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Conserved domains on  [gi|1788921534|ref|XP_031823762|]
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polypeptide N-acetylgalactosaminyltransferase 17 isoform X2 [Sarcophilus harrisii]

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 ...
 80-379 1.42e-165

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: 470.53  E-value: 1.42e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  80 SIIFIFVNEALSVILRSVHSAVNHTPAHLLKEIILVDDNSDEEELKAPLEEYvHKRYPGLVKVVRNQKREGLIRARIEGW 159
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEY-YKKYLPKVKVLRLKKREGLIRARIAGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 160 KVATGQITGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENSA-HGYSWELWCMYISPPKDWWDA 238
Cdd:cd02510    80 RAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDArGGFDWSLHFKWLPLPEEERRR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 239 GDPSLPIRTPAMIGCSFVVNRKFFGEIGLLDPGMDVYGGENIELGIKVWLCGGSMEVLPCSRVAHIER-KKKPYNNNIGF 317
Cdd:cd02510   160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1788921534 318 YT-KRNALRVAEVWMDDYKSHVYIAWNLPLenpGIDIGDVSERRALRKRLKCKNFQWYLDHVY 379
Cdd:cd02510   240 GTvLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT17 cd23474
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 382-521 3.70e-102

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


:

Pssm-ID: 467352  Cd Length: 142  Bit Score: 302.97  E-value: 3.70e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 382 MRRYNNTIAYGELRNNKAKDVCLDQGPQENHTAILYPCHGWGPQLTRYTREGFLHLGALGTTTLLPDTRCLVDNGKSRFP 461
Cdd:cd23474     1 MRRYNNTVAYGELRNNKAKDVCLDQGPPENHTAILYPCHGWGPQLARYTKEGYLHLGALGTTTLLPDTRCLVDNKKSRFP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1788921534 462 QLLDCDKVKSSLHKRWNFIQNGAIMNKGTGRCLEVESRPS--IDLILRSCTGQRWTIKNFIK 521
Cdd:cd23474    81 QLLDCDKVKSILHKRWNFIQNGAIMNLGTGRCLEVENRGNfgIDLILRSCTGQRWTIKNFIK 142
 
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 ...
 80-379 1.42e-165

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: 470.53  E-value: 1.42e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  80 SIIFIFVNEALSVILRSVHSAVNHTPAHLLKEIILVDDNSDEEELKAPLEEYvHKRYPGLVKVVRNQKREGLIRARIEGW 159
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEY-YKKYLPKVKVLRLKKREGLIRARIAGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 160 KVATGQITGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENSA-HGYSWELWCMYISPPKDWWDA 238
Cdd:cd02510    80 RAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDArGGFDWSLHFKWLPLPEEERRR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 239 GDPSLPIRTPAMIGCSFVVNRKFFGEIGLLDPGMDVYGGENIELGIKVWLCGGSMEVLPCSRVAHIER-KKKPYNNNIGF 317
Cdd:cd02510   160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1788921534 318 YT-KRNALRVAEVWMDDYKSHVYIAWNLPLenpGIDIGDVSERRALRKRLKCKNFQWYLDHVY 379
Cdd:cd02510   240 GTvLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT17 cd23474
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 382-521 3.70e-102

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


Pssm-ID: 467352  Cd Length: 142  Bit Score: 302.97  E-value: 3.70e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 382 MRRYNNTIAYGELRNNKAKDVCLDQGPQENHTAILYPCHGWGPQLTRYTREGFLHLGALGTTTLLPDTRCLVDNGKSRFP 461
Cdd:cd23474     1 MRRYNNTVAYGELRNNKAKDVCLDQGPPENHTAILYPCHGWGPQLARYTKEGYLHLGALGTTTLLPDTRCLVDNKKSRFP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1788921534 462 QLLDCDKVKSSLHKRWNFIQNGAIMNKGTGRCLEVESRPS--IDLILRSCTGQRWTIKNFIK 521
Cdd:cd23474    81 QLLDCDKVKSILHKRWNFIQNGAIMNLGTGRCLEVENRGNfgIDLILRSCTGQRWTIKNFIK 142
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 80-264 1.51e-26

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: 105.55  E-value: 1.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  80 SIIFIFVNEAlSVILRSVHSAVNHTpaHLLKEIILVDDNSdEEELKAPLEEYVHKryPGLVKVVRNQKREGLIRARIEGW 159
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGS-TDGTVEIAEEYAKK--DPRVRVIRLPENRGKAGARNAGL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 160 KVATGQITGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENsahgyswelwcmyISPPKDWWDAG 239
Cdd:pfam00535  75 RAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASR-------------ITLSRLPFFLG 141

                         170       180
                  ....*....|....*....|....*
gi 1788921534 240 DPSLPIRTPAMIGCSFVVNRKFFGE 264
Cdd:pfam00535 142 LRLLGLNLPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
390-514 2.29e-18

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 81.04  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 390 AYGELRNnKAKDVCLD--QGPQENHTAILYPCHG-WGPQLTRYTREGFLHLGAlgtttllpDTRCL--VDNGKSRFPQLL 464
Cdd:pfam00652   1 ATGRIRN-RASGKCLDvpGGSSAGGPVGLYPCHGsNGNQLWTLTGDGTIRSVA--------SDLCLdvGSTADGAKVVLW 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1788921534 465 DCDKVKSSlhKRWNFIQNGA-IMNKGTGRCLEV--ESRPSIDLILRSC----TGQRW 514
Cdd:pfam00652  72 PCHPGNGN--QRWRYDEDGTqIRNPQSGKCLDVsgAGTSNGKVILWTCdsgnPNQQW 126
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
77-332 3.71e-13

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 68.48  E-value: 3.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  77 PQISIIFIFVNEAlSVILRSVHSAVNHTPAHLlkEIILVDDNSDEEELkapleEYVHKRYPGLVKVVRNQKREGLIRARI 156
Cdd:COG1216     3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTA-----ELLAALAFPRVRVIRNPENLGFAAARN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 157 EGWKVATGQITGFFDAHVEFTAGWAEPVLsriqenrkrvilpsidnikqdnfevqryensahgyswELWCMYISppkdww 236
Cdd:COG1216    75 LGLRAAGGDYLLFLDDDTVVEPDWLERLL-------------------------------------AAACLLIR------ 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 237 dagdpslpirtpamigcsfvvnRKFFGEIGLLDPGMDVYGGEnIELGIKVWLCGGSMEVLPCSRVAHIERKKKPYNNNIg 316
Cdd:COG1216   112 ----------------------REVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRA- 167

                         250
                  ....*....|....*.
gi 1788921534 317 FYTKRNALRVAEVWMD 332
Cdd:COG1216   168 YYLGRNRLLFLRKHGP 183
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 397-517 1.15e-09

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 55.98  E-value: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  397 NKAKDVCLDQgPQENHTAILYPCHGWGP-QLTRYTREGflhlgalgTTTLLPDTRCL-VDNGKSRFPQLLDCDKVKSSLh 474
Cdd:smart00458   3 SGNTGKCLDV-NGNKNPVGLFDCHGTGGnQLWKLTSDG--------AIRIKDTDLCLtANGNTGSTVTLYSCDGTNDNQ- 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1788921534  475 kRWNFIQNGAIMNKGTGRCLEV-ESRPSIDLILRSCTG---QRWTIK 517
Cdd:smart00458  73 -YWEVNKDGTIRNPDSGKCLDVkDGNTGTKVILWTCSGnpnQKWIFE 118
 
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 ...
 80-379 1.42e-165

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: 470.53  E-value: 1.42e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  80 SIIFIFVNEALSVILRSVHSAVNHTPAHLLKEIILVDDNSDEEELKAPLEEYvHKRYPGLVKVVRNQKREGLIRARIEGW 159
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEY-YKKYLPKVKVLRLKKREGLIRARIAGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 160 KVATGQITGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENSA-HGYSWELWCMYISPPKDWWDA 238
Cdd:cd02510    80 RAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDArGGFDWSLHFKWLPLPEEERRR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 239 GDPSLPIRTPAMIGCSFVVNRKFFGEIGLLDPGMDVYGGENIELGIKVWLCGGSMEVLPCSRVAHIER-KKKPYNNNIGF 317
Cdd:cd02510   160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1788921534 318 YT-KRNALRVAEVWMDDYKSHVYIAWNLPLenpGIDIGDVSERRALRKRLKCKNFQWYLDHVY 379
Cdd:cd02510   240 GTvLRNYKRVAEVWMDEYKEYFYKARPELR---NIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT17 cd23474
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 382-521 3.70e-102

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


Pssm-ID: 467352  Cd Length: 142  Bit Score: 302.97  E-value: 3.70e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 382 MRRYNNTIAYGELRNNKAKDVCLDQGPQENHTAILYPCHGWGPQLTRYTREGFLHLGALGTTTLLPDTRCLVDNGKSRFP 461
Cdd:cd23474     1 MRRYNNTVAYGELRNNKAKDVCLDQGPPENHTAILYPCHGWGPQLARYTKEGYLHLGALGTTTLLPDTRCLVDNKKSRFP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1788921534 462 QLLDCDKVKSSLHKRWNFIQNGAIMNKGTGRCLEVESRPS--IDLILRSCTGQRWTIKNFIK 521
Cdd:cd23474    81 QLLDCDKVKSILHKRWNFIQNGAIMNLGTGRCLEVENRGNfgIDLILRSCTGQRWTIKNFIK 142
beta-trefoil_Ricin_GALNT8-like cd23438
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 387-518 3.69e-78

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8)-like subfamily; The GALNT8-like subfamily includes GALNT8, GALNT9, GALNT17 and GALNT18. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT9 does not glycosylate apomucin or SDC3. Members of this family comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467316  Cd Length: 134  Bit Score: 241.18  E-value: 3.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 387 NTIAYGELRNNKAKDVCLDQGPQENHTAILYPCHGWGPQLTRYTREGFLHLGALGTTTlLPDTRCLVDNGKSRFPQLLDC 466
Cdd:cd23438     1 NTVAYGEMRNSLVTDLCLDQGPKENHTAILYPCHGWSPQLVRYTKDGQLYLGQLGSTA-SPDTRCLVDDGKSDKPQLLDC 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1788921534 467 DKVKSSLHKRWNFIQNGAIMNKGTGRCLEVESRP---SIDLILRSCTGQRWTIKN 518
Cdd:cd23438    80 SKVKNRLQKYWDFSQGGAIQNRATGRCLEVEEDKlnfGHRLVLQTCSGQKWNIKN 134
beta-trefoil_Ricin_GALNT9 cd23473
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 382-521 1.75e-61

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 9 (GALNT9) and similar proteins; GALNT9 (EC 2.4.1.41), also called polypeptide GalNAc transferase 9, GalNAc-T9, pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT9 does not glycosylate apomucin or SDC3. GALNT9 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467351  Cd Length: 145  Bit Score: 198.26  E-value: 1.75e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 382 MRRYNNTIAYGELRNNKAKDVCLDQGPQENHTAILYPCHGWGPQLTRYTREGFLHLGALGTTTLLPDTRCLVDNGKSRFP 461
Cdd:cd23473     1 MRIYNNTITYGEVRNSKASGYCLDQGSEEDDKAILYPCHGMSSQLVRYSTEGLLQLGPLGSTAFLPDTKCLVDDGRGRTP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788921534 462 QLLDCDKVKSSLHKRWNFIQNGAIMNKGTGRCLEVE----SRPSIDLILRSCTGQRWTIKNFIK 521
Cdd:cd23473    81 TLKKCEDVARPAQRLWDFTQNGPIISRDTGRCLEVEmskdANFGLRLVVQRCSGQKWMIRNWIK 144
beta-trefoil_Ricin_GALNT18 cd23475
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 382-520 1.03e-37

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 18 (GALNT18) and similar proteins; GALNT18 (EC 2.4.1.41), also called polypeptide GalNAc transferase 18, GalNAc-T18, polypeptide GalNAc transferase-like protein 4, GalNAc-T-like protein 4, pp-GaNTase-like protein 4, polypeptide N-acetylgalactosaminyltransferase-like protein 4, protein-UDP acetylgalactosaminyltransferase-like protein 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT18 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467353  Cd Length: 142  Bit Score: 135.44  E-value: 1.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 382 MRRYNNTIAYGELRNNKAKDVCLDQGPQENHTAILYPCHGWGPQLTRYTREGFLHLGALGTTTLLPDTRCLVD-NGKsrf 460
Cdd:cd23475     1 MRMYTDTIAYGVLQNSLKTDLCLDQGPDTDNIPIMYICHGMTPQNVYYTSNQQLHVGILSPTIDDDDNRCLVDvNSR--- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1788921534 461 PQLLDCDKVKSSLHK-RWNFIQNGAIMNKGTGRCLEVESRPSID----LILRSCTGQRWTIKNFI 520
Cdd:cd23475    78 PRLIECSYAKAKRMKlYWLFTQGGSIQNKKSKRCLELQENADNEfgyqLVLQKCSGQRWTITNVL 142
beta-trefoil_Ricin_GALNT8 cd23472
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 379-521 3.48e-34

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8) and similar proteins; GALNT8 (EC 2.4.1.41), also called polypeptide GalNAc transferase 8, GalNAc-T8, pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8, may catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT8 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467350  Cd Length: 146  Bit Score: 126.08  E-value: 3.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 379 YPEMRRYNNTIAYGELRNNKAKDVCLDQGPQENHTAILYPCHGWGPQLTRYTREGFLHLGALGTTTLLPDtRCLVDNGKS 458
Cdd:cd23472     1 YPVLMPIQTIVGYGTMKNSLNENICIDQGPVPGNTPIMYGCHGYSPQFVYYHLTGELYVGGLKADIYASD-RCLTDPGEG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1788921534 459 RFPQLLDCDK-VKSSLHKRWNFIQNGAIMNKGTGRCLEV---ESRPSIDLILRSCTGQRWTIKNFIK 521
Cdd:cd23472    80 WKPELVSCQDaTLKGLNMYWDFKQGTAIINRKTKRCLEIsldKTPSYYTLILQTCTGQKWEIQHVLM 146
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 80-264 1.51e-26

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: 105.55  E-value: 1.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  80 SIIFIFVNEAlSVILRSVHSAVNHTpaHLLKEIILVDDNSdEEELKAPLEEYVHKryPGLVKVVRNQKREGLIRARIEGW 159
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGS-TDGTVEIAEEYAKK--DPRVRVIRLPENRGKAGARNAGL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 160 KVATGQITGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENsahgyswelwcmyISPPKDWWDAG 239
Cdd:pfam00535  75 RAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASR-------------ITLSRLPFFLG 141

                         170       180
                  ....*....|....*....|....*
gi 1788921534 240 DPSLPIRTPAMIGCSFVVNRKFFGE 264
Cdd:pfam00535 142 LRLLGLNLPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
390-514 2.29e-18

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 81.04  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 390 AYGELRNnKAKDVCLD--QGPQENHTAILYPCHG-WGPQLTRYTREGFLHLGAlgtttllpDTRCL--VDNGKSRFPQLL 464
Cdd:pfam00652   1 ATGRIRN-RASGKCLDvpGGSSAGGPVGLYPCHGsNGNQLWTLTGDGTIRSVA--------SDLCLdvGSTADGAKVVLW 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1788921534 465 DCDKVKSSlhKRWNFIQNGA-IMNKGTGRCLEV--ESRPSIDLILRSC----TGQRW 514
Cdd:pfam00652  72 PCHPGNGN--QRWRYDEDGTqIRNPQSGKCLDVsgAGTSNGKVILWTCdsgnPNQQW 126
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 390-518 1.11e-16

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: 76.18  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 390 AYGELRNnKAKDVCLD-QGPQENHTAILYPCHGWG-PQLTRYTREGFLHLGalgtttllpdTRCLVDNGKSRFPQLLDCD 467
Cdd:cd23437     4 AWGEIRN-LGTGLCLDtMGHQNGGPVGLYPCHGMGgNQLFRLNEAGQLAVG----------EQCLTASGSGGKVKLRKCN 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1788921534 468 KVKSslhKRWNFI-QNGAIMNKGTGRCLEVESRPSIdLILRSCTG----QRWTIKN 518
Cdd:cd23437    73 LGET---GKWEYDeATGQIRHKGTGKCLDLNEGTNK-LILQPCDSsspsQKWEFNE 124
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
77-332 3.71e-13

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 68.48  E-value: 3.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  77 PQISIIFIFVNEAlSVILRSVHSAVNHTPAHLlkEIILVDDNSDEEELkapleEYVHKRYPGLVKVVRNQKREGLIRARI 156
Cdd:COG1216     3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTA-----ELLAALAFPRVRVIRNPENLGFAAARN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 157 EGWKVATGQITGFFDAHVEFTAGWAEPVLsriqenrkrvilpsidnikqdnfevqryensahgyswELWCMYISppkdww 236
Cdd:COG1216    75 LGLRAAGGDYLLFLDDDTVVEPDWLERLL-------------------------------------AAACLLIR------ 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 237 dagdpslpirtpamigcsfvvnRKFFGEIGLLDPGMDVYGGEnIELGIKVWLCGGSMEVLPCSRVAHIERKKKPYNNNIg 316
Cdd:COG1216   112 ----------------------REVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRA- 167

                         250
                  ....*....|....*.
gi 1788921534 317 FYTKRNALRVAEVWMD 332
Cdd:COG1216   168 YYLGRNRLLFLRKHGP 183
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 77-196 1.97e-12

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 66.26  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  77 PQISIIFIFVNEAlSVILRSVHSAVNHTPAHLlkEIILVDDNSDEEELKApLEEYVhKRYPGlVKVVRNQKREGLIRARI 156
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTAEI-LRELA-AKDPR-IRVIRLERNRGKGAARN 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1788921534 157 EGWKVATGQITGFFDAHVEFTAGWAEPVLSRIQENRKRVI 196
Cdd:COG0463    76 AGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 73-303 7.59e-12

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: 66.30  E-value: 7.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  73 SKDLPQISIIFIFVNEALsVILRSVHSAVNHTPAHLLKEIILVDDNSDEEELKApLEEYVHKRYPglVKVVRNQKREGLI 152
Cdd:COG1215    25 PADLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEI-ARELAAEYPR--VRVIERPENGGKA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 153 RARIEGWKVATGQITGFFDAHVEFTAGWAEPVLSRIQenrkrvilpsidnikqdnfevqryensahgyswelwcmyispp 232
Cdd:COG1215   101 AALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFA------------------------------------------- 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1788921534 233 kdwwdagDPSLpirtpAMIGCSFVVNRKFFGEIGLLDPGMdvyGGENIELGIKVWLCGGSMEVLPCSRVAH 303
Cdd:COG1215   138 -------DPGV-----GASGANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYE 193
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 81-196 1.44e-11

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: 62.52  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  81 IIFIFVNEAlSVILRSVHSAVNHTPAHLlkEIILVDDNSDEEELKApLEEYVHKRYPglVKVVRNQKREGLIRARIEGWK 160
Cdd:cd00761     1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTLEI-LEEYAKKDPR--VIRVINEENQGLAAARNAGLK 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1788921534 161 VATGQITGFFDAHVEFTAGWAEPVLSRIQENRKRVI 196
Cdd:cd00761    75 AARGEYILFLDADDLLLPDWLERLVAELLADPEADA 110
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 389-517 1.82e-11

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: 61.58  E-value: 1.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 389 IAYGELRNnKAKDVCLDQGPQENHTA---ILYPCHGWGP-QLTRYTREG-FLHlgalGTTTLLpdtrCLvDNGKSRFPQL 463
Cdd:cd23435     2 GYYGALRN-KGSELCLDVNNPNGQGGkpvIMYGCHGLGGnQYFEYTSKGeIRH----NIGKEL----CL-HASGSDEVIL 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 464 LDC--DKVKSSLHKRWNFIQNGAIMNKGTGRCLEVeSRPSIdlILRSCTG----QRWTIK 517
Cdd:cd23435    72 QHCtsKGKDVPPEQKWLFTQDGTIRNPASGLCLHA-SGYKV--LLRTCNPsddsQKWTFI 128
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 387-516 2.40e-11

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: 61.18  E-value: 2.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 387 NTIAYGELRNNKaKDVCLD--QGPQENHTAI-LYPCHG--WGPQLTRYTREGFLHlgalgtttllPDTRCL-VDNGKSRF 460
Cdd:cd23459     3 DVLAYGQVRNPG-TNLCLDtlQRDEDKGYNLgLYPCQGglSSNQLFSLSKKGELR----------REESCAdVQGTEESK 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 461 PQLLDCDKvKSSLHKRWNFIQNGAIMNKGTGRCLEVE-SRPSIDLILRSCTG---QRWTI 516
Cdd:cd23459    72 VILITCHG-LEKFNQKWKHTKGGQIVHLASGKCLDAEgLKSGDDVTLAKCDGslsQKWTF 130
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 403-515 2.83e-10

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: 58.13  E-value: 2.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 403 CLD---QGPQENHTAILYPCHGWGPQLTRYTREGFLHLGalgtttllpDTRCLVDNGKSRFP----QLLDCDkvkSSLHK 475
Cdd:cd23418    16 CLDvpgGSTTNGTRLILWDCHGGANQQFTFTSAGELRVG---------GDKCLDAAGGGTTNgtpvVIWPCN---GGANQ 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1788921534 476 RWNFIQNGAIMNKGTGRCLEVE---SRPSIDLILRSCTG---QRWT 515
Cdd:cd23418    84 KWRFNSDGTIRNVNSGLCLDVAgggTANGTRLILWSCNGgsnQRWR 129
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 387-515 6.47e-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: 56.99  E-value: 6.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 387 NTIAYGELRNnKAKDVCLDQG---PQENHTAILYPCHGWGP-QLTRYTREGFLHLgalgtttllpDTRCLVDNGKSRFPQ 462
Cdd:cd23462     1 EALAYGEIRN-LAGKLCLDAPgrkKELNKPVGLYPCHGQGGnQYWMLTKDGEIRR----------DDLCLDYAGGSGDVT 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1788921534 463 LLDCDKVKSSlhKRWNF-IQNGAIMNKGTGRCLEVeSRPSIDLILRSCTG----QRWT 515
Cdd:cd23462    70 LYPCHGMKGN--QFWIYdEETKQIVHGTSKKCLEL-SDDSSKLVMEPCNGssprQQWE 124
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 397-517 1.15e-09

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 55.98  E-value: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  397 NKAKDVCLDQgPQENHTAILYPCHGWGP-QLTRYTREGflhlgalgTTTLLPDTRCL-VDNGKSRFPQLLDCDKVKSSLh 474
Cdd:smart00458   3 SGNTGKCLDV-NGNKNPVGLFDCHGTGGnQLWKLTSDG--------AIRIKDTDLCLtANGNTGSTVTLYSCDGTNDNQ- 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1788921534  475 kRWNFIQNGAIMNKGTGRCLEV-ESRPSIDLILRSCTG---QRWTIK 517
Cdd:smart00458  73 -YWEVNKDGTIRNPDSGKCLDVkDGNTGTKVILWTCSGnpnQKWIFE 118
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 448-518 4.12e-08

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 51.74  E-value: 4.12e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1788921534  448 DTRCLVDNGKSRFPQLLDCDKVKSslHKRWNFIQNGAIMNKGTGRCLEVESRPSIDLILRSCTG----QRWTIKN 518
Cdd:smart00458   6 TGKCLDVNGNKNPVGLFDCHGTGG--NQLWKLTSDGAIRIKDTDLCLTANGNTGSTVTLYSCDGtndnQYWEVNK 78
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 387-518 2.71e-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: 49.62  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 387 NTIAYGELRNnKAKDVCLDQ-GPQENHTAILYPCHGWG-PQLTRYTREGFLHlgalgtttllPDTRCLvDNGKSRFP-QL 463
Cdd:cd23433     2 DYYSLGEIRN-VETNLCLDTmGRKAGEKVGLSSCHGQGgNQVFSYTAKGEIR----------SDDLCL-DASRKGGPvKL 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 464 LDCDkVKSSLHKrWNFI-QNGAIMNKGTGRCLEV-ESRPSIDLILRSCTG---QRWTIKN 518
Cdd:cd23433    70 EKCH-GMGGNQE-WEYDkETKQIRHVNSGLCLTApNEDDPNEPVLRPCDGgpsQKWELEG 127
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 390-517 3.57e-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: 48.98  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 390 AYGELRNNkAKDVCLD-QGPQENH-TAILYPCHGWGP-QLTRYTREGflhlgalgttTLLPDTRCL-VDNGKSrfPQLLD 465
Cdd:cd23460     1 GLGQIKHT-ESGLCLDwAGESNGDkTVALKPCHGGGGnQFWMYTGDG----------QIRQDHLCLtADEGNK--VTLRE 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1788921534 466 CDKVKSSLhkRWNFIQN-GAIMNKGTGRCLEVESRPSIdLILRSCTG----QRWTIK 517
Cdd:cd23460    68 CADQLPSQ--EWSYDEKtGTIRHRSTGLCLTLDANNDV-VILKECDSnslwQKWIFQ 121
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 87-172 6.17e-06

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 47.53  E-value: 6.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  87 NEA--LSVILRSVHSAVNHTPAhllkEIILVDDNS-DE-----EELKapleeyvhKRYPGLVKVVRNQKReGLIRARIEG 158
Cdd:cd06442     7 NERenIPELIERLDAALKGIDY----EIIVVDDNSpDGtaeivRELA--------KEYPRVRLIVRPGKR-GLGSAYIEG 73

                          90
                  ....*....|....
gi 1788921534 159 WKVATGQITGFFDA 172
Cdd:cd06442    74 FKAARGDVIVVMDA 87
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 87-172 6.39e-06

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 46.80  E-value: 6.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  87 NEA--LSVILRSVHSAVNHTPAHllkEIILVDDNSDEEELKApLEEYvHKRYPGlVKVVRNQKREGLIRARIEGWKVATG 164
Cdd:cd04179     7 NEEenIPELVERLLAVLEEGYDY---EIIVVDDGSTDGTAEI-AREL-AARVPR-VRVIRLSRNFGKGAAVRAGFKAARG 80


                  ....*...
gi 1788921534 165 QITGFFDA 172
Cdd:cd04179    81 DIVVTMDA 88
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 84-305 8.47e-06

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: 46.01  E-value: 8.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  84 IFVN-EALSVILRSVHSAVNHTPAHLlkEIILVDDNSDEEELkapleEYVHKRYPGlVKVVRNQKREGLIRARIEGWKVA 162
Cdd:cd04186     2 IIVNyNSLEYLKACLDSLLAQTYPDF--EVIVVDNASTDGSV-----ELLRELFPE-VRLIRNGENLGFGAGNNQGIREA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 163 TGQITGFFDAHVEFTAGWAEPVLSRIQENRkrvilpsidnikqdnfevqryensahgyswelwcmyisppkdwwDAGdps 242
Cdd:cd04186    74 KGDYVLLLNPDTVVEPGALLELLDAAEQDP--------------------------------------------DVG--- 106

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1788921534 243 lpIRTPAMIGCSFVVNRKFFGEIGLLDPGMDVYgGENIELGIKVWLCGGSMEVLPCSRVAHIE 305
Cdd:cd04186   107 --IVGPKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYHHG 166
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 397-513 1.03e-05

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 15 (GALNT15) and similar proteins; GALNT15 (EC 2.4.1.41), also called polypeptide GalNAc transferase 15, GalNAc-T15, polypeptide GalNAc transferase-like protein 2, GalNAc-T-like protein 2, pp-GaNTase-like protein 2, polypeptide N-acetylgalactosaminyltransferase-like protein 2, protein-UDP acetylgalactosaminyltransferase-like protein 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, GALNT15 can transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. It prefers Muc1a as its substrate. GALNT15 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467320 [Multi-domain]  Cd Length: 124  Bit Score: 44.74  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 397 NKAKDVCLDQGPQEN---HTAILYPCHGW-GPQLTRYT-----REGFLHLgalgtttllpdtrCLVDNGKSRFPQllDCD 467
Cdd:cd23442    10 NTGTGYCADYIHGWRlagGPVELSPCSGQnGNQLFEYTsdkeiRFGSLQL-------------CLDVRQEQVVLQ--NCT 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1788921534 468 KVKSSLHkrWNFIQNGAIMNKGTGRCLE-VESRPSIDLILRSCTGQR 513
Cdd:cd23442    75 KEKTSQK--WDFQETGRIVHILSGKCIEaVESENSKLLFLSPCNGQR 119
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 403-515 1.67e-05

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


Pssm-ID: 467329 [Multi-domain]  Cd Length: 125  Bit Score: 44.25  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 403 CLD---QGPQENHTAILYPCHGWGPQLTRYTREGFLHlgALGtttllpdtRCL--VDNGKSRFP--QLLDCDkvkSSLHK 475
Cdd:cd23451    13 CLDvpgSSTADGNPVQIYTCNGTAAQKWTLGTDGTLR--VLG--------KCLdvSGGGTANGTlvQLWDCN---GTGAQ 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1788921534 476 RWNFIQNGAIMNKGTGRCLEVES---RPSIDLILRSCTG---QRWT 515
Cdd:cd23451    80 KWVPRADGTLYNPQSGKCLDAPGgstTDGTQLQLYTCNGtaaQQWT 125
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 390-515 1.74e-05

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


Pssm-ID: 467294 [Multi-domain]  Cd Length: 120  Bit Score: 44.35  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 390 AYGELRNNkAKDVCLDQGPQENhtAILYPCHGWGPQL--TRYTREGFLHLGALGTTtllpdtRCLVDNGKSRFpQLLDCD 467
Cdd:cd23415     1 GTVRLRNV-ATGRCLDSNAGGN--VYTGPCNGGPYQRwtWSGVGDGTVTLRNAATG------RCLDSNGNGGV-YTLPCN 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1788921534 468 kvkSSLHKRWNFIQ----NGAIMNKGTGRCLevESRPSIDLILRSCTG---QRWT 515
Cdd:cd23415    71 ---GGSYQRWRVTStsggGVTLRNVATGRCL--DSNGSGGVYTRPCNGgsyQRWR 120
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 390-514 2.23e-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: 44.28  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 390 AYGELRNnKAKDVCLD--QGPQENHTAI-LYPCHGWGPQLTRYTREGFlhlgalGTTTLLP--DTRCLVDNGKSRFP--- 461
Cdd:cd00161     1 GTYRIVN-AASGKCLDvaGGSTANGAPVqQWTCNGGANQQWTLTPVGD------GYYTIRNvaSGKCLDVAGGSTANgan 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788921534 462 -QLLDCDkvkSSLHKRWNFIQNG----AIMNKGTGRCLEVESRPSID---LILRSCTG---QRW 514
Cdd:cd00161    74 vQQWTCN---GGDNQQWRLEPVGdgyyRIVNKHSGKCLDVSGGSTANganVQQWTCNGganQQW 134
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 450-515 4.32e-05

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


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 42.97  E-value: 4.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1788921534 450 RCLVDNGKSRFPQLLDCDKvkSSLHKRWNFIQNGAIMNKGTGRCLEVESR-PSIDLILRSC----TGQRWT 515
Cdd:cd23385    12 KCLAARSSSSKVSLSTCNP--NSPNQQWKWTSGHRLFNVGTGKCLGVSSSsPSSPLRLFECdsedELQKWK 80
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 390-516 4.66e-05

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467312 [Multi-domain]  Cd Length: 121  Bit Score: 43.08  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 390 AYGELRNnkaKDVCLDQ-GPQENHTAILYPCHGWG-PQLTRYTREGFLHLGALgtttllpdtrCL-VDNGKSRFPQLL-D 465
Cdd:cd23434     1 KFGSLKQ---GNLCLDTlGHKAGGTVGLYPCHGTGgNQEWSFTKDGQIKHDDL----------CLtVVDRAPGSLVTLqP 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1788921534 466 CDKVKSSlhKRWNFIQNGA-IMNKGTGRCLEVESRPSIDLILRSCTG----QRWTI 516
Cdd:cd23434    68 CREDDSN--QKWEQIENNSkLRHVGSNLCLDSRNAKSGGLTVETCDPssgsQQWKF 121
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 87-172 7.04e-05

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 44.10  E-value: 7.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  87 NEAlSVILRSVHSAVNHTPAHLLK--EIILVDDNSDEEELKApLEEYVHKrYPGLVKVVRNQKREGLIRARIEGWKVATG 164
Cdd:cd04188     7 NEE-KRLPPTLEEAVEYLEERPSFsyEIIVVDDGSKDGTAEV-ARKLARK-NPALIRVLTLPKNRGKGGAVRAGMLAARG 83


                  ....*...
gi 1788921534 165 QITGFFDA 172
Cdd:cd04188    84 DYILFADA 91
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 87-172 7.42e-05

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: 43.37  E-value: 7.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  87 NEAlSVILRSVHSAVNHTpaHLLKEIILVDDNSDEEELKAPLEEYVhkRYPGLVKVVRNQKREGLIRARIEGWKVATGQI 166
Cdd:cd06423     7 NEE-AVIERTIESLLALD--YPKLEVIVVDDGSTDDTLEILEELAA--LYIRRVLVVRDKENGGKAGALNAGLRHAKGDI 81


                  ....*.
gi 1788921534 167 TGFFDA 172
Cdd:cd06423    82 VVVLDA 87
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 77-171 8.14e-05

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 43.73  E-value: 8.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  77 PQISIIFIFVNEALSVILRSVHSAVNHTPAHLlkEIILVDDNSDEEELKAPLEEYV--HKRypglVKVVRNQKREGLIRA 154
Cdd:cd04184     1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYAaqDPR----IKVVFREENGGISAA 74

                          90
                  ....*....|....*..
gi 1788921534 155 RIEGWKVATGQITGFFD 171
Cdd:cd04184    75 TNSALELATGEFVALLD 91
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 391-517 1.07e-04

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 12 (GALNT12) and similar proteins; GALNT12 (EC 2.4.1.41), also called polypeptide GalNAc transferase 12, GalNAc-T12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT12 has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with non-glycosylated Muc2 and Muc7. It displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. It may play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs. GALNT12 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467349  Cd Length: 140  Bit Score: 42.48  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 391 YGELRNNKAKDVCLDQGP-QENHTA----ILYPCHGWGP-QLTRYTRegflhLGALGTTTLLPDTRCLVDNGKSRFPQLL 464
Cdd:cd23471     4 FGMLKNKGMTNYCFDYNPpDEHQIAghqvILYQCHGMGQnQFFEYTS-----QNEIRYNTRQPEGCAAVDAGTDFLTMHL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1788921534 465 dCDKVKSSLHKRWNFI--QNGAIMNKGTGRCLEVESRPSIDL---ILRSCTG---QRWTIK 517
Cdd:cd23471    79 -CRENRQAVPENQKFIfrEDGSLFHVQTQKCVQAVRNESSGSpapVLRPCTDsdhQKWFFK 138
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 450-516 2.74e-04

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: 41.20  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 450 RCLVDNGKSRFP----QLLDCDkvkSSLHKRWNFIQNGA----IMNKGTGRCLEVESRPSID---LILRSCTG---QRWT 515
Cdd:cd00161    12 KCLDVAGGSTANgapvQQWTCN---GGANQQWTLTPVGDgyytIRNVASGKCLDVAGGSTANganVQQWTCNGgdnQQWR 88


                  .
gi 1788921534 516 I 516
Cdd:cd00161    89 L 89
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 79-174 6.43e-04

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 41.47  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  79 ISIIFIFVNEALSVILRSVHSAVNHTPAhllkEIILVDDNSDEEELKAPLEEYVHKRypglvKVVRNQKREGLIRARIEG 158
Cdd:cd06434     2 VTVIIPVYDEDPDVFRECLRSILRQKPL----EIIVVTDGDDEPYLSILSQTVKYGG-----IFVITVPHPGKRRALAEG 72

                          90
                  ....*....|....*.
gi 1788921534 159 WKVATGQITGFFDAHV 174
Cdd:cd06434    73 IRHVTTDIVVLLDSDT 88
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 387-516 1.02e-03

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 11 (GALNT11) and similar proteins; GALNT11 (EC 2.4.1.41), also called polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes its activation, modulating the balance between motile and immotile (sensory) cilia at the left-right organizer (LRO). GALNT11 displays the same enzyme activity toward MUC1, MUC4, and EA2 as GALNT1. It is not involved in glycosylation of erythropoietin (EPO). GALNT11 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467318 [Multi-domain]  Cd Length: 127  Bit Score: 39.28  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534 387 NTIAYGELRNNkAKDVCL--DQGPQENHTA-ILYPCHGWGP-QLTRYTREGFLHLGALGtttllpdtrCL-VDNGKSRFP 461
Cdd:cd23440     1 KVIRKGQLKHA-GSGLCLvaEDEVSQKGSLlVLRPCSRNDKkQLWYYTEDGELRLANLL---------CLdSSETSSDFP 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1788921534 462 QLLDCDKvkSSLHKRWNFIQNGAIMNKGTGRCLEV-ESRPSIDLILRSCTG---QRWTI 516
Cdd:cd23440    71 RLMKCHG--SGGSQQWRFKKDNRLYNPASGQCLAAsKNGTSGYVTMDICSDspsQKWVF 127
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 74-172 3.78e-03

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. 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 of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 39.10  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788921534  74 KDLPQISIIFIFVNEAlSVILRSVHSAVN-HTPAHLLkEIILVDDNSD--EEELkapLEEYVHKRypglVKVVRNQKREG 150
Cdd:cd06439    26 AYLPTVTIIIPAYNEE-AVIEAKLENLLAlDYPRDRL-EIIVVSDGSTdgTAEI---AREYADKG----VKLLRFPERRG 96

                          90       100
                  ....*....|....*....|..
gi 1788921534 151 LIRARIEGWKVATGQITGFFDA 172
Cdd:cd06439    97 KAAALNRALALATGEIVVFTDA 118
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 450-519 8.88e-03

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


Pssm-ID: 467294 [Multi-domain]  Cd Length: 120  Bit Score: 36.26  E-value: 8.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1788921534 450 RCLVDNGKSRfPQLLDCDkvkSSLHKRWNFIQNGA----IMNKGTGRCLevESRPSIDLILRSCTG---QRWTIKNF 519
Cdd:cd23415    12 RCLDSNAGGN-VYTGPCN---GGPYQRWTWSGVGDgtvtLRNAATGRCL--DSNGNGGVYTLPCNGgsyQRWRVTST 82
 
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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