectin activity). The B chain contains two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the second ricin B-type lectin domain.


Pssm-ID: 467368 [Multi-domain]  Cd Length: 125  Bit Score: 38.21  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  66 CSDSRQQQYLQHTSRKEIHFGSPQHLCFA----VRQEQVILQNCteEGLAihQQHWDFQENGMIVHILSGKCMEavVQEN 141
Cdd:cd23490   28 CVVTSVQQQWALYGDGTIRVNSDRSLCVTsngyNSKDLIIILKC--QGLP--NQRWVFNTDGTIVNPNSKLVMD--VKQS 101

                         90       100
                 ....*....|....*....|...
gi 975830131 142 NKDL---YLRPCDGKARQQWRFD 161
Cdd:cd23490  102 DVSLreiILFPPTGNPNQQWITQ 124
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 115-160 1.01e-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: 37.03  E-value: 1.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 975830131 115 QHWDF----QENGMIVHILSGKCMEAvvqENNKDLYLRPCDGKARQQWRF 160
Cdd:cd23415   33 QRWTWsgvgDGTVTLRNAATGRCLDS---NGNGGVYTLPCNGGSYQRWRV 79
beta-trefoil_Ricin_GALNT8-like cd23438
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 114-160 1.14e-03

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: 37.41  E-value: 1.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 975830131 114 QQHWDFQENGMIVHILSGKCMEavVQENNKD----LYLRPCDGkarQQWRF 160
Cdd:cd23438   87 QKYWDFSQGGAIQNRATGRCLE--VEEDKLNfghrLVLQTCSG---QKWNI 132
beta-trefoil_Ricin_GALNT17 cd23474
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 112-158 1.15e-03

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


Pssm-ID: 467352  Cd Length: 142  Bit Score: 37.18  E-value: 1.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 975830131 112 IHQQHWDFQENGMIVHILSGKCMEAVVQEN-NKDLYLRPCDGkarQQW 158
Cdd:cd23474   91 ILHKRWNFIQNGAIMNLGTGRCLEVENRGNfGIDLILRSCTG---QRW 135
beta-trefoil_Ricin_RIPs_II_rpt2 cd23444
second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ...
 100-158 1.23e-03

second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating proteins (RIPs); Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. They consist of a catalytic A-chain which has rRNA N-glycosidase activity and a lectin B-chain containing two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The lectin chain facilitates the internalization of the catalytic chain on binding to the cell surface. The two chains are connected by a disulfide bridge. This model corresponds to the second ricin B-type lectin domain. Members of this family includes Ricinus communis ricin, bitter gourd (Momordica charantia) seed lectin (BGSL), snake gourd (Trichosanthes anguina) seed lectin (SGSL), Sambucus ebulus ebulin I, Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf, Abrus precatorius abrin (ABR) and agglutinin-I (AAG), and Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs).


Pssm-ID: 467322 [Multi-domain]  Cd Length: 122  Bit Score: 36.87  E-value: 1.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 975830131 100 VILQNCteEGLAihQQHWDFQENGMIVHILSGKCMEavVQENNKDLY---LRPCDGKARQQW 158
Cdd:cd23444   65 IVVLSC--SGSS--GQRWVFRNDGTILNLYTGLVMD--VKESDPSLKqiiLWPATGGPNQQW 120
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 123-162 1.53e-03

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: 36.96  E-value: 1.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 975830131 123 GMIVHILSGKCMEAV--VQENNKDLYLRPCDGKARQQWRFDQ 162
Cdd:cd00161    3 YRIVNAASGKCLDVAggSTANGAPVQQWTCNGGANQQWTLTP 44
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
115-162 1.76e-03

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 35.82  E-value: 1.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 975830131  115 QHWDFQENG-----MIVHILSGKCMEAV--VQENNKDLYLRPCDGKARQQWRFDQ 162
Cdd:pfam14200   3 QQWRFGGTVgdgyyTIVNVASGKYLDVAggSTANGANVQQWTDNGNDNQQWRIVD 57
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 113-160 1.91e-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: 36.53  E-value: 1.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 975830131 113 HQQHWDFQENG----MIVHILSGKCME--AVVQENNKDLYLRPCDGKARQQWRF 160
Cdd:cd23458   36 SNQQWTLVEIDngyyRIKASHSGKCLDvaGGSTANGANIQQWDCVGGANQQWKL 89
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 38-158 2.40e-03

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


Pssm-ID: 467334 [Multi-domain]  Cd Length: 122  Bit Score: 36.18  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  38 KLHNTGLGLCADCQaEGDILGCPMVLAPCSDSRQQQ-YLQHTSRkeIHFGSPQHLCFAVRQE-----QVILQNCTEEgla 111
Cdd:cd23456    4 QLKSQASGLCLDVS-GGATNGANVVVYDCNNSNSQKwYYDATGR--LHSKANPGKCLDAGGEnsngaNVVLWACNDS--- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 975830131 112 IHQQhWDFQENGMIVHILSGKCMEAVVQENNKdLYLRPCDGKARQQW 158
Cdd:cd23456   78 ANQR-WDFDGNFIRSRNNTNLALDAYGSQGSN-VGLWQFHGGANQQW 122
beta-trefoil_Ricin_AglA cd23425
ricin B-type lectin domain, beta-trefoil fold, found in alpha-galactosidase A (AglA) and ...
 83-160 3.69e-03

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: 35.50  E-value: 3.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 975830131  83 IHFGSPQHLCFAVRQEQVILQNCTEEGLAIHQQHWDFQENGMIvhiLSGKCMEAvvqeNNKDLYLRPCDGKARQQWRF 160
Cdd:cd23425    6 IIFNTASGNCLTADAAEVKFQTCDGSDSQIWQVRKSGILRNLS---NTGQCLTA----DGANVSLSPCDTSTSQNWSY 76
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 37-158 4.17e-03

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: 35.41  E-value: 4.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  37 GKLHNTGLGLCADCQA--EGDILGcpmvLAPCSDSRQQQYLQHTSRKEIHfgsPQHLCFAVRQEQ--VILQNCTE-EGla 111
Cdd:cd23466    7 GEIRNVETNQCLDNMArkENEKVG----IFNCHGMGGNQVFSYTANKEIR---TDDLCLDVSKLNgpVMMLKCHHlKG-- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 975830131 112 ihQQHWDFQENGM-IVHILSGKCMEAVVQENNKDLYLRPCDGKARQQW 158
Cdd:cd23466   78 --NQLWEYDPVKLtLLHVNSNQCLDKATEEDSQVPSIRDCNGSRSQQW 123
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 114-159 4.61e-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: 35.49  E-value: 4.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 975830131 114 QQHWDFQ----ENGMIVHILSGKCMEAVvqeNNKDLYLRPCDGKARQQWR 159
Cdd:cd23415   74 YQRWRVTstsgGGVTLRNVATGRCLDSN---GSGGVYTRPCNGGSYQRWR 120
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 99-161 6.62e-03

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: 35.02  E-value: 6.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 975830131  99 QVILQNCTeeGLAihQQHWDFQENGMIVHiLSGKCMEAVVQ--ENNKDLYLRPCDGKARQQWRFD 161
Cdd:cd23418   29 RLILWDCH--GGA--NQQFTFTSAGELRV-GGDKCLDAAGGgtTNGTPVVIWPCNGGANQKWRFN 88
beta-trefoil_Ricin_ebulin-like_rpt1 cd23483
first ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and ...
 45-159 7.82e-03

first ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and similar proteins; The family includes Sambucus ebulus ebulin I and Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf. Ebulin l is a type II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus. It is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. It is considered a nontoxic type II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type II RIP like ricins. Ebulin l binds an A-chain substrate analogue, pteroic acid. It binds bind galactose and lactose in subdomain 1alpha in a similar manner to that of ricin. In contrast, it binds only the monosaccharide galactose, and not the disaccharide lactose in subdomain 2gamma. SNAV is a non-toxic GalNAc-specific type II RIP which strongly inhibits mammalian protein synthesis but does not affect plant nor bacterial protein synthesis. SNAI is a Neu5Ac(alpha2-6)Gal/GalNAc-specific agglutinin. It also acts as a type II RIP that strongly inhibits mammalian but not plant ribosomes. SNAI' is another NeuAc(alpha2,6)Gal/GalNAc binding type II RIP from elderberry (Sambucus nigra) bark. It is a minor bark protein which closely resembles the major Neu5Ac(alpha2,6)Gal/GalNAc binding type II RIP, SNAI, with respect to its carbohydrate-binding specificity and ribosome-inactivating activity but has a different molecular structure due to a single cysteine residue present in the B chain of SNAI but absent from SNAI'. SNAIf is a fruit-specific SNAI. It functions as a fetuin-binding fruit lectin. Like Ebulin l, SNAV, SNAI, SNAI' and SNAIf consist of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain. It may also be responsible for cell agglutination (lectin activity). The B chain contains two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. This model corresponds to the first ricin B-type lectin domain.


Pssm-ID: 467361 [Multi-domain]  Cd Length: 127  Bit Score: 34.79  E-value: 7.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975830131  45 GLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSrkeihfGSPQHL--CFAV----RQEQVILQNCTEegLAIHQQHWD 118
Cdd:cd23483   11 GLCVDVRNGYDTDGTPVQLWPCGTQRNQQWTFDTD------GTIRSMgkCMTAnglnSGSYVMIYNCST--AAPEATKWV 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 975830131 119 FQENGMIVHILSGKCMEAVVQENNKDLYLRPCDGKARQQWR 159
Cdd:cd23483   83 VSIDGTITNPSSGLVLTAPRAASGTTLLLENNIHAASQGWT 123
 
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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