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Conserved domains on  [gi|71052141|gb|AAH30625|]
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GALNTL2 protein [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 ...
 32-153 4.57e-55

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: 170.70  E-value: 4.57e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  32 RPSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpQHLCFAVRQEQVILQNCTEEgla 111
Cdd:cd23442   1 APYFSGQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGS-LQLCLDVRQEQVVLQNCTKE--- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 71052141 112 IHQQHWDFQENGMIVHILSGKCMEAVVQENNKDLYLRPCDEK 153
Cdd:cd23442  77 KTSQKWDFQETGRIVHILSGKCIEAVESENSKLLFLSPCNGQ 118
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 1-23 2.08e-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: 2.08e-05
                        10        20
                ....*....|....*....|...
gi 71052141   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 ...
 32-153 4.57e-55

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: 170.70  E-value: 4.57e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  32 RPSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpQHLCFAVRQEQVILQNCTEEgla 111
Cdd:cd23442   1 APYFSGQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGS-LQLCLDVRQEQVVLQNCTKE--- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 71052141 112 IHQQHWDFQENGMIVHILSGKCMEAVVQENNKDLYLRPCDEK 153
Cdd:cd23442  77 KTSQKWDFQETGRIVHILSGKCIEAVESENSKLLFLSPCNGQ 118
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
35-152 3.90e-20

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 81.42  E-value: 3.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141    35 FSGKLHNTGLGLCADCQAeGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQhLCFAVRQE----QVILQNCTEEGl 110
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPG-GSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVASD-LCLDVGSTadgaKVVLWPCHPGN- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 71052141   111 aiHQQHWDFQENG-MIVHILSGKCMEAVVQEN-NKDLYLRPCDE 152
Cdd:pfam00652  78 --GNQRWRYDEDGtQIRNPQSGKCLDVSGAGTsNGKVILWTCDS 119
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 43-154 8.93e-07

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 45.97  E-value: 8.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141     43 GLGLCADCQAEGDilgcPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQhLCFAVRQ---EQVILQNCTEEGLAihqQHWDF 119
Cdd:smart00458   5 NTGKCLDVNGNKN----PVGLFDCHGTGGNQLWKLTSDGAIRIKDTD-LCLTANGntgSTVTLYSCDGTNDN---QYWEV 76

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 71052141    120 QENGMIVHILSGKCMEAVVQENNKDLYLRPCDEKP 154
Cdd:smart00458  77 NKDGTIRNPDSGKCLDVKDGNTGTKVILWTCSGNP 111
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 1-23 2.08e-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: 2.08e-05
                        10        20
                ....*....|....*....|...
gi 71052141   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 ...
 32-153 4.57e-55

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: 170.70  E-value: 4.57e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  32 RPSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpQHLCFAVRQEQVILQNCTEEgla 111
Cdd:cd23442   1 APYFSGQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGS-LQLCLDVRQEQVVLQNCTKE--- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 71052141 112 IHQQHWDFQENGMIVHILSGKCMEAVVQENNKDLYLRPCDEK 153
Cdd:cd23442  77 KTSQKWDFQETGRIVHILSGKCIEAVESENSKLLFLSPCNGQ 118
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
35-152 3.90e-20

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 81.42  E-value: 3.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141    35 FSGKLHNTGLGLCADCQAeGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQhLCFAVRQE----QVILQNCTEEGl 110
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPG-GSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVASD-LCLDVGSTadgaKVVLWPCHPGN- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 71052141   111 aiHQQHWDFQENG-MIVHILSGKCMEAVVQEN-NKDLYLRPCDE 152
Cdd:pfam00652  78 --GNQRWRYDEDGtQIRNPQSGKCLDVSGAGTsNGKVILWTCDS 119
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 33-151 3.37e-15

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: 68.90  E-value: 3.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  33 PSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQHLCFAVRQEQ-VILQNCTEEGLA 111
Cdd:cd23435   1 PGYYGALRNKGSELCLDVNNPNGQGGKPVIMYGCHGLGGNQYFEYTSKGEIRHNIGKELCLHASGSDeVILQHCTSKGKD 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 71052141 112 I-HQQHWDFQENGMIVHILSGKCMEAvvqeNNKDLYLRPCD 151
Cdd:cd23435  81 VpPEQKWLFTQDGTIRNPASGLCLHA----SGYKVLLRTCN 117
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 36-152 4.29e-11

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: 57.76  E-value: 4.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  36 SGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGspqHLC--FAVRQEQVILQNCteeglaiH 113
Cdd:cd23462   5 YGEIRNLAGKLCLDAPGRKKELNKPVGLYPCHGQGGNQYWMLTKDGEIRRD---DLCldYAGGSGDVTLYPC-------H 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 71052141 114 Q----QHWDF-QENGMIVHILSGKCMEavVQENNKDLYLRPCDE 152
Cdd:cd23462  75 GmkgnQFWIYdEETKQIVHGTSKKCLE--LSDDSSKLVMEPCNG 116
beta-trefoil_Ricin_GALNT4 cd23469
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 33-151 6.42e-11

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: 57.60  E-value: 6.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  33 PSFSGKLHNTGL-GLCADCQA-EGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQHLCFAVRQEQ--VILQNCTEE 108
Cdd:cd23469   1 PGWHGAVRSMGIsSECLDYNSpEHNPTGAHLSLFGCHGQGGNQFFEYTSNKEIRFNSVTELCAEVPDQKnyIGMKHCPKD 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71052141 109 GLAIHQQ-HWDFQENGMIVHILSGKCMEAV-VQENNKDLYLRPCD 151
Cdd:cd23469  81 GSPVPANiIWHFKEDGTIYHPHSGMCISAYrTPEGRADVQMRTCD 125
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 33-150 1.04e-10

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: 57.11  E-value: 1.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  33 PSFSGKLHNTGL-GLCADCQA--EGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQ-HLCFAVR--QEQVILQNCT 106
Cdd:cd23471   1 PGFFGMLKNKGMtNYCFDYNPpdEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTRQpEGCAAVDagTDFLTMHLCR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 71052141 107 EEGLAI-HQQHWDFQENGMIVHILSGKCMEAVVQENNKDL--YLRPC 150
Cdd:cd23471  81 ENRQAVpENQKFIFREDGSLFHVQTQKCVQAVRNESSGSPapVLRPC 127
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 31-156 2.87e-08

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: 50.73  E-value: 2.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  31 PRPSFsGKLHNTGLGLCADcqAEGDILGCPMVLAPCSDSR------QQQYLQHTSRKEIHFGSPQH---LCF-AVRQEQ- 99
Cdd:cd23476   3 PAAAW-GEIRNVGTGLCAD--TKHGALGSPLRLEGCVKGRgeaawnNGQVFTFGWREDIRPGDPQHtkkFCFdAISHNSp 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71052141 100 VILQNCteEGLAiHQQHWDFQENGMIVHILSGKCMEAvvQENNKDLYLRPCDekPAS 156
Cdd:cd23476  80 VTLYDC--HGMK-GNQLWRYRKDKTLYHPVSNSCMDC--SESDHRIFMNTCN--PSS 129
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 36-152 5.75e-08

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: 49.26  E-value: 5.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  36 SGKLHNTGLGLCADCQAEGdiLGCPMVLAPCSDSRQQ--QYLQHTSRKEIHFGSPQHlCF----AVRQEQVILQNCteeg 109
Cdd:cd23439   2 SGEIRNVGSGLCIDTKHGG--ENDEVRLSKCVKDGGGgeQQFELTWHEDIRPKKRKV-CFdvssHTPGAPVILYAC---- 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 71052141 110 laiHQ----QHWDFQEN-GMIVHILSGKCMEAVvqENNKDLYLRPCDE 152
Cdd:cd23439  75 ---HGmkgnQLWKYRPNtKQLYHPVSGLCLDAD--PGSGKVFMNHCDE 117
beta-trefoil_Ricin_GALNT3 cd23468
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 33-146 5.84e-08

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: 49.42  E-value: 5.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  33 PSFSGKLHNTGLGLCADCqAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQHLCFAVRQEQVILQNCTEEG--- 109
Cdd:cd23468   2 PLIFGAIKNVGKELCLDV-GENNHGGKPLIMYNCHGLGGNQYFEYSTHHEIRHNIQKELCLHGSQGSVQLKECTYKGrnt 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 71052141 110 LAIHQQHWDFQENGMIVHILSGKCMEA------VVQENNKDLY 146
Cdd:cd23468  81 AVLPEEKWELQKDQLLYNPALNMCLSAngenpsLVPCNPSDPF 123
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 37-153 1.90e-07

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: 47.82  E-value: 1.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  37 GKLHNTGLGLCADCQAEGDILGCPmVLAPCSDSRQQQYLQHTSRKEIHFGspqHLCFAVRQ-EQVILQNCTEEGLAihqQ 115
Cdd:cd23460   3 GQIKHTESGLCLDWAGESNGDKTV-ALKPCHGGGGNQFWMYTGDGQIRQD---HLCLTADEgNKVTLRECADQLPS---Q 75

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 71052141 116 HWDFQENGM-IVHILSGKCMEavVQENNKDLYLRPCDEK 153
Cdd:cd23460  76 EWSYDEKTGtIRHRSTGLCLT--LDANNDVVILKECDSN 112
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 37-160 2.51e-07

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: 47.76  E-value: 2.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  37 GKLHNTGLGLCAdcQAEGDIL--GCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpqHLCFAV---RQEQVILQNCTEEGLA 111
Cdd:cd23440   6 GQLKHAGSGLCL--VAEDEVSqkGSLLVLRPCSRNDKKQLWYYTEDGELRLAN--LLCLDSsetSSDFPRLMKCHGSGGS 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71052141 112 ihqQHWDFQENGMIVHILSGKCMEAVVQENNKDLYLRPCDEKPASSGVL 160
Cdd:cd23440  82 ---QQWRFKKDNRLYNPASGQCLAASKNGTSGYVTMDICSDSPSQKWVF 127
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 35-152 3.89e-07

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: 46.90  E-value: 3.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  35 FSGKLHNTGLGLCADCQAEGDilGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpqhLCFAVR--QEQVILQNCTEEGlai 112
Cdd:cd23437   4 AWGEIRNLGTGLCLDTMGHQN--GGPVGLYPCHGMGGNQLFRLNEAGQLAVGE---QCLTASgsGGKVKLRKCNLGE--- 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 71052141 113 hQQHWDFQE-NGMIVHILSGKCMEavVQENNKDLYLRPCDE 152
Cdd:cd23437  76 -TGKWEYDEaTGQIRHKGTGKCLD--LNEGTNKLILQPCDS 113
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 46-156 8.82e-07

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: 46.24  E-value: 8.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  46 LCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpqhLCFAVRQEQ----VILQNCTEEGlaihQQHWDFQE 121
Cdd:cd23441  13 LCLDSDEQLFQGPALLILAPCSNSSDSQEWSFTKDGQLQTQG---LCLTVDSSSkdlpVVLETCSDDP----KQKWTRTG 85

                        90       100       110
                ....*....|....*....|....*....|....*
gi 71052141 122 NGmIVHILSGKCMEAVVQennKDLYLRPCDEKPAS 156
Cdd:cd23441  86 RQ-LVHSESGLCLDSRKK---KGLVVSPCRSGAPS 116
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 43-154 8.93e-07

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 45.97  E-value: 8.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141     43 GLGLCADCQAEGDilgcPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQhLCFAVRQ---EQVILQNCTEEGLAihqQHWDF 119
Cdd:smart00458   5 NTGKCLDVNGNKN----PVGLFDCHGTGGNQLWKLTSDGAIRIKDTD-LCLTANGntgSTVTLYSCDGTNDN---QYWEV 76

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 71052141    120 QENGMIVHILSGKCMEAVVQENNKDLYLRPCDEKP 154
Cdd:smart00458  77 NKDGTIRNPDSGKCLDVKDGNTGTKVILWTCSGNP 111
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 99-154 1.04e-06

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: 46.16  E-value: 1.04e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71052141  99 QVILQNCTEEGLAihQQHWDFQENGMIVHILSGKCMEAVVQENNKDLYLRPCDEKP 154
Cdd:cd23459  71 KVILITCHGLEKF--NQKWKHTKGGQIVHLASGKCLDAEGLKSGDDVTLAKCDGSL 124
beta-trefoil_Ricin_GALNT6 cd23470
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 33-151 2.11e-06

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: 45.24  E-value: 2.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  33 PSFSGKLHNTGLGLCADCqAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSPQHLCFAVRQEQVILQNCTEEGLAI 112
Cdd:cd23470   1 PTFYGAIKNEGTNQCLDV-GENNRGGKPLIMYSCHGMGGNQYFEYTTHKELRHNIAKQLCLRVSKGPVQLGECHYKGKNS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 71052141 113 H---QQHWDFQENGMIVHILSGKCMEAvvqeNNKDLYLRPCD 151
Cdd:cd23470  80 QvppDEEWELTQDHLIRNSGSNMCLTA----RGKHPAMAPCN 117
beta-trefoil_Ricin_GALNTL6 cd23477
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 30-156 8.11e-06

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: 43.77  E-value: 8.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  30 EPRPSFSGKLHNTGLGLCADCQ--AEGDILGCPMVLAPCSDS--RQQQYLQHTSRKEIHFGSPQH---LCF-AVRQEQ-V 100
Cdd:cd23477   1 EPPPAAWGEIRNVAANLCVDSKhgATGTELRLDICVKDGSERtwSHEQLFTFGWREDIRPGEPLHtrkFCFdAISHNSpV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71052141 101 ILQNCteEGLAiHQQHWDFQENGMIVHILSGKCMEAvvQENNKDLYLRPCDEKPAS 156
Cdd:cd23477  81 TLYDC--HGMK-GNQLWSYRKDKTLFHPVSNSCMDC--NPADKKIFMNRCDPLSET 131
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 1-23 2.08e-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: 2.08e-05
                        10        20
                ....*....|....*....|...
gi 71052141   1 MERLQLQRRLGCRTFHWFLANVY 23
Cdd:cd02510 277 SERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 36-155 3.40e-05

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: 41.97  E-value: 3.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  36 SGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQ-YLQHTSRKEIHFGSPQH-LCFAVRQ------EQVILQNCTe 107
Cdd:cd00161   2 TYRIVNAASGKCLDVAGGSTANGAPVQQWTCNGGANQQwTLTPVGDGYYTIRNVASgKCLDVAGgstangANVQQWTCN- 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 71052141 108 eGLAihQQHWDFQENG----MIVHILSGKCMEAV--VQENNKDLYLRPCDEKPA 155
Cdd:cd00161  81 -GGD--NQQWRLEPVGdgyyRIVNKHSGKCLDVSggSTANGANVQQWTCNGGAN 131
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 37-154 2.83e-04

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: 39.22  E-value: 2.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  37 GKLHNTGLGLCADC--QAEGDILGcpmvLAPCSDSRQQQYLQHTSRKEIHFGSpqhLCFAVRQ--EQVILQNCTEEGLai 112
Cdd:cd23433   7 GEIRNVETNLCLDTmgRKAGEKVG----LSSCHGQGGNQVFSYTAKGEIRSDD---LCLDASRkgGPVKLEKCHGMGG-- 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 71052141 113 hQQHWDF-QENGMIVHILSGKCMEAVVQENNKDLYLRPCDEKP 154
Cdd:cd23433  78 -NQEWEYdKETKQIRHVNSGLCLTAPNEDDPNEPVLRPCDGGP 119
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 36-137 4.16e-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: 35.79  E-value: 4.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71052141  36 SGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSRQQQYLQHTSRKEIHFGSpqhLCFAV------RQEQVILQNCTEEG 109
Cdd:cd23418   5 GGQIRGYGSGRCLDVPGGSTTNGTRLILWDCHGGANQQFTFTSAGELRVGGD---KCLDAagggttNGTPVVIWPCNGGA 81

                        90       100
                ....*....|....*....|....*...
gi 71052141 110 LaihqQHWDFQENGMIVHILSGKCMEAV 137
Cdd:cd23418  82 N----QKWRFNSDGTIRNVNSGLCLDVA 105
 
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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