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Conserved domains on  [gi|45553141|ref|NP_996098|]
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uncharacterized protein Dmel_CG7304 [Drosophila melanogaster]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase( domain architecture ID 11551826)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 113-417 8.12e-134

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: 391.57  E-value: 8.12e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 113 SIIMIFRNEQLVVLLRTLHSLVERTPKYLYIELILVNDHSDTDFWNDKLSliffdnYVHRYIHPKARILHLPEQVGLIKA 192
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLE------EYYKKYLPKVKVLRLKKREGLIRA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 193 RNLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAEQSYTLATPILDNLDEQTLAYQRSIE-RRGMYDWSLTRREVPLSR 271
Cdd:cd02510  75 RIAGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGdARGGFDWSLHFKWLPLPE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 272 A--RRSHLPWPYEVAAVRTSVFAIPAVWFQDISNFDNNLRGFGAAELELSFKVWCTGGRIVQVPCSRVGHLQPKDedyLK 349
Cdd:cd02510 155 EerRRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRK---RK 231

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45553141 350 RYGDLHKMGeQKSRNLKRIIEVWTGDLKSAIYKYQPHLLNISEGDLNEPRKLYKQNECQSFKEFINDI 417
Cdd:cd02510 232 PYTFPGGSG-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENV 298
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 432-549 1.90e-42

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). 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. Pgant8 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 both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. 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: 467339  Cd Length: 128  Bit Score: 148.32  E-value: 1.90e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 432 YASGHVKTLEFPKKCLTIN--AKSQNLFLERCSTNNT----LQNWTLTYVKDLRVAG-NICAEVRPNlRLGYSFCHSLGG 504
Cdd:cd23461   1 FASGVIQSVAFPNLCLDILgrSHGGPPVLAKCSSNKSmpgtFQNFSLTFHRQIKHGTsDDCLEVRGN-NVRLSRCHYQGG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 45553141 505 RQSWHYDSVSNQLMS---NTKCLEFTDELN-IFLAICDAANGKQRWILD 549
Cdd:cd23461  80 NQYWKYDYETHQLINggqNNKCLEADVESLkITLSICDSDNVEQKWKWG 128
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 113-417 8.12e-134

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: 391.57  E-value: 8.12e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 113 SIIMIFRNEQLVVLLRTLHSLVERTPKYLYIELILVNDHSDTDFWNDKLSliffdnYVHRYIHPKARILHLPEQVGLIKA 192
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLE------EYYKKYLPKVKVLRLKKREGLIRA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 193 RNLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAEQSYTLATPILDNLDEQTLAYQRSIE-RRGMYDWSLTRREVPLSR 271
Cdd:cd02510  75 RIAGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGdARGGFDWSLHFKWLPLPE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 272 A--RRSHLPWPYEVAAVRTSVFAIPAVWFQDISNFDNNLRGFGAAELELSFKVWCTGGRIVQVPCSRVGHLQPKDedyLK 349
Cdd:cd02510 155 EerRRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRK---RK 231

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45553141 350 RYGDLHKMGeQKSRNLKRIIEVWTGDLKSAIYKYQPHLLNISEGDLNEPRKLYKQNECQSFKEFINDI 417
Cdd:cd02510 232 PYTFPGGSG-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENV 298
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 432-549 1.90e-42

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). 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. Pgant8 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 both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. 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: 467339  Cd Length: 128  Bit Score: 148.32  E-value: 1.90e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 432 YASGHVKTLEFPKKCLTIN--AKSQNLFLERCSTNNT----LQNWTLTYVKDLRVAG-NICAEVRPNlRLGYSFCHSLGG 504
Cdd:cd23461   1 FASGVIQSVAFPNLCLDILgrSHGGPPVLAKCSSNKSmpgtFQNFSLTFHRQIKHGTsDDCLEVRGN-NVRLSRCHYQGG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 45553141 505 RQSWHYDSVSNQLMS---NTKCLEFTDELN-IFLAICDAANGKQRWILD 549
Cdd:cd23461  80 NQYWKYDYETHQLINggqNNKCLEADVESLkITLSICDSDNVEQKWKWG 128
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
433-546 1.41e-18

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 81.81  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141   433 ASGHVKTLeFPKKCLTINAKSQ---NLFLERCSTNNTLQNWTLTYVKDLR-VAGNICAEVR---PNLRLGYSFCHSLGGR 505
Cdd:pfam00652   1 ATGRIRNR-ASGKCLDVPGGSSaggPVGLYPCHGSNGNQLWTLTGDGTIRsVASDLCLDVGstaDGAKVVLWPCHPGNGN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 45553141   506 QSWHYDSVSNQLMS--NTKCLEFTDELN----IFLAICDAANGKQRW 546
Cdd:pfam00652  80 QRWRYDEDGTQIRNpqSGKCLDVSGAGTsngkVILWTCDSGNPNQQW 126
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 113-265 2.12e-16

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 77.05  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141   113 SIIMIFRNEQLVvLLRTLHSLVERTpkYLYIELILVNDHSdTDFwndklSLIFFDNYVHRYihPKARILHLPEQVGLIKA 192
Cdd:pfam00535   1 SVIIPTYNEEKY-LLETLESLLNQT--YPNFEIIVVDDGS-TDG-----TVEIAEEYAKKD--PRVRVIRLPENRGKAGA 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553141   193 RNLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAEQSYTLATPILDNLDEQTLAYQRSIERRGMYDWSLTRR 265
Cdd:pfam00535  70 RNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGL 142
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
113-374 8.32e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 70.41  E-value: 8.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 113 SIIMIFRNeQLVVLLRTLHSLVERTpkYLYIELILVNDHSDTDFwndklsliffDNYVHRYIHPKARILHLPEQVGLIKA 192
Cdd:COG1216   6 SVVIPTYN-RPELLRRCLESLLAQT--YPPFEVIVVDNGSTDGT----------AELLAALAFPRVRVIRNPENLGFAAA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 193 RNLAASEAKAENLVFVDAQVEFTNGWLSPLldtiaeqsytlatpildnldeqtlayqrsierrgmydwsltrrevplsra 272
Cdd:COG1216  73 RNLGLRAAGGDYLLFLDDDTVVEPDWLERL-------------------------------------------------- 102

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 273 rrshlpwpyevaaVRTSVFAIPAVWFQDISNFDNNLRGFGaAELELSFKVWCTGGRIVQVPCSRVGHLQPKDEDYLKRYG 352
Cdd:COG1216 103 -------------LAAACLLIRREVFEEVGGFDERFFLYG-EDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAY 168

                       250       260
                ....*....|....*....|..
gi 45553141 353 DLHkmgeqksRNLKRIIEVWTG 374
Cdd:COG1216 169 YLG-------RNRLLFLRKHGP 183
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 441-548 2.15e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 46.74  E-value: 2.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141    441 EFPKKCLTINAKSQNLFLERCSTNNTLQNWTLTYVKDLR-VAGNICAEVRPN----LRLgYSfCHSLGGRQSWHYDsvSN 515
Cdd:smart00458   4 GNTGKCLDVNGNKNPVGLFDCHGTGGNQLWKLTSDGAIRiKDTDLCLTANGNtgstVTL-YS-CDGTNDNQYWEVN--KD 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 45553141    516 QLMSN---TKCLEFTD---ELNIFLAICDaANGKQRWIL 548
Cdd:smart00458  80 GTIRNpdsGKCLDVKDgntGTKVILWTCS-GNPNQKWIF 117
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
 107-339 1.88e-05

mycofactocin system glycosyltransferase; Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.


Pssm-ID: 274884 [Multi-domain]  Cd Length: 466  Bit Score: 47.45  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141   107 DEMKPASIIMIFRNEQlVVLLRTLHSLVERTPKYLYIELILVNDHSDTDFwndklsliffDNYVHRYIHPKARILHLPEQ 186
Cdd:TIGR03965  71 PSPPSVTVVVPVRNRP-AGLARLLAALLALDYPRDRLEVIVVDDGSEDPV----------PTRAARGARLPVRVIRHPRR 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141   187 VGLIKARNLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAEQSYTLATPILDNLDEQTLAYQRSIERRGMYDwsLTRRE 266
Cdd:TIGR03965 140 QGPAAARNAGARAARTEFVAFTDSDVVPRPGWLRALLAHFDDPGVALVAPRVVALPAADTRLARYEAVRSSLD--LGPEE 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553141   267 VPL-SRARRSHLPwpyeVAAVRTSVFAIPAVwfqdiSNFDNNLRgfGAAELELSFKVWCTGGRIVQVPCSRVGH 339
Cdd:TIGR03965 218 AVVrPRGPVSYVP----SAALLVRRRALLEV-----GGFDERLE--VGEDVDLCWRLCEAGGRVRYEPAAVVAH 280
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 113-417 8.12e-134

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: 391.57  E-value: 8.12e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 113 SIIMIFRNEQLVVLLRTLHSLVERTPKYLYIELILVNDHSDTDFWNDKLSliffdnYVHRYIHPKARILHLPEQVGLIKA 192
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLE------EYYKKYLPKVKVLRLKKREGLIRA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 193 RNLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAEQSYTLATPILDNLDEQTLAYQRSIE-RRGMYDWSLTRREVPLSR 271
Cdd:cd02510  75 RIAGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGdARGGFDWSLHFKWLPLPE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 272 A--RRSHLPWPYEVAAVRTSVFAIPAVWFQDISNFDNNLRGFGAAELELSFKVWCTGGRIVQVPCSRVGHLQPKDedyLK 349
Cdd:cd02510 155 EerRRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRK---RK 231

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45553141 350 RYGDLHKMGeQKSRNLKRIIEVWTGDLKSAIYKYQPHLLNISEGDLNEPRKLYKQNECQSFKEFINDI 417
Cdd:cd02510 232 PYTFPGGSG-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENV 298
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 432-549 1.90e-42

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). 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. Pgant8 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 both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. 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: 467339  Cd Length: 128  Bit Score: 148.32  E-value: 1.90e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 432 YASGHVKTLEFPKKCLTIN--AKSQNLFLERCSTNNT----LQNWTLTYVKDLRVAG-NICAEVRPNlRLGYSFCHSLGG 504
Cdd:cd23461   1 FASGVIQSVAFPNLCLDILgrSHGGPPVLAKCSSNKSmpgtFQNFSLTFHRQIKHGTsDDCLEVRGN-NVRLSRCHYQGG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 45553141 505 RQSWHYDSVSNQLMS---NTKCLEFTDELN-IFLAICDAANGKQRWILD 549
Cdd:cd23461  80 NQYWKYDYETHQLINggqNNKCLEADVESLkITLSICDSDNVEQKWKWG 128
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
433-546 1.41e-18

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 81.81  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141   433 ASGHVKTLeFPKKCLTINAKSQ---NLFLERCSTNNTLQNWTLTYVKDLR-VAGNICAEVR---PNLRLGYSFCHSLGGR 505
Cdd:pfam00652   1 ATGRIRNR-ASGKCLDVPGGSSaggPVGLYPCHGSNGNQLWTLTGDGTIRsVASDLCLDVGstaDGAKVVLWPCHPGNGN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 45553141   506 QSWHYDSVSNQLMS--NTKCLEFTDELN----IFLAICDAANGKQRW 546
Cdd:pfam00652  80 QRWRYDEDGTQIRNpqSGKCLDVSGAGTsngkVILWTCDSGNPNQQW 126
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 113-265 2.12e-16

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 77.05  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141   113 SIIMIFRNEQLVvLLRTLHSLVERTpkYLYIELILVNDHSdTDFwndklSLIFFDNYVHRYihPKARILHLPEQVGLIKA 192
Cdd:pfam00535   1 SVIIPTYNEEKY-LLETLESLLNQT--YPNFEIIVVDDGS-TDG-----TVEIAEEYAKKD--PRVRVIRLPENRGKAGA 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553141   193 RNLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAEQSYTLATPILDNLDEQTLAYQRSIERRGMYDWSLTRR 265
Cdd:pfam00535  70 RNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGL 142
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 433-547 7.43e-14

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: 68.52  E-value: 7.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 433 ASGHVKTlEFPKKCLTINAKSQN--LFLERCS--TNNTLQNWTLTYVKDLRVAG-NICAEV---RPNLRLGYSFCHSLGG 504
Cdd:cd23439   1 ASGEIRN-VGSGLCIDTKHGGENdeVRLSKCVkdGGGGEQQFELTWHEDIRPKKrKVCFDVsshTPGAPVILYACHGMKG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 45553141 505 RQSWHYDSVSNQL---MSNtKCLE-FTDELNIFLAICDAANGKQRWI 547
Cdd:cd23439  80 NQLWKYRPNTKQLyhpVSG-LCLDaDPGSGKVFMNHCDESSDTQKWT 125
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
113-374 8.32e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 70.41  E-value: 8.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 113 SIIMIFRNeQLVVLLRTLHSLVERTpkYLYIELILVNDHSDTDFwndklsliffDNYVHRYIHPKARILHLPEQVGLIKA 192
Cdd:COG1216   6 SVVIPTYN-RPELLRRCLESLLAQT--YPPFEVIVVDNGSTDGT----------AELLAALAFPRVRVIRNPENLGFAAA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 193 RNLAASEAKAENLVFVDAQVEFTNGWLSPLldtiaeqsytlatpildnldeqtlayqrsierrgmydwsltrrevplsra 272
Cdd:COG1216  73 RNLGLRAAGGDYLLFLDDDTVVEPDWLERL-------------------------------------------------- 102

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 273 rrshlpwpyevaaVRTSVFAIPAVWFQDISNFDNNLRGFGaAELELSFKVWCTGGRIVQVPCSRVGHLQPKDEDYLKRYG 352
Cdd:COG1216 103 -------------LAAACLLIRREVFEEVGGFDERFFLYG-EDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAY 168

                       250       260
                ....*....|....*....|..
gi 45553141 353 DLHkmgeqksRNLKRIIEVWTG 374
Cdd:COG1216 169 YLG-------RNRLLFLRKHGP 183
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 432-549 2.01e-10

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


Pssm-ID: 467340 [Multi-domain]  Cd Length: 126  Bit Score: 58.53  E-value: 2.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 432 YASGHVKTLEfPKKCL----TINAKSQNLFLERCSTNNTLQNWTLTYVKDLRVaGNIC---AEVRPNLRLgYSfCHSLGG 504
Cdd:cd23462   3 LAYGEIRNLA-GKLCLdapgRKKELNKPVGLYPCHGQGGNQYWMLTKDGEIRR-DDLCldyAGGSGDVTL-YP-CHGMKG 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 45553141 505 RQSWHYDSVSNQLMSNT--KCLEFTDEL-NIFLAICDAANGKQRWILD 549
Cdd:cd23462  79 NQFWIYDEETKQIVHGTskKCLELSDDSsKLVMEPCNGSSPRQQWEFE 126
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 113-333 4.43e-10

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 59.72  E-value: 4.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 113 SIIMIFRNEQLVvLLRTLHSLVERTpkYLYIELILVNDHSdTDfwnDKLSLIffDNYVHRYihPKARILHLPEQVGLIKA 192
Cdd:COG0463   5 SVVIPTYNEEEY-LEEALESLLAQT--YPDFEIIVVDDGS-TD---GTAEIL--RELAAKD--PRIRVIRLERNRGKGAA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 193 RNLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAEQSYTLAtpildnldeqtlAYQRSIERRGMYDWSLTRREVPLSRA 272
Cdd:COG0463  74 RNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV------------YGSRLIREGESDLRRLGSRLFNLVRL 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45553141 273 RRSHLPWPYEVAAVRTSVFAipAVWFQDISNFDNNLrgfgaaelelsFKVWCTGGRIVQVP 333
Cdd:COG0463 142 LTNLPDSTSGFRLFRREVLE--ELGFDEGFLEDTEL-----------LRALRHGFRIAEVP 189
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 105-228 7.83e-10

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 60.14  E-value: 7.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 105 DSDEMKPASIIMIFRNEQlVVLLRTLHSLVERTPKYLYIELILVNDHSDTDFWNdklsliffdnYVHRYI--HPKARILH 182
Cdd:COG1215  24 APADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAE----------IARELAaeYPRVRVIE 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 45553141 183 LPEQVGLIKARNLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAE 228
Cdd:COG1215  93 RPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFAD 138
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 114-229 2.06e-09

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 56.36  E-value: 2.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 114 IIMIFRNEQLVvLLRTLHSLVERTpkYLYIELILVNDHSDTDFWNDKLSLIFFDNYVHRYIHPKARilhlpeqvGLIKAR 193
Cdd:cd00761   1 VIIPAYNEEPY-LERCLESLLAQT--YPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQ--------GLAAAR 69

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 45553141 194 NLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAEQ 229
Cdd:cd00761  70 NAGLKAARGEYILFLDADDLLLPDWLERLVAELLAD 105
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 445-548 8.89e-09

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: 53.92  E-value: 8.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 445 KCLTIN----AKSQNLFLERCSTNNTLQNWTLTYVKDLRVAGNICAEV----RPNLRLgySFCHSLGGRQSWHYDSVsNQ 516
Cdd:cd23440  15 LCLVAEdevsQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLLCLDSsetsSDFPRL--MKCHGSGGSQQWRFKKD-NR 91

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 45553141 517 L--MSNTKCLEFTDELNIF---LAICDAANGkQRWIL 548
Cdd:cd23440  92 LynPASGQCLAASKNGTSGyvtMDICSDSPS-QKWVF 127
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 429-550 3.89e-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: 49.23  E-value: 3.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 429 RTDYASGHVKTLEfPKKCL-TINAKS-QNLFLERCSTNNTLQNWTLTYVKDLRvAGNICAEVRP---NLRLgySFCHSLG 503
Cdd:cd23433   1 LDYYSLGEIRNVE-TNLCLdTMGRKAgEKVGLSSCHGQGGNQVFSYTAKGEIR-SDDLCLDASRkggPVKL--EKCHGMG 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 45553141 504 GRQSWHYDSVSNQLM-SNTK-CLEFTDELN---IFLAICDAANGkQRWILDN 550
Cdd:cd23433  77 GNQEWEYDKETKQIRhVNSGlCLTAPNEDDpnePVLRPCDGGPS-QKWELEG 127
beta-trefoil_Ricin_GALNTL6 cd23477
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 499-560 4.95e-07

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: 49.55  E-value: 4.95e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553141 499 CHSLGGRQSWHY--DSVSNQLMSNTkCLEFT-DELNIFLAICDAANGKQRWILDNINLSVMQSAN 560
Cdd:cd23477  85 CHGMKGNQLWSYrkDKTLFHPVSNS-CMDCNpADKKIFMNRCDPLSETQQWIFEHTNMTVLEKFN 148
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 114-340 5.08e-07

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 49.87  E-value: 5.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 114 IIMIFRNeQLVVLLRTLHSLVERTPKYLyiELILV-NDHSDTDFWndklslIFFDNYvhryihPKARILHLPEQVGLIKA 192
Cdd:cd04186   1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVdNASTDGSVE------LLRELF------PEVRLIRNGENLGFGAG 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 193 RNLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAEQSytlatpildnldeqtlayqrsierrgmydwsltrrevplsra 272
Cdd:cd04186  66 NNQGIREAKGDYVLLLNPDTVVEPGALLELLDAAEQDP------------------------------------------ 103

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45553141 273 rrshlpwpyEVAAVRTSV----FAIPAVWFQDISNFDNNLRGFGaAELELSFKVWCTGGRIVQVPCSRVGHL 340
Cdd:cd04186 104 ---------DVGIVGPKVsgafLLVRREVFEEVGGFDEDFFLYY-EDVDLCLRARLAGYRVLYVPQAVIYHH 165
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 441-548 2.15e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 46.74  E-value: 2.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141    441 EFPKKCLTINAKSQNLFLERCSTNNTLQNWTLTYVKDLR-VAGNICAEVRPN----LRLgYSfCHSLGGRQSWHYDsvSN 515
Cdd:smart00458   4 GNTGKCLDVNGNKNPVGLFDCHGTGGNQLWKLTSDGAIRiKDTDLCLTANGNtgstVTL-YS-CDGTNDNQYWEVN--KD 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 45553141    516 QLMSN---TKCLEFTD---ELNIFLAICDaANGKQRWIL 548
Cdd:smart00458  80 GTIRNpdsGKCLDVKDgntGTKVILWTCS-GNPNQKWIF 117
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 435-548 2.22e-06

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: 46.67  E-value: 2.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 435 GHVKTLEFPKkCLTINAKSQ---NLFLERCSTNNTLQNWTLTYVKDLRvAGNICAEVRPNLRLGYSFCHSLGGRQSWHYD 511
Cdd:cd23460   3 GQIKHTESGL-CLDWAGESNgdkTVALKPCHGGGGNQFWMYTGDGQIR-QDHLCLTADEGNKVTLRECADQLPSQEWSYD 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 45553141 512 SVSNQLM--SNTKCLEFTDELNIF-LAICDAANGKQRWIL 548
Cdd:cd23460  81 EKTGTIRhrSTGLCLTLDANNDVViLKECDSNSLWQKWIF 120
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 113-230 1.69e-05

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 46.46  E-value: 1.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 113 SIIMIFRNEQLVvLLRTLHSLVERTPKYLYIELILVNDHSDTDFWNdklsliffdnYVHRYI--HPKARILHLPEQVgLI 190
Cdd:cd02525   3 SIIIPVRNEEKY-IEELLESLLNQSYPKDLIEIIVVDGGSTDGTRE----------IVQEYAakDPRIRLIDNPKRI-QS 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 45553141 191 KARNLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAEQS 230
Cdd:cd02525  71 AGLNIGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTG 110
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
 107-339 1.88e-05

mycofactocin system glycosyltransferase; Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.


Pssm-ID: 274884 [Multi-domain]  Cd Length: 466  Bit Score: 47.45  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141   107 DEMKPASIIMIFRNEQlVVLLRTLHSLVERTPKYLYIELILVNDHSDTDFwndklsliffDNYVHRYIHPKARILHLPEQ 186
Cdd:TIGR03965  71 PSPPSVTVVVPVRNRP-AGLARLLAALLALDYPRDRLEVIVVDDGSEDPV----------PTRAARGARLPVRVIRHPRR 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141   187 VGLIKARNLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAEQSYTLATPILDNLDEQTLAYQRSIERRGMYDwsLTRRE 266
Cdd:TIGR03965 140 QGPAAARNAGARAARTEFVAFTDSDVVPRPGWLRALLAHFDDPGVALVAPRVVALPAADTRLARYEAVRSSLD--LGPEE 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553141   267 VPL-SRARRSHLPwpyeVAAVRTSVFAIPAVwfqdiSNFDNNLRgfGAAELELSFKVWCTGGRIVQVPCSRVGH 339
Cdd:TIGR03965 218 AVVrPRGPVSYVP----SAALLVRRRALLEV-----GGFDERLE--VGEDVDLCWRLCEAGGRVRYEPAAVVAH 280
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 114-233 2.14e-05

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 46.13  E-value: 2.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 114 IIMIFRNEQLVvLLRTLHSLVERTPKYLYIELILVNDHSdTDFWNDKLSLIFFDNYVH--------RYIHPKARILHlpe 185
Cdd:cd04192   1 VVIAARNEAEN-LPRLLQSLSALDYPKEKFEVILVDDHS-TDGTVQILEFAAAKPNFQlkilnnsrVSISGKKNALT--- 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 45553141 186 qvglikarnLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAEQSYTL 233
Cdd:cd04192  76 ---------TAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGL 114
beta-trefoil_Ricin_GALNT5 cd23436
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 445-546 8.41e-05

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


Pssm-ID: 467314  Cd Length: 132  Bit Score: 42.47  E-value: 8.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 445 KCLTINakSQNLFLERCSTNNTLQNWTLTYVKDLRvAGNIC-AEVRPNLRLGYSFCHSLGGRQSWHYDSVSNQ--LM--- 518
Cdd:cd23436  16 KCIAIE--NTTLTLQDCDLNNKSQHFNYTWLRLIR-QGELClAPVEAEGALTLHPCDNTNNGLRWLHKSLIAFpeLMdhi 92

                        90       100       110
                ....*....|....*....|....*....|....
gi 45553141 519 -----SNTKCLEFTDELNI-FLAICDAANGKQRW 546
Cdd:cd23436  93 mlehqSQPTCLEADPSQKIlRLNACDSFKRYQKW 126
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 468-547 1.64e-04

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: 41.51  E-value: 1.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 468 QNWTLTYVKDLRVaGNICAEVRPN-LRLGYSFCHsLGGRQSWHYDSVSNQLM-SNT-KCLEFTDELN-IFLAICDAANGK 543
Cdd:cd23437  40 QLFRLNEAGQLAV-GEQCLTASGSgGKVKLRKCN-LGETGKWEYDEATGQIRhKGTgKCLDLNEGTNkLILQPCDSSSPS 117


                ....
gi 45553141 544 QRWI 547
Cdd:cd23437 118 QKWE 121
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 114-210 3.76e-04

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 41.44  E-value: 3.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 114 IIMIFRNEQlVVLLRTLHSLVERTpkYLYIELILVNDHSDTDFwNDKLSLIFfdnyvhrYIHPKARILHLPEQVGLiKAR 193
Cdd:cd06423   1 IIVPAYNEE-AVIERTIESLLALD--YPKLEVIVVDDGSTDDT-LEILEELA-------ALYIRRVLVVRDKENGG-KAG 68

                        90
                ....*....|....*....
gi 45553141 194 NLAA--SEAKAENLVFVDA 210
Cdd:cd06423  69 ALNAglRHAKGDIVVVLDA 87
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 493-552 5.15e-04

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: 39.97  E-value: 5.15e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45553141 493 RLGYSFCHSLGGRQSWHYdSVSNQLMSNTKCLEFTDELN-IFLAICDaANGKQRWILDNIN 552
Cdd:cd23437  27 PVGLYPCHGMGGNQLFRL-NEAGQLAVGEQCLTASGSGGkVKLRKCN-LGETGKWEYDEAT 85
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 433-547 6.16e-04

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


Pssm-ID: 467319 [Multi-domain]  Cd Length: 122  Bit Score: 39.69  E-value: 6.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 433 ASGHVKTLEfpkKCL----TINAKSQNLFLERCSTNNTLQNWTLTYVKDLRVAGNiCAEVRP---NLRLGYSFChSLGGR 505
Cdd:cd23441   4 AYGQIKQGN---LCLdsdeQLFQGPALLILAPCSNSSDSQEWSFTKDGQLQTQGL-CLTVDSsskDLPVVLETC-SDDPK 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 45553141 506 QSWHYdsVSNQLM-SNTK-CLEFTDELNIFLAICDAANGKQRWI 547
Cdd:cd23441  79 QKWTR--TGRQLVhSESGlCLDSRKKKGLVVSPCRSGAPSQKWD 120
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 499-560 7.61e-04

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


Pssm-ID: 467354  Cd Length: 150  Bit Score: 40.33  E-value: 7.61e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553141 499 CHSLGGRQSWHY--DSVSNQLMSNTkCLEF-TDELNIFLAICDAANGKQRWILDNINLSVMQSAN 560
Cdd:cd23476  85 CHGMKGNQLWRYrkDKTLYHPVSNS-CMDCsESDHRIFMNTCNPSSPTQQWLFEHTNSTVLEKFN 148
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 429-550 1.16e-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: 39.26  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553141 429 RTDYASGHVKTLEfPKKCLTINAKSQN--LFLERCSTNNTLQNWTLTYVKDLRvAGNICAEVR----PNLRLGysfCHSL 502
Cdd:cd23466   1 RHYFSLGEIRNVE-TNQCLDNMARKENekVGIFNCHGMGGNQVFSYTANKEIR-TDDLCLDVSklngPVMMLK---CHHL 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 45553141 503 GGRQSWHYDSVSNQLM--SNTKCLE-FTDELNIFLAICDAANGK-QRWILDN 550
Cdd:cd23466  76 KGNQLWEYDPVKLTLLhvNSNQCLDkATEEDSQVPSIRDCNGSRsQQWLLRN 127
beta-trefoil_Ricin_hemolysin cd23423
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ...
 481-546 2.46e-03

ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar proteins; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cytolysis by forming heptameric pores in target host membranes. After binding to target membranes, the protein assembles into a heptameric pre-pore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation. Hemolysin may be called "cytolysin" or "cytolytic toxin", according to a specific action for certain cells. For example, this subfamily includes Vibrio vulnificus cytolysin that attack blood cell membranes and cause cell rupture, thereby liberating hemoglobins. Members of this subfamily contain 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 harbor a putative sugar-binding pocket.


Pssm-ID: 467301 [Multi-domain]  Cd Length: 119  Bit Score: 38.13  E-value: 2.46e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45553141 481 AGNICAEVRPNLRLGYSFCHSLGGRQSWHYDSvSNQLMS---NTKCLEFTDELNIFLAICDAANGkQRW 546
Cdd:cd23423  12 FNNRCLTVDNNGRVTLESCDSGDRNQSWILDS-EGRYRSrvaPDLCLDADDDGLLTLEQCSLSLT-QKW 78
 
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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