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Conserved domains on  [gi|1775678398|ref|NP_001363321|]
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polypeptide N-acetylgalactosaminyltransferase 13 isoform 1 [Homo sapiens]

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
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 ...
118-418 0e+00

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: 529.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 118 SVVIVFHNEAWSTLLRTVYSVINRSPHYLLSEVILVDDASERDFLKLTLENYVKNLEVPVKIIRMEERSGLIRARLRGAA 197
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 198 ASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREmdRR 277
Cdd:cd02510    81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 278 KGDRTLPVRTPTMAGGLFSIDRNYFEEIGTYDAGMDIWGGENLEMSFRIWQCGGSLEIVTCSHVGHVFR-KATPYTFPGG 356
Cdd:cd02510   159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1775678398 357 TGhVINKNNRRLAEVWMDEFKDFFYIISPGVVKVDYGDVSVRKTLRENLKCKPFSWYLENIY 418
Cdd:cd02510   239 SG-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
425-551 7.75e-100

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 13 (GALNT13) and similar proteins; GALNT13 (EC 2.4.1.41), also called polypeptide GalNAc transferase 13, GalNAc-T13, pp-GaNTase 13, protein-UDP acetylgalactosaminyltransferase 13, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. GALNT13 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). The model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


:

Pssm-ID: 467345  Cd Length: 127  Bit Score: 297.71  E-value: 7.75e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 425 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQL 504
Cdd:cd23467     1 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNQL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1775678398 505 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 551
Cdd:cd23467    81 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMKDCSGSRSQQWLLRN 127
 
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 ...
118-418 0e+00

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: 529.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 118 SVVIVFHNEAWSTLLRTVYSVINRSPHYLLSEVILVDDASERDFLKLTLENYVKNLEVPVKIIRMEERSGLIRARLRGAA 197
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 198 ASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREmdRR 277
Cdd:cd02510    81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 278 KGDRTLPVRTPTMAGGLFSIDRNYFEEIGTYDAGMDIWGGENLEMSFRIWQCGGSLEIVTCSHVGHVFR-KATPYTFPGG 356
Cdd:cd02510   159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1775678398 357 TGhVINKNNRRLAEVWMDEFKDFFYIISPGVVKVDYGDVSVRKTLRENLKCKPFSWYLENIY 418
Cdd:cd02510   239 SG-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
425-551 7.75e-100

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 13 (GALNT13) and similar proteins; GALNT13 (EC 2.4.1.41), also called polypeptide GalNAc transferase 13, GalNAc-T13, pp-GaNTase 13, protein-UDP acetylgalactosaminyltransferase 13, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. GALNT13 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). The model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467345  Cd Length: 127  Bit Score: 297.71  E-value: 7.75e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 425 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQL 504
Cdd:cd23467     1 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNQL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1775678398 505 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 551
Cdd:cd23467    81 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMKDCSGSRSQQWLLRN 127
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
118-299 3.69e-37

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: 135.22  E-value: 3.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 118 SVVIVFHNEaWSTLLRTVYSVINRSphYLLSEVILVDDASERDFLKLtLENYVKNLEvPVKIIRMEERSGLIRARLRGAA 197
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQT--YPNFEIIVVDDGSTDGTVEI-AEEYAKKDP-RVRVIRLPENRGKAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 198 ASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMagsdmtyggfnWKLNFRWYPVPQREMDRR 277
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR-----------RASRITLSRLPFFLGLRL 144
                         170       180
                  ....*....|....*....|..
gi 1775678398 278 KGdRTLPVRTPTMAGGLFSIDR 299
Cdd:pfam00535 145 LG-LNLPFLIGGFALYRREALE 165
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
431-547 4.23e-37

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 133.81  E-value: 4.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLDNMGRKE-NEKVGIFNCHGMGGNQVFSYTADKEIRT--DDLCLDVSR--LNGPVIMLKCHHMRGNQLW 505
Cdd:pfam00652   3 GRIRNRASGKCLDVPGGSSaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDVGStaDGAKVVLWPCHPGNGNQRW 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1775678398 506 EYDAERLTLRHVNSNQCLDEPSEEDKMVP-TMQDC-SGSRSQQW 547
Cdd:pfam00652  83 RYDEDGTQIRNPQSGKCLDVSGAGTSNGKvILWTCdSGNPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
433-550 1.69e-29

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 112.60  E-value: 1.69e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398  433 IRNVETNQCLDNMGRKENekVGIFNCHGMGGNQVFSYTADKEIRT--DDLCLDVSRLNG-PVIMLKCHHMRGNQLWEYDA 509
Cdd:smart00458   1 IISGNTGKCLDVNGNKNP--VGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGsTVTLYSCDGTNDNQYWEVNK 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1775678398  510 ERlTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLR 550
Cdd:smart00458  79 DG-TIRNPDSGKCLDVKDGNTGTKVILWTCSGNPNQKWIFE 118
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
115-312 1.10e-15

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 75.89  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 115 PNTSVVIVFHNEAwSTLLRTVYSVINRSphYLLSEVILVDDASERDFLKLtLENYVKNLEvPVKIIRMEERSGLIRARLR 194
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQT--YPDFEIIVVDDGSTDGTAEI-LRELAAKDP-RIRVIRLERNRGKGAARNA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 195 GAAASKGQVITFLDAHCECTLGWLEPLLARIKEDrktvvcpiidvisddtfeymaGSDMTYGGFNWKLNFRWYPVPQREM 274
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEG---------------------PADLVYGSRLIREGESDLRRLGSRL 135
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1775678398 275 DRRkgdRTLPVRTPTMAGGLFSIDRNYFEEIGtYDAGM 312
Cdd:COG0463   136 FNL---VRLLTNLPDSTSGFRLFRREVLEELG-FDEGF 169
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
418-547 9.68e-14

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 70.97  E-value: 9.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 418 YPDSQIPRR-YYSLGEIRnVETNQCLDNMGR-KENEKVGIFNCHGmGGNQVFSYTADKEIRTDDLCLDVSRLN----GPV 491
Cdd:NF035930  106 YPDYPGQGGgGWGGREIR-GKGGLCLDVSGGlRPGNGLIVYNCNG-GENQRFTWGRGGELRVGDLCLDVADGNtrdgARV 183
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 492 IMLKCHHMRgNQLWeyDAERLTLRHVNSNQCLDepSEEDKMVP----TMQDCSGSRSQQW 547
Cdd:NF035930  184 IAWSCSGGP-NQRW--RWRGGQIRSRLSGKCLD--IEGGRARPgqpvIVWSCNGGPNQRW 238
 
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 ...
118-418 0e+00

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: 529.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 118 SVVIVFHNEAWSTLLRTVYSVINRSPHYLLSEVILVDDASERDFLKLTLENYVKNLEVPVKIIRMEERSGLIRARLRGAA 197
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 198 ASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREmdRR 277
Cdd:cd02510    81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 278 KGDRTLPVRTPTMAGGLFSIDRNYFEEIGTYDAGMDIWGGENLEMSFRIWQCGGSLEIVTCSHVGHVFR-KATPYTFPGG 356
Cdd:cd02510   159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1775678398 357 TGhVINKNNRRLAEVWMDEFKDFFYIISPGVVKVDYGDVSVRKTLRENLKCKPFSWYLENIY 418
Cdd:cd02510   239 SG-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
425-551 7.75e-100

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 13 (GALNT13) and similar proteins; GALNT13 (EC 2.4.1.41), also called polypeptide GalNAc transferase 13, GalNAc-T13, pp-GaNTase 13, protein-UDP acetylgalactosaminyltransferase 13, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. GALNT13 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). The model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467345  Cd Length: 127  Bit Score: 297.71  E-value: 7.75e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 425 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQL 504
Cdd:cd23467     1 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNQL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1775678398 505 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 551
Cdd:cd23467    81 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMKDCSGSRSQQWLLRN 127
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
425-551 1.84e-89

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: 271.15  E-value: 1.84e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 425 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQL 504
Cdd:cd23466     1 RHYFSLGEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDDLCLDVSKLNGPVMMLKCHHLKGNQL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1775678398 505 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 551
Cdd:cd23466    81 WEYDPVKLTLLHVNSNQCLDKATEEDSQVPSIRDCNGSRSQQWLLRN 127
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
425-551 3.95e-76

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: 236.44  E-value: 3.95e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 425 RRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQL 504
Cdd:cd23433     1 LDYYSLGEIRNVETNLCLDTMGRKAGEKVGLSSCHGQGGNQVFSYTAKGEIRSDDLCLDASRKGGPVKLEKCHGMGGNQE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1775678398 505 WEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 551
Cdd:cd23433    81 WEYDKETKQIRHVNSGLCLTAPNEDDPNEPVLRPCDGGPSQKWELEG 127
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
428-550 1.59e-44

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: 153.68  E-value: 1.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 428 YSLGEIRNVETNQCLDNMGRK--ENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQLW 505
Cdd:cd23462     3 LAYGEIRNLAGKLCLDAPGRKkeLNKPVGLYPCHGQGGNQYWMLTKDGEIRRDDLCLDYAGGSGDVTLYPCHGMKGNQFW 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1775678398 506 EYDAERLTLRHVNSNQCLDepSEEDKMVPTMQDCSG-SRSQQWLLR 550
Cdd:cd23462    83 IYDEETKQIVHGTSKKCLE--LSDDSSKLVMEPCNGsSPRQQWEFE 126
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
431-547 6.91e-41

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: 143.98  E-value: 6.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKChHMRGNQLWEYDAE 510
Cdd:cd23437     6 GEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKC-NLGETGKWEYDEA 84
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1775678398 511 RLTLRHVNSNQCLDEPSEEDKMvpTMQDCSGSR-SQQW 547
Cdd:cd23437    85 TGQIRHKGTGKCLDLNEGTNKL--ILQPCDSSSpSQKW 120
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
118-299 3.69e-37

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: 135.22  E-value: 3.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 118 SVVIVFHNEaWSTLLRTVYSVINRSphYLLSEVILVDDASERDFLKLtLENYVKNLEvPVKIIRMEERSGLIRARLRGAA 197
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQT--YPNFEIIVVDDGSTDGTVEI-AEEYAKKDP-RVRVIRLPENRGKAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 198 ASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMagsdmtyggfnWKLNFRWYPVPQREMDRR 277
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR-----------RASRITLSRLPFFLGLRL 144
                         170       180
                  ....*....|....*....|..
gi 1775678398 278 KGdRTLPVRTPTMAGGLFSIDR 299
Cdd:pfam00535 145 LG-LNLPFLIGGFALYRREALE 165
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
431-547 4.23e-37

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 133.81  E-value: 4.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLDNMGRKE-NEKVGIFNCHGMGGNQVFSYTADKEIRT--DDLCLDVSR--LNGPVIMLKCHHMRGNQLW 505
Cdd:pfam00652   3 GRIRNRASGKCLDVPGGSSaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDVGStaDGAKVVLWPCHPGNGNQRW 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1775678398 506 EYDAERLTLRHVNSNQCLDEPSEEDKMVP-TMQDC-SGSRSQQW 547
Cdd:pfam00652  83 RYDEDGTQIRNPQSGKCLDVSGAGTSNGKvILWTCdSGNPNQQW 126
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
431-547 6.31e-30

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: 113.98  E-value: 6.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLDNMGRKENEKVGIFNC--HGMGGNQVFSYTADKEIR--TDDLCLDVSRL--NGPVIMLKCHHMRGNQL 504
Cdd:cd23439     3 GEIRNVGSGLCIDTKHGGENDEVRLSKCvkDGGGGEQQFELTWHEDIRpkKRKVCFDVSSHtpGAPVILYACHGMKGNQL 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1775678398 505 WEYDAERLTLRHVNSNQCLDEPSEEDKMVptMQDC-SGSRSQQW 547
Cdd:cd23439    83 WKYRPNTKQLYHPVSGLCLDADPGSGKVF--MNHCdESSDTQKW 124
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
431-547 8.40e-30

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: 113.19  E-value: 8.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNveTNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDV--SRLNGPVIMLKCHHMRGNQLWEYD 508
Cdd:cd23434     3 GSLKQ--GNLCLDTLGHKAGGTVGLYPCHGTGGNQEWSFTKDGQIKHDDLCLTVvdRAPGSLVTLQPCREDDSNQKWEQI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1775678398 509 AERLTLRHVNSNQCLDEPSEEDKMVpTMQDCSG-SRSQQW 547
Cdd:cd23434    81 ENNSKLRHVGSNLCLDSRNAKSGGL-TVETCDPsSGSQQW 119
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
433-550 1.69e-29

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 112.60  E-value: 1.69e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398  433 IRNVETNQCLDNMGRKENekVGIFNCHGMGGNQVFSYTADKEIRT--DDLCLDVSRLNG-PVIMLKCHHMRGNQLWEYDA 509
Cdd:smart00458   1 IISGNTGKCLDVNGNKNP--VGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGsTVTLYSCDGTNDNQYWEVNK 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1775678398  510 ERlTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLR 550
Cdd:smart00458  79 DG-TIRNPDSGKCLDVKDGNTGTKVILWTCSGNPNQKWIFE 118
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
429-550 3.27e-29

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: 111.77  E-value: 3.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 429 SLGEIRNVETNQCLDNMGRKENEK-VGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVsRLNGPVIMLKCHHMRGNQLWEY 507
Cdd:cd23460     1 GLGQIKHTESGLCLDWAGESNGDKtVALKPCHGGGGNQFWMYTGDGQIRQDHLCLTA-DEGNKVTLRECADQLPSQEWSY 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1775678398 508 DAERLTLRHVNSNQCLDEPSEEDkmVPTMQDCSGSR-SQQWLLR 550
Cdd:cd23460    80 DEKTGTIRHRSTGLCLTLDANND--VVILKECDSNSlWQKWIFQ 121
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
431-547 1.89e-28

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: 110.10  E-value: 1.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLDNMGRKENEK--VGIFNCHGMG-GNQVFSYTADKEIRTDDLCLDVS-RLNGPVIMLKCHH-MRGNQLW 505
Cdd:cd23459     8 GQVRNPGTNLCLDTLQRDEDKGynLGLYPCQGGLsSNQLFSLSKKGELRREESCADVQgTEESKVILITCHGlEKFNQKW 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1775678398 506 EYDAERlTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQW 547
Cdd:cd23459    88 KHTKGG-QIVHLASGKCLDAEGLKSGDDVTLAKCDGSLSQKW 128
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
424-548 3.82e-23

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: 95.09  E-value: 3.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 424 PRRYyslGEIRNVETNQCLDNMGRKENE--KVGIFNCHGMGGNQVFSYTADKEIRTD---DLCLDVSRlNGPVIMLKCHH 498
Cdd:cd23435     1 PGYY---GALRNKGSELCLDVNNPNGQGgkPVIMYGCHGLGGNQYFEYTSKGEIRHNigkELCLHASG-SDEVILQHCTS 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1775678398 499 ----MRGNQLWEYDAERlTLRHVNSNQCLdepsEEDKMVPTMQDCSGS-RSQQWL 548
Cdd:cd23435    77 kgkdVPPEQKWLFTQDG-TIRNPASGLCL----HASGYKVLLRTCNPSdDSQKWT 126
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
426-547 8.53e-20

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: 85.18  E-value: 8.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 426 RYYSLGEIRNVETNQCLDNM--GRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDD--LCLDVSrlNGPVIMLKCHHMRG 501
Cdd:cd23442     1 APYFSGQLYNTGTGYCADYIhgWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSlqLCLDVR--QEQVVLQNCTKEKT 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1775678398 502 NQLWEYDAERlTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQW 547
Cdd:cd23442    79 SQKWDFQETG-RIVHILSGKCIEAVESENSKLLFLSPCNGQRNQMW 123
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
431-549 7.50e-18

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: 80.78  E-value: 7.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLDNMGRKENEKVGIFNC-HGMGG-----NQVFSYTADKEIRTDD------LCLDVSRLNGPVIMLKCHH 498
Cdd:cd23476     8 GEIRNVGTGLCADTKHGALGSPLRLEGCvKGRGEaawnnGQVFTFGWREDIRPGDpqhtkkFCFDAISHNSPVTLYDCHG 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1775678398 499 MRGNQLWEYDAERlTLRHVNSNQCLDEPSEEDKMVptMQDCS-GSRSQQWLL 549
Cdd:cd23476    88 MKGNQLWRYRKDK-TLYHPVSNSCMDCSESDHRIF--MNTCNpSSPTQQWLF 136
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
431-547 1.36e-17

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: 78.91  E-value: 1.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLDNMGRK--ENEKVGIFNCHGmGGNQVFSYTADKEIRTDDLCLDVSR---LNG-PVIMLKCHHMrGNQL 504
Cdd:cd23451     3 GPVRLANAGKCLDVPGSStaDGNPVQIYTCNG-TAAQKWTLGTDGTLRVLGKCLDVSGggtANGtLVQLWDCNGT-GAQK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1775678398 505 WEYDAERlTLRHVNSNQCLDEPSeeDKMVPTMQ----DCSGSRSQQW 547
Cdd:cd23451    81 WVPRADG-TLYNPQSGKCLDAPG--GSTTDGTQlqlyTCNGTAAQQW 124
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
429-547 1.48e-17

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: 78.93  E-value: 1.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 429 SLGEIRNVETNQCLD--NMGRKENEKVGIFNCHGmGGNQVFSYTADKEIR-TDDLCLDVS---RLNG-PVIMLKCHHmRG 501
Cdd:cd23418     4 GGGQIRGYGSGRCLDvpGGSTTNGTRLILWDCHG-GANQQFTFTSAGELRvGGDKCLDAAgggTTNGtPVVIWPCNG-GA 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1775678398 502 NQLWEYDAERlTLRHVNSNQCLDEPSEEDKMVPTMQ--DCSGSRSQQW 547
Cdd:cd23418    82 NQKWRFNSDG-TIRNVNSGLCLDVAGGGTANGTRLIlwSCNGGSNQRW 128
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
119-234 3.67e-17

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: 78.70  E-value: 3.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 119 VVIVFHNEAwSTLLRTVYSVINRSPHYLlsEVILVDDASERDFLKLtLENYVKNlEVPVKIIRMEERSGLIRARLRGAAA 198
Cdd:cd00761     1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTLEI-LEEYAKK-DPRVIRVINEENQGLAAARNAGLKA 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1775678398 199 SKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVC 234
Cdd:cd00761    76 ARGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
431-549 3.84e-17

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: 77.80  E-value: 3.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLdnMGRKENEKVG----IFNCHGMGGNQVFSYTADKEIRTDD-LCLDVSRLNGPVIML-KCHHMRGNQL 504
Cdd:cd23440     6 GQLKHAGSGLCL--VAEDEVSQKGsllvLRPCSRNDKKQLWYYTEDGELRLANlLCLDSSETSSDFPRLmKCHGSGGSQQ 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1775678398 505 WEYDAERlTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLL 549
Cdd:cd23440    84 WRFKKDN-RLYNPASGQCLAASKNGTSGYVTMDICSDSPSQKWVF 127
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
428-547 5.59e-17

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: 77.44  E-value: 5.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 428 YSLGEIRNVE-TNQCLDNMGRKENEKVGIFNCHG----MGGNQVFSYTADKEIR--TDDLCLDVSRLNgpVIMLKCHHMR 500
Cdd:cd23461     1 FASGVIQSVAfPNLCLDILGRSHGGPPVLAKCSSnksmPGTFQNFSLTFHRQIKhgTSDDCLEVRGNN--VRLSRCHYQG 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1775678398 501 GNQLWEYDAERLTLRH-VNSNQCLdEPSEEDKMVpTMQDC-SGSRSQQW 547
Cdd:cd23461    79 GNQYWKYDYETHQLINgGQNNKCL-EADVESLKI-TLSICdSDNVEQKW 125
beta-trefoil_Ricin_GALNTL6 cd23477
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
429-554 1.24e-16

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: 76.90  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 429 SLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGN------QVFSYTADKEIR------TDDLCLDVSRLNGPVIMLKC 496
Cdd:cd23477     6 AWGEIRNVAANLCVDSKHGATGTELRLDICVKDGSErtwsheQLFTFGWREDIRpgeplhTRKFCFDAISHNSPVTLYDC 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1775678398 497 HHMRGNQLWEYDAERlTLRHVNSNQCLDEPSEEDKMVptMQDCS-GSRSQQWLLR--NMTL 554
Cdd:cd23477    86 HGMKGNQLWSYRKDK-TLFHPVSNSCMDCNPADKKIF--MNRCDpLSETQQWIFEhtNMTV 143
beta-trefoil_Ricin_GALNT3 cd23468
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
431-550 4.53e-16

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) and similar proteins; GALNT3 (EC 2.4.1.41), also called polypeptide GalNAc transferase 3, GalNAc-T3, pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT3 has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. It probably glycosylates fibronectin in vivo as well as FGF23. It plays a central role in phosphate homeostasis. GALNT3 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467346  Cd Length: 129  Bit Score: 74.85  E-value: 4.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLDNMGRKENEKVGI-FNCHGMGGNQVFSYTADKEIRTD---DLCLDVSRlnGPVIMLKCHH------MR 500
Cdd:cd23468     6 GAIKNVGKELCLDVGENNHGGKPLImYNCHGLGGNQYFEYSTHHEIRHNiqkELCLHGSQ--GSVQLKECTYkgrntaVL 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1775678398 501 GNQLWEYDAERLtLRHVNSNQCLDEPSEEDKMVPtmqdCSGSRS-QQWLLR 550
Cdd:cd23468    84 PEEKWELQKDQL-LYNPALNMCLSANGENPSLVP----CNPSDPfQQWIFR 129
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
426-505 6.00e-16

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 74.49  E-value: 6.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 426 RYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTAD-KEIR--TDDLCLDVSR---LNGPVIMLKCHHM 499
Cdd:pfam00652  41 TLTGDGTIRSVASDLCLDVGSTADGAKVVLWPCHPGNGNQRWRYDEDgTQIRnpQSGKCLDVSGagtSNGKVILWTCDSG 120

                  ....*.
gi 1775678398 500 RGNQLW 505
Cdd:pfam00652 121 NPNQQW 126
beta-trefoil_Ricin_GALNT6 cd23470
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
431-548 7.59e-16

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 6 (GALNT6) and similar proteins; GALNT6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 6, GalNAc-T6, pp-GaNTase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT6 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467348  Cd Length: 128  Bit Score: 74.13  E-value: 7.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLDnMGrkENEKVG----IFNCHGMGGNQVFSYTADKEIRTD---DLCLDVSRlnGPVIMLKCHH----- 498
Cdd:cd23470     5 GAIKNEGTNQCLD-VG--ENNRGGkpliMYSCHGMGGNQYFEYTTHKELRHNiakQLCLRVSK--GPVQLGECHYkgkns 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1775678398 499 -MRGNQLWEYDAERLtLRHVNSNQCLDEPSEEdkmvPTMQDCSGSRSQQ-WL 548
Cdd:cd23470    80 qVPPDEEWELTQDHL-IRNSGSNMCLTARGKH----PAMAPCNPADPHQlWS 126
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
115-312 1.10e-15

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 75.89  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 115 PNTSVVIVFHNEAwSTLLRTVYSVINRSphYLLSEVILVDDASERDFLKLtLENYVKNLEvPVKIIRMEERSGLIRARLR 194
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQT--YPDFEIIVVDDGSTDGTAEI-LRELAAKDP-RIRVIRLERNRGKGAARNA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 195 GAAASKGQVITFLDAHCECTLGWLEPLLARIKEDrktvvcpiidvisddtfeymaGSDMTYGGFNWKLNFRWYPVPQREM 274
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEG---------------------PADLVYGSRLIREGESDLRRLGSRL 135
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1775678398 275 DRRkgdRTLPVRTPTMAGGLFSIDRNYFEEIGtYDAGM 312
Cdd:COG0463   136 FNL---VRLLTNLPDSTSGFRLFRREVLEELG-FDEGF 169
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
431-547 1.34e-14

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: 70.86  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLDNMG--RKENEKVGIFNCHGmGGNQVFSYTADK----EIRT--DDLCLDV---SRLNG-PVIMLKCHH 498
Cdd:cd00161     3 YRIVNAASGKCLDVAGgsTANGAPVQQWTCNG-GANQQWTLTPVGdgyyTIRNvaSGKCLDVaggSTANGaNVQQWTCNG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1775678398 499 mRGNQLWEYDAERL---TLRHVNSNQCLD--EPSEEDKMVPTMQDCSGSRSQQW 547
Cdd:cd00161    82 -GDNQQWRLEPVGDgyyRIVNKHSGKCLDvsGGSTANGANVQQWTCNGGANQQW 134
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
115-383 1.60e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 72.33  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 115 PNTSVVIVFHNEaWSTLLRTVYSVINRSphYLLSEVILVDDASERDFLkltleNYVKNLEVP-VKIIRMEERSGLIRARL 193
Cdd:COG1216     3 PKVSVVIPTYNR-PELLRRCLESLLAQT--YPPFEVIVVDNGSTDGTA-----ELLAALAFPrVRVIRNPENLGFAAARN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 194 RGAAASKGQVITFLDAHCECTLGWLEPLLArikedrktvvcpiidvisddtfeymagsdmtyggfnwklnfrwypvpqre 273
Cdd:COG1216    75 LGLRAAGGDYLLFLDDDTVVEPDWLERLLA-------------------------------------------------- 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 274 mdrrkgdrtlpvrtptmAGGLFsIDRNYFEEIGTYDAGMDIWGGEnLEMSFRIWQCGGSLEIVTCSHVGHVFRKAtpyTF 353
Cdd:COG1216   105 -----------------AACLL-IRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGAS---SG 162
                         250       260       270
                  ....*....|....*....|....*....|
gi 1775678398 354 PGGTGHVINKNNRRLAEVWMDEFKDFFYII 383
Cdd:COG1216   163 PLLRAYYLGRNRLLFLRKHGPRPLLRLALL 192
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
418-547 9.68e-14

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 70.97  E-value: 9.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 418 YPDSQIPRR-YYSLGEIRnVETNQCLDNMGR-KENEKVGIFNCHGmGGNQVFSYTADKEIRTDDLCLDVSRLN----GPV 491
Cdd:NF035930  106 YPDYPGQGGgGWGGREIR-GKGGLCLDVSGGlRPGNGLIVYNCNG-GENQRFTWGRGGELRVGDLCLDVADGNtrdgARV 183
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 492 IMLKCHHMRgNQLWeyDAERLTLRHVNSNQCLDepSEEDKMVP----TMQDCSGSRSQQW 547
Cdd:NF035930  184 IAWSCSGGP-NQRW--RWRGGQIRSRLSGKCLD--IEGGRARPgqpvIVWSCNGGPNQRW 238
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
431-547 1.15e-13

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: 67.81  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNveTNQCLDNMGRK--ENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDV--SRLNGPVIMLKCHHmRGNQLWE 506
Cdd:cd23441     6 GQIKQ--GNLCLDSDEQLfqGPALLILAPCSNSSDSQEWSFTKDGQLQTQGLCLTVdsSSKDLPVVLETCSD-DPKQKWT 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1775678398 507 YdaERLTLRHVNSNQCLDEPSeedKMVPTMQDC-SGSRSQQW 547
Cdd:cd23441    83 R--TGRQLVHSESGLCLDSRK---KKGLVVSPCrSGAPSQKW 119
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
106-229 2.02e-13

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: 71.31  E-value: 2.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 106 KTKVYPDELPNTSVVIVFHNEAwSTLLRTVYSVIN-RSPHYLLsEVILVDDASERDFLKLtLENYvKNLEVPVKIIRMEE 184
Cdd:COG1215    20 RRRRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAqDYPKEKL-EVIVVDDGSTDETAEI-AREL-AAEYPRVRVIERPE 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1775678398 185 RSGLIRARLRGAAASKGQVITFLDAHCECTLGWLEPLLARIKEDR 229
Cdd:COG1215    96 NGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG 140
beta-trefoil_Ricin_GALNT4 cd23469
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
431-547 3.09e-11

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 4 (GALNT4) and similar proteins; GALNT4 (EC 2.4.1.41), also called polypeptide GalNAc transferase 4, GalNAc-T4, pp-GaNTase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT4 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467347  Cd Length: 136  Bit Score: 61.07  E-value: 3.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVE-TNQCLDNMGRKEN---EKVGIFNCHGMGGNQVFSYTADKEIRTD---DLCLDVSRLNGPVIMLKCHH----M 499
Cdd:cd23469     5 GAVRSMGiSSECLDYNSPEHNptgAHLSLFGCHGQGGNQFFEYTSNKEIRFNsvtELCAEVPDQKNYIGMKHCPKdgspV 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1775678398 500 RGNQLWEYdAERLTLRHVNSNQCLDE-PSEEDKMVPTMQDCS-GSRSQQW 547
Cdd:cd23469    85 PANIIWHF-KEDGTIYHPHSGMCISAyRTPEGRADVQMRTCDaGDKNQLW 133
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
438-550 8.22e-10

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


Pssm-ID: 467349  Cd Length: 140  Bit Score: 57.11  E-value: 8.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 438 TNQCLDNMGRKENEKVG----IFNCHGMGGNQVFSYTADKEIRTD----DLCLDVSRLNGPVIMLKC----HHMRGNQLW 505
Cdd:cd23471    13 TNYCFDYNPPDEHQIAGhqviLYQCHGMGQNQFFEYTSQNEIRYNtrqpEGCAAVDAGTDFLTMHLCrenrQAVPENQKF 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1775678398 506 EYDaERLTLRHVNSNQCLD--EPSEEDKMVPTMQDCSGSRSQQWLLR 550
Cdd:cd23471    93 IFR-EDGSLFHVQTQKCVQavRNESSGSPAPVLRPCTDSDHQKWFFK 138
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
433-547 3.18e-09

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: 55.13  E-value: 3.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 433 IRNVETNQCLDNmgrKENEKVGIFNCHGmGGNQVFSYTADKE-------IRTdDLCLDvSRLNGPVIMLKCHHMRgNQLW 505
Cdd:cd23415     5 LRNVATGRCLDS---NAGGNVYTGPCNG-GPYQRWTWSGVGDgtvtlrnAAT-GRCLD-SNGNGGVYTLPCNGGS-YQRW 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1775678398 506 E---YDAERLTLRHVNSNQCLDepSEEDKMVpTMQDCSGSRSQQW 547
Cdd:cd23415    78 RvtsTSGGGVTLRNVATGRCLD--SNGSGGV-YTRPCNGGSYQRW 119
beta-trefoil_Ricin_hemolysin cd23423
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ...
478-547 9.00e-09

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: 53.54  E-value: 9.00e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1775678398 478 DDLCLDVSRlNGPVIMLKCHHMRGNQLWEYDAE-RLTLRhVNSNQCLDepSEEDKMVpTMQDCSGSRSQQW 547
Cdd:cd23423    13 NNRCLTVDN-NGRVTLESCDSGDRNQSWILDSEgRYRSR-VAPDLCLD--ADDDGLL-TLEQCSLSLTQKW 78
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
479-556 2.57e-08

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: 52.76  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 479 DLCLDV---SRLNG-PVIMLKCHHmRGNQLWEYDAERL---TLRHVNSNQCLD--EPSEEDKMVPTMQDCSGSRSQQWLL 549
Cdd:cd00161    11 GKCLDVaggSTANGaPVQQWTCNG-GANQQWTLTPVGDgyyTIRNVASGKCLDvaGGSTANGANVQQWTCNGGDNQQWRL 89

                  ....*..
gi 1775678398 550 RNMTLGT 556
Cdd:cd00161    90 EPVGDGY 96
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
118-333 2.97e-08

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: 54.93  E-value: 2.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 118 SVVIVFHNEAwSTLLRTVYSVINRSPHYLLSEVILVDDASERDflklTLEnYVKNLEVPVKIIRMEERSGLIR--ARLRG 195
Cdd:cd02525     3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTDG----TRE-IVQEYAAKDPRIRLIDNPKRIQsaGLNIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 196 AAASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEY---MAGSDMTYGGfnwKLNFRwypVPQR 272
Cdd:cd02525    77 IRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKaiaVAQSSPLGSG---GSAYR---GGAV 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1775678398 273 EMdrrkgdrtlpVRTPTMAGGLFSIDRnyFEEIGTYDAGMDIwgGENLEMSFRIWQCGGSL 333
Cdd:cd02525   151 KI----------GYVDTVHHGAYRREV--FEKVGGFDESLVR--NEDAELNYRLRKAGYKI 197
beta-trefoil_Ricin_SCDase_rpt1 cd23499
first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
476-554 4.32e-08

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


Pssm-ID: 467377 [Multi-domain]  Cd Length: 131  Bit Score: 52.07  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 476 RTDDLCLDVS-RLNGP-----VIMLKCHHMRGNQLWEYDAERLTLRH-VNSNQCLDEPSEE-DKMVPTMQDCSGSRSQQW 547
Cdd:cd23499     8 RASGKCLDIPgNDNDVvnganVILWDCADKSADQRWIYDAASGMLRNkANPSYCLDNRGQAyNGGEVVLWQCEDSDNLRW 87

                  ....*..
gi 1775678398 548 LLRNMTL 554
Cdd:cd23499    88 TYDNGVL 94
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
119-318 6.72e-08

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: 53.45  E-value: 6.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 119 VVIVFHNEAwSTLLRTVYSVINRS-PHYLLsEVILVDDASERDFLKLtLENYVKNLEVPVKIIRMEER--SGLIRARLRG 195
Cdd:cd04192     1 VVIAARNEA-ENLPRLLQSLSALDyPKEKF-EVILVDDHSTDGTVQI-LEFAAAKPNFQLKILNNSRVsiSGKKNALTTA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 196 AAASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTF-------EYMAGSDMTYGGFNWKLnfrwyp 268
Cdd:cd04192    78 IKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFKGKSLlakfqrlDWLSLLGLIAGSFGLGK------ 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1775678398 269 vpqremdrrkgdrtlpvrtPTMAGGL-FSIDRNYFEEIGTYDAGMDIWGGE 318
Cdd:cd04192   152 -------------------PFMCNGAnMAYRKEAFFEVGGFEGNDHIASGD 183
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
119-312 2.42e-07

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: 51.07  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 119 VVIVFHNEAwSTLLRTVYSVinRSPHYLLSEVILVDDASERDFLKLtLENYVKNLEVPVKIIRMEERSGLIRARLRGAAA 198
Cdd:cd06423     1 IIVPAYNEE-AVIERTIESL--LALDYPKLEVIVVDDGSTDDTLEI-LEELAALYIRRVLVVRDKENGGKAGALNAGLRH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 199 SKGQVITFLDAHCECTLGWLEPLLARIKEDRKTV-VCPIIDVISDD--------TFEYMagsdmtyggfnwklnfRWYPV 269
Cdd:cd06423    77 AKGDIVVVLDADTILEPDALKRLVVPFFADPKVGaVQGRVRVRNGSenlltrlqAIEYL----------------SIFRL 140
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1775678398 270 PQREMDRRKGdrtlpvrTPTMAGGLFSIDRNYFEEIGTYDAGM 312
Cdd:cd06423   141 GRRAQSALGG-------VLVLSGAFGAFRREALREVGGWDEDT 176
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
431-547 4.29e-07

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14) and similar proteins; GALNT14 (EC 2.4.1.41), also called polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, protein-UDP acetylgalactosaminyltransferase 14, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, 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. 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. GALNT14 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: 467356  Cd Length: 140  Bit Score: 49.48  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRnvETNQCLDNMgRKENEKVGIFN---CHGMGG----NQVFSYTADKEIRTDDLCLDVSRL--NGPVIMLKCHHMRG 501
Cdd:cd23478    10 GVIR--QRQNCLESR-RVEGQELPNLSlspCIKSKGvpakSQEWAYTYNQQIRQQQLCLSVHTLfpGSPVVLVPCKEGDG 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1775678398 502 NQLWEYDAERltLRHVNSNQCLD-----EPSEEDKMVpTMQDC-SGSRSQQW 547
Cdd:cd23478    87 KQRWTKVGSH--IEHMASRFCLDtemfgDGTESSKEI-VINPCeSSAMSQRW 135
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
477-554 6.08e-07

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: 48.36  E-value: 6.08e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1775678398 477 TDDLCLDVSRLNGPVIMLKCHHMRGNQLWEYDAERlTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSR-SQQWLLRNMTL 554
Cdd:cd23385     9 DLGKCLAARSSSSKVSLSTCNPNSPNQQWKWTSGH-RLFNVGTGKCLGVSSSSPSSPLRLFECDSEDeLQKWKCSKDGL 86
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
479-547 6.13e-07

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


Pssm-ID: 467334 [Multi-domain]  Cd Length: 122  Bit Score: 48.51  E-value: 6.13e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1775678398 479 DLCLDVS---RLNGPVIMLKCHHmRGNQLWEYDAERLTLRHVNSNQCLD---EPSEEDKMVptMQDCSGSRSQQW 547
Cdd:cd23456    11 GLCLDVSggaTNGANVVVYDCNN-SNSQKWYYDATGRLHSKANPGKCLDaggENSNGANVV--LWACNDSANQRW 82
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
432-547 1.26e-06

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467336 [Multi-domain]  Cd Length: 135  Bit Score: 47.70  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 432 EIRNVETNQCLDNMGRKENEKVGI--FNCHGmGGNQVFSYTADK----EIRT--DDLCLDV---SRLNGPVIML-KCHHM 499
Cdd:cd23458     4 RIRNRNSGKCIDVAGGSTANGANIqqWDCGS-GSNQQWTLVEIDngyyRIKAshSGKCLDVaggSTANGANIQQwDCVGG 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1775678398 500 rGNQLWEY-DAE----RLTLRHvnSNQCLD--EPSEEDKMVPTMQDCSGSRSQQW 547
Cdd:cd23458    83 -ANQQWKLqDLGngyfELKARH--SGKCLDvaGGSTANGASIQQWTCNGNDNQRF 134
beta-trefoil_Ricin_SCDase_rpt2 cd23500
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
432-547 1.64e-06

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


Pssm-ID: 467378 [Multi-domain]  Cd Length: 128  Bit Score: 47.46  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 432 EIRNVETNQCLD--NMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTD---DLCLDVSRLN----GPVIMLKCHHMRGN 502
Cdd:cd23500     4 TYRSKRSGKCLSaaNGSQLNGSLVQLDACHASAGQLWYFDPKKGTIRSAldgNKCLAIPGGNtgnhTQLQLADCDASNPA 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1775678398 503 QLWEYDAERLTLRhVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQW 547
Cdd:cd23500    84 QQFNYDGGVFRSR-LNSNQVIDASGGSDGSELILYDYHGGSNQRW 127
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
119-237 2.91e-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: 47.55  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 119 VVIVFHNeAWSTLLRTVYSVINRSPHYLlsEVILVDDASERDflkltLENYVKNLEVPVKIIRMEERSGLIRARLRGAAA 198
Cdd:cd04186     1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVDNASTDG-----SVELLRELFPEVRLIRNGENLGFGAGNNQGIRE 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1775678398 199 SKGQVITFLDAHCECTLGWLEPLLARIKEDRKT-VVCPII 237
Cdd:cd04186    73 AKGDYVLLLNPDTVVEPGALLELLDAAEQDPDVgIVGPKV 112
beta-trefoil_Ricin_CELIII-like_rpt2 cd23420
second ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2 ...
431-524 3.05e-06

second ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2+-dependent hemolytic lectin CEL-III and similar proteins; CEL-III is a Ca2+-dependent and galactose-specific lectin that exhibits hemolytic and hemagglutinating activities. It functions as an oligomer that forms an ion-permeable pore in the cell membrane. CEL-III consists of three domains: two N-terminal ricin B-type lectin domains, and a C-terminal pore-forming domain. The ricin B-type lectin domains show a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. The model corresponds to the second ricin B-type lectin domain.


Pssm-ID: 467299 [Multi-domain]  Cd Length: 133  Bit Score: 46.77  E-value: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVETNQCLDNMGRKENEKVGIFNCHGmGGNQVFSYTADKEIRTDD--LCLDVSRLNGP--VIMLKCHHMRgNQLWE 506
Cdd:cd23420     6 GRLRNEKSDLCLDVEGSDGKGNVLMYSCED-NLDQWFRYYENGEIVNAKsrMCLDVSGSDGSgnVGIYRCEDLR-DQMWS 83
                          90       100
                  ....*....|....*....|...
gi 1775678398 507 Y-----DAERLTLRHVNSNQCLD 524
Cdd:cd23420    84 RpnqycNGDYCSFLNKESNKCLD 106
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
479-556 3.54e-06

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: 46.27  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 479 DLCLDVSRlNGPVIMLKCHHmRGNQLWEYDAER---LTLRHVNSNQCLDEpseEDKMVPTMQDCSGSRSQQWLLRNMTLG 555
Cdd:cd23415    11 GRCLDSNA-GGNVYTGPCNG-GPYQRWTWSGVGdgtVTLRNAATGRCLDS---NGNGGVYTLPCNGGSYQRWRVTSTSGG 85

                  .
gi 1775678398 556 T 556
Cdd:cd23415    86 G 86
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
115-208 5.49e-06

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: 47.20  E-value: 5.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 115 PNTSVVIVFHNEAWSTLLRTVYSVINRS-PHYllsEVILVDDASERDFLKLTLENYVKNlEVPVKIIRMEERSGLIRARL 193
Cdd:cd04184     1 PLISIVMPVYNTPEKYLREAIESVRAQTyPNW---ELCIADDASTDPEVKRVLKKYAAQ-DPRIKVVFREENGGISAATN 76
                          90
                  ....*....|....*
gi 1775678398 194 RGAAASKGQVITFLD 208
Cdd:cd04184    77 SALELATGEFVALLD 91
beta-trefoil_Ricin_hemolysin cd23423
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ...
439-524 1.53e-05

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: 44.29  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 439 NQCLDNmgrKENEKVGIFNCHGMGGNQVFSYTADKEIRT---DDLCLDVSRlNGPVIMLKCHHMRgNQLWEYDAERLTLR 515
Cdd:cd23423    14 NRCLTV---DNNGRVTLESCDSGDRNQSWILDSEGRYRSrvaPDLCLDADD-DGLLTLEQCSLSL-TQKWEWEGDRLKNR 88

                  ....*....
gi 1775678398 516 HVNSNQCLD 524
Cdd:cd23423    89 YLDTGWVLT 97
beta-trefoil_Ricin_SCDase_rpt1 cd23499
first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
432-550 1.57e-05

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


Pssm-ID: 467377 [Multi-domain]  Cd Length: 131  Bit Score: 44.75  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 432 EIRNVETNQCLDNMGRKEN----EKVGIFNCHGMGGNQVFSYTADKEIRTD----DLCLDvSR----LNGPVIMLKCHHm 499
Cdd:cd23499     4 RIVNRASGKCLDIPGNDNDvvngANVILWDCADKSADQRWIYDAASGMLRNkanpSYCLD-NRgqayNGGEVVLWQCED- 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1775678398 500 RGNQLWEYDAERLTLRHvNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLR 550
Cdd:cd23499    82 SDNLRWTYDNGVLRSKH-NPNIVLDAYGRDNNSQVGQWEYHGGANQQWELR 131
beta-trefoil_Ricin_GALNT9 cd23473
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
431-551 2.23e-05

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: 44.57  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRNVE-TNQCLDNmGRKENEKVGIFNCHGMgGNQVFSYTADKEIR----------TDDLCL-DVSRLNGPVIMlKCHH 498
Cdd:cd23473    11 GEVRNSKaSGYCLDQ-GSEEDDKAILYPCHGM-SSQLVRYSTEGLLQlgplgstaflPDTKCLvDDGRGRTPTLK-KCED 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1775678398 499 M-RGNQ-LWEYdAERLTLRHVNSNQCLDEPSEEDK---MVPTMQDCSGsrsQQWLLRN 551
Cdd:cd23473    88 VaRPAQrLWDF-TQNGPIISRDTGRCLEVEMSKDAnfgLRLVVQRCSG---QKWMIRN 141
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
439-547 5.08e-05

ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine protease I (RPI) and similar proteins; RPI, also called serine protease 1, is a major serine protease exhibiting lytic activity toward living yeast cells. It has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI. RPI contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467330 [Multi-domain]  Cd Length: 125  Bit Score: 42.89  E-value: 5.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 439 NQCLDNMGRKENE--KVGIFNCHGMGGnQVFSYTADKEIRTDDLCLDV---SRLNGPVIMLKCHHMRGNQLWEYDAERlT 513
Cdd:cd23452    11 NKCIDVPNSSTTDgaPLQLWDCNGTNA-QKWTFASDGTLRALGKCLDVawgGTDNGTAVQLWTCSGNPAQQFVLSGAG-D 88
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1775678398 514 LRHVNSNQCLDEPSEEDKMVPTMQ--DCSGSRSQQW 547
Cdd:cd23452    89 LVNPQANKCVDVSGGNSGNGTRLQlwECSGNANQKW 124
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
119-209 9.38e-05

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: 43.33  E-value: 9.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 119 VVIVFHNEAwSTLLRTVYSVINRSPHYLLSEVILVDDASERDFLKLtLENYVKNLEVpVKIIRMEERSGLIRARLRGAAA 198
Cdd:cd04179     1 VVIPAYNEE-ENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEI-ARELAARVPR-VRVIRLSRNFGKGAAVRAGFKA 77
                          90
                  ....*....|.
gi 1775678398 199 SKGQVITFLDA 209
Cdd:cd04179    78 ARGDIVVTMDA 88
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
119-234 1.50e-04

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: 43.32  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 119 VVIVFHNEAwSTLLRTV-----YSVINRSPHYllsEVILVDDASERDFLKLtLENYVKNLEVPVKIIRMEERSGLIRARL 193
Cdd:cd04188     1 VVIPAYNEE-KRLPPTLeeaveYLEERPSFSY---EIIVVDDGSKDGTAEV-ARKLARKNPALIRVLTLPKNRGKGGAVR 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1775678398 194 RGAAASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVC 234
Cdd:cd04188    76 AGMLAARGDYILFADADLATPFEELEKLEEALKTSGYDIAI 116
beta-trefoil_Ricin_unchar cd23412
ricin B-type lectin domain, beta-trefoil fold, found in uncharacterized macrophage mannose ...
481-547 2.33e-04

ricin B-type lectin domain, beta-trefoil fold, found in uncharacterized macrophage mannose receptor (MRC)-like proteins; The subfamily corresponds to a group of uncharacterized ricin B-type lectin beta-trefoil domain-containing proteins from Gnathostomata. They show high sequence similarity with macrophage mannose receptor (MRC) family proteins.


Pssm-ID: 467790  Cd Length: 127  Bit Score: 41.23  E-value: 2.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1775678398 481 CLDVS-RLNGPVIMLKCHHMRGNQLWEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQW 547
Cdd:cd23412    15 CIQVDhGESERVSLAECKPHSEHQQWSWDPETRALSSLHTGECLTVLKIQEFGSVRLEPCGSREPQAW 82
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
149-326 4.42e-04

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 42.26  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 149 EVILVDDASERDFL-------KLTLENYVKNLEvpvkiirmEERSGLIRARLRGAAASKGQVITFLDAHCECTLGWLEPL 221
Cdd:pfam10111  31 ELIIINDGSTDKTLeevssikDHNLQVYYPNAP--------DTTYSLAASRNRGTSHAIGEYISFIDGDCLWSPDKFEKQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 222 L--ARIKEDRKT----VVCPIIDVISDDTFEYMAGSDMTyggfnWKLNFRwypvpqremdrrkgdRTLPVRTPTMA---- 291
Cdd:pfam10111 103 LkiATSLALQENiqaaVVLPVTDLNDESSNFLRRGGDLT-----ASGDVL---------------RDLLVFYSPLAiffa 162
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1775678398 292 --GGLFSIDRNYFEEIGTYDAGMDIWGGENLEMSFRI 326
Cdd:pfam10111 163 pnSSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRL 199
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
288-338 6.82e-04

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


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 38.36  E-value: 6.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1775678398 288 PTMAGGLFSIDRNYFEEIGTYDAGMDIWGGENLEMSFRIWQCGGSLEIVTC 338
Cdd:pfam02709  17 KTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG 67
beta-trefoil_Ricin_GALNT8-like cd23438
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
431-551 9.11e-04

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: 39.72  E-value: 9.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 431 GEIRN-VETNQCLDNmGRKENEKVGIFNCHGMgGNQVFSYTADKEI---------RTDDLCL-DVSRLNGPViMLKCHHM 499
Cdd:cd23438     6 GEMRNsLVTDLCLDQ-GPKENHTAILYPCHGW-SPQLVRYTKDGQLylgqlgstaSPDTRCLvDDGKSDKPQ-LLDCSKV 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1775678398 500 --RGNQLWEYdAERLTLRHVNSNQCLDepSEEDKMVP----TMQDCSGsrsQQWLLRN 551
Cdd:cd23438    83 knRLQKYWDF-SQGGAIQNRATGRCLE--VEEDKLNFghrlVLQTCSG---QKWNIKN 134
beta-trefoil_Ricin_RIPs_II_rpt2 cd23444
second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ...
478-551 9.78e-04

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


Pssm-ID: 467322 [Multi-domain]  Cd Length: 122  Bit Score: 39.18  E-value: 9.78e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1775678398 478 DDLCLDVSRlNGPVIMLKCHHMRGNQLWEYDAERlTLR-HVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRN 551
Cdd:cd23444    10 NDLCLQANG-GNNVWLEECVSNKKEQKWALYPDG-TIRpNQNRNLCLTSSSDVQGSIIVVLSCSGSSGQRWVFRN 82
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
433-547 1.15e-03

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: 39.12  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775678398 433 IRNVETNQCLDNmgRKENEKVGIFNCHGMGGNQVFSYTADKEIR--TDDLCLDVS--RLNGPVIMLKCHHMRGNQLWEYD 508
Cdd:cd23385     5 IYNEDLGKCLAA--RSSSSKVSLSTCNPNSPNQQWKWTSGHRLFnvGTGKCLGVSssSPSSPLRLFECDSEDELQKWKCS 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1775678398 509 AERLTLRHVNSNQCLDEPSEEDKMVPTMQDCsgsrSQQW 547
Cdd:cd23385    83 KDGLLLLKGLGLLLLYDKSGKNVVVSKGSGL----SSRW 117
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
502-556 3.61e-03

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 36.97  E-value: 3.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1775678398 502 NQLWEYDAERL----TLRHVNSNQCLDEP--SEEDKMVPTMQDCSGSRSQQWLLRNMTLGT 556
Cdd:pfam14200   2 NQQWRFGGTVGdgyyTIVNVASGKYLDVAggSTANGANVQQWTDNGNDNQQWRIVDAGDGY 62
 
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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