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Conserved domains on  [gi|153792095|ref|NP_071370|]
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polypeptide N-acetylgalactosaminyltransferase 11 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 ...
154-452 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: 525.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 154 SVVICFYNEAFSALLRTVHSVIDRTPAHLLHEIILVDDDSDFDDLKGELDEYVQKYLPgKIKVIRNTKREGLIRGRMIGA 233
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLP-KVKVLRLKKREGLIRARIAGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 234 AHATGEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVVCPVIDIISADTLAYS-SSPVVRGGFNWGLHFKWDLVPLSELgR 312
Cdd:cd02510   80 RAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRgSSGDARGGFDWSLHFKWLPLPEEER-R 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 313 AEGATAPIKSPTMAGGLFAMNRQYFHELGQYDSGMDIWGGENLEISFRIWMCGGKLFIIPCSRVGHIFR-KRRPYGSPEG 391
Cdd:cd02510  159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792095 392 QDTMTHNSLRLAHVWLDEYKEQYFSLRPDLKTKSYGNISERVELRKKLGCKSFKWYLDNVY 452
Cdd:cd02510  239 SGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
478-606 1.12e-63

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: 205.30  E-value: 1.12e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 478 KVLQRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSLLCLDMSETRsSDPPRLMKCHGSG 557
Cdd:cd23440    1 KVIRKGQLKHAGSGLCLVAEDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLLCLDSSETS-SDFPRLMKCHGSG 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 153792095 558 GSQQWTFGKNNRLYQVSVGQCLRAVDPlGQKGSVAMAICDGSSSQQWHL 606
Cdd:cd23440   80 GSQQWRFKKDNRLYNPASGQCLAASKN-GTSGYVTMDICSDSPSQKWVF 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 ...
154-452 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: 525.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 154 SVVICFYNEAFSALLRTVHSVIDRTPAHLLHEIILVDDDSDFDDLKGELDEYVQKYLPgKIKVIRNTKREGLIRGRMIGA 233
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLP-KVKVLRLKKREGLIRARIAGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 234 AHATGEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVVCPVIDIISADTLAYS-SSPVVRGGFNWGLHFKWDLVPLSELgR 312
Cdd:cd02510   80 RAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRgSSGDARGGFDWSLHFKWLPLPEEER-R 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 313 AEGATAPIKSPTMAGGLFAMNRQYFHELGQYDSGMDIWGGENLEISFRIWMCGGKLFIIPCSRVGHIFR-KRRPYGSPEG 391
Cdd:cd02510  159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792095 392 QDTMTHNSLRLAHVWLDEYKEQYFSLRPDLKTKSYGNISERVELRKKLGCKSFKWYLDNVY 452
Cdd:cd02510  239 SGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
478-606 1.12e-63

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: 205.30  E-value: 1.12e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 478 KVLQRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSLLCLDMSETRsSDPPRLMKCHGSG 557
Cdd:cd23440    1 KVIRKGQLKHAGSGLCLVAEDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLLCLDSSETS-SDFPRLMKCHGSG 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 153792095 558 GSQQWTFGKNNRLYQVSVGQCLRAVDPlGQKGSVAMAICDGSSSQQWHL 606
Cdd:cd23440   80 GSQQWRFKKDNRLYNPASGQCLAASKN-GTSGYVTMDICSDSPSQKWVF 127
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
154-335 1.19e-30

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: 117.50  E-value: 1.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095  154 SVVICFYNEAfSALLRTVHSVIDRTpaHLLHEIILVDDDSDFDdLKGELDEYVQKYlpGKIKVIRNTKREGLIRGRMIGA 233
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGSTDG-TVEIAEEYAKKD--PRVRVIRLPENRGKAGARNAGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095  234 AHATGEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVVCPVIDIISADTLAYssspvvrggfNWGLHFKWDLVPLSELGRA 313
Cdd:pfam00535  75 RAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY----------RRASRITLSRLPFFLGLRL 144
                         170       180
                  ....*....|....*....|..
gi 153792095  314 EGATAPIKSPTMAGGLFAMNRQ 335
Cdd:pfam00535 145 LGLNLPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
483-604 5.22e-28

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 108.77  E-value: 5.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095  483 GRLYHLQTNKCLVAQGRpSQKGGLVVLKACDYSDPNQIWIYNEEHEL-VLNSLLCLDMSETRSSDPPRLMKCHGSGGSQQ 561
Cdd:pfam00652   3 GRIRNRASGKCLDVPGG-SSAGGPVGLYPCHGSNGNQLWTLTGDGTIrSVASDLCLDVGSTADGAKVVLWPCHPGNGNQR 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 153792095  562 WTFGKNNR-LYQVSVGQCLRAVDPLGQKGSVAMAICD-GSSSQQW 604
Cdd:pfam00652  82 WRYDEDGTqIRNPQSGKCLDVSGAGTSNGKVILWTCDsGNPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
487-607 6.85e-25

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 99.89  E-value: 6.85e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095   487 HLQTNKCLVAQGRPSQkgglVVLKACDYSDPNQIWIYNEEHEL-VLNSLLCLDMSETRSSdPPRLMKCHGSGGSQQWTFG 565
Cdd:smart00458   3 SGNTGKCLDVNGNKNP----VGLFDCHGTGGNQLWKLTSDGAIrIKDTDLCLTANGNTGS-TVTLYSCDGTNDNQYWEVN 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 153792095   566 KNNRLYQVSVGQCLRAVDPLGQKgSVAMAICDGSSSQQWHLE 607
Cdd:smart00458  78 KDGTIRNPDSGKCLDVKDGNTGT-KVILWTCSGNPNQKWIFE 118
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
154-372 5.76e-16

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 77.05  E-value: 5.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 154 SVVICFYNEAfSALLRTVHSVIDRTPAHLlhEIILVdddsdfddlkgelD--------EYVQKYLPG--KIKVIRNTKRE 223
Cdd:COG0463    5 SVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVV-------------DdgstdgtaEILRELAAKdpRIRVIRLERNR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 224 GLIRGRMIGAAHATGEVLVFLDSHCEVNVMWLQPLLAAIREDRHtvvcpviDIISADTLAYSSSPVVRGGFNWGLHFKWD 303
Cdd:COG0463   69 GKGAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPA-------DLVYGSRLIREGESDLRRLGSRLFNLVRL 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792095 304 LVPLselgraegatapiksPTMAGGLFAMNRQYFHELGqYDSGMdiwgGENLEIsFRIWMCGGKLFIIP 372
Cdd:COG0463  142 LTNL---------------PDSTSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVP 189
 
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 ...
154-452 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: 525.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 154 SVVICFYNEAFSALLRTVHSVIDRTPAHLLHEIILVDDDSDFDDLKGELDEYVQKYLPgKIKVIRNTKREGLIRGRMIGA 233
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLP-KVKVLRLKKREGLIRARIAGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 234 AHATGEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVVCPVIDIISADTLAYS-SSPVVRGGFNWGLHFKWDLVPLSELgR 312
Cdd:cd02510   80 RAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRgSSGDARGGFDWSLHFKWLPLPEEER-R 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 313 AEGATAPIKSPTMAGGLFAMNRQYFHELGQYDSGMDIWGGENLEISFRIWMCGGKLFIIPCSRVGHIFR-KRRPYGSPEG 391
Cdd:cd02510  159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792095 392 QDTMTHNSLRLAHVWLDEYKEQYFSLRPDLKTKSYGNISERVELRKKLGCKSFKWYLDNVY 452
Cdd:cd02510  239 SGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
478-606 1.12e-63

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: 205.30  E-value: 1.12e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 478 KVLQRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSLLCLDMSETRsSDPPRLMKCHGSG 557
Cdd:cd23440    1 KVIRKGQLKHAGSGLCLVAEDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLLCLDSSETS-SDFPRLMKCHGSG 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 153792095 558 GSQQWTFGKNNRLYQVSVGQCLRAVDPlGQKGSVAMAICDGSSSQQWHL 606
Cdd:cd23440   80 GSQQWRFKKDNRLYNPASGQCLAASKN-GTSGYVTMDICSDSPSQKWVF 127
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
154-335 1.19e-30

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: 117.50  E-value: 1.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095  154 SVVICFYNEAfSALLRTVHSVIDRTpaHLLHEIILVDDDSDFDdLKGELDEYVQKYlpGKIKVIRNTKREGLIRGRMIGA 233
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGSTDG-TVEIAEEYAKKD--PRVRVIRLPENRGKAGARNAGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095  234 AHATGEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVVCPVIDIISADTLAYssspvvrggfNWGLHFKWDLVPLSELGRA 313
Cdd:pfam00535  75 RAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY----------RRASRITLSRLPFFLGLRL 144
                         170       180
                  ....*....|....*....|..
gi 153792095  314 EGATAPIKSPTMAGGLFAMNRQ 335
Cdd:pfam00535 145 LGLNLPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
483-604 5.22e-28

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 108.77  E-value: 5.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095  483 GRLYHLQTNKCLVAQGRpSQKGGLVVLKACDYSDPNQIWIYNEEHEL-VLNSLLCLDMSETRSSDPPRLMKCHGSGGSQQ 561
Cdd:pfam00652   3 GRIRNRASGKCLDVPGG-SSAGGPVGLYPCHGSNGNQLWTLTGDGTIrSVASDLCLDVGSTADGAKVVLWPCHPGNGNQR 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 153792095  562 WTFGKNNR-LYQVSVGQCLRAVDPLGQKGSVAMAICD-GSSSQQW 604
Cdd:pfam00652  82 WRYDEDGTqIRNPQSGKCLDVSGAGTSNGKVILWTCDsGNPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
487-607 6.85e-25

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 99.89  E-value: 6.85e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095   487 HLQTNKCLVAQGRPSQkgglVVLKACDYSDPNQIWIYNEEHEL-VLNSLLCLDMSETRSSdPPRLMKCHGSGGSQQWTFG 565
Cdd:smart00458   3 SGNTGKCLDVNGNKNP----VGLFDCHGTGGNQLWKLTSDGAIrIKDTDLCLTANGNTGS-TVTLYSCDGTNDNQYWEVN 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 153792095   566 KNNRLYQVSVGQCLRAVDPLGQKgSVAMAICDGSSSQQWHLE 607
Cdd:smart00458  78 KDGTIRNPDSGKCLDVKDGNTGT-KVILWTCSGNPNQKWIFE 118
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
478-607 1.08e-23

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: 96.67  E-value: 1.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 478 KVLQRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSlLCLDMSETrsSDPPRLMKCHGSG 557
Cdd:cd23462    1 EALAYGEIRNLAGKLCLDAPGRKKELNKPVGLYPCHGQGGNQYWMLTKDGEIRRDD-LCLDYAGG--SGDVTLYPCHGMK 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153792095 558 GSQQWTFGK-NNRLYQVSVGQCLRAVDPlgqKGSVAMAICDGSSS-QQWHLE 607
Cdd:cd23462   78 GNQFWIYDEeTKQIVHGTSKKCLELSDD---SSKLVMEPCNGSSPrQQWEFE 126
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
483-608 1.56e-19

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: 84.67  E-value: 1.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 483 GRLYHLQTNKCLVAQGRpsQKGGLVVLKACDYSDPNQIWIYNEEHELVlNSLLCLDMSetRSSDPPRLMKCHGSGGSQQW 562
Cdd:cd23433    7 GEIRNVETNLCLDTMGR--KAGEKVGLSSCHGQGGNQVFSYTAKGEIR-SDDLCLDAS--RKGGPVKLEKCHGMGGNQEW 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 153792095 563 TFGKN-NRLYQVSVGQCLRAVDPlGQKGSVAMAICDGSSSQQWHLEG 608
Cdd:cd23433   82 EYDKEtKQIRHVNSGLCLTAPNE-DDPNEPVLRPCDGGPSQKWELEG 127
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
483-604 2.35e-16

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: 75.56  E-value: 2.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 483 GRLYHLQTNKCLVAQGRPSQkGGLVVLKACDYSDPNQIWIYNEEHELVlNSLLCLDmseTRSSDPPRLMKCHGSGGSQQW 562
Cdd:cd23460    3 GQIKHTESGLCLDWAGESNG-DKTVALKPCHGGGGNQFWMYTGDGQIR-QDHLCLT---ADEGNKVTLRECADQLPSQEW 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 153792095 563 TF-GKNNRLYQVSVGQCLRAVDplgQKGSVAMAICDGSS-SQQW 604
Cdd:cd23460   78 SYdEKTGTIRHRSTGLCLTLDA---NNDVVILKECDSNSlWQKW 118
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
154-372 5.76e-16

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 77.05  E-value: 5.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 154 SVVICFYNEAfSALLRTVHSVIDRTPAHLlhEIILVdddsdfddlkgelD--------EYVQKYLPG--KIKVIRNTKRE 223
Cdd:COG0463    5 SVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVV-------------DdgstdgtaEILRELAAKdpRIRVIRLERNR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 224 GLIRGRMIGAAHATGEVLVFLDSHCEVNVMWLQPLLAAIREDRHtvvcpviDIISADTLAYSSSPVVRGGFNWGLHFKWD 303
Cdd:COG0463   69 GKGAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPA-------DLVYGSRLIREGESDLRRLGSRLFNLVRL 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792095 304 LVPLselgraegatapiksPTMAGGLFAMNRQYFHELGqYDSGMdiwgGENLEIsFRIWMCGGKLFIIP 372
Cdd:COG0463  142 LTNL---------------PDSTSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVP 189
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
151-418 1.58e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 75.41  E-value: 1.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 151 PAASVVICFYNEAfSALLRTVHSVIDRTPAHllHEIILVDDDSdfddlKGELDEYVQKYLPGKIKVIRNTKREGLIRGRM 230
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPP--FEVIVVDNGS-----TDGTAELLAALAFPRVRVIRNPENLGFAAARN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 231 IGAAHATGEVLVFLDSHCEVNVMWLQPLLAAiredrhtvvcpvidiisadtlayssspvvrggfnwglhfkwdlvplsel 310
Cdd:COG1216   75 LGLRAAGGDYLLFLDDDTVVEPDWLERLLAA------------------------------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 311 graegatapiksptmagGLFAMNRQYFHELGQYDSGMDIWGGEnLEISFRIWMCGGKLFIIPCSRVGHIFRKRRpyGSPE 390
Cdd:COG1216  106 -----------------ACLLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASS--GPLL 165
                        250       260
                 ....*....|....*....|....*...
gi 153792095 391 GQDTMTHNSLRLAHVWLDEYKEQYFSLR 418
Cdd:COG1216  166 RAYYLGRNRLLFLRKHGPRPLLRLALLR 193
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
491-604 4.13e-12

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: 63.52  E-value: 4.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 491 NKCLVAQGRPSQKGGLVVLKACDYSDpNQIWIYNEEHELVLNSLLCLDMS--ETRSSDPPRLMKCHGsGGSQQWTFGKNN 568
Cdd:cd23418   14 GRCLDVPGGSTTNGTRLILWDCHGGA-NQQFTFTSAGELRVGGDKCLDAAggGTTNGTPVVIWPCNG-GANQKWRFNSDG 91
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 153792095 569 RLYQVSVGQCLRAvdPLGQKGSVAMAI---CDGSSSQQW 604
Cdd:cd23418   92 TIRNVNSGLCLDV--AGGGTANGTRLIlwsCNGGSNQRW 128
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
481-604 6.81e-12

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: 63.16  E-value: 6.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 481 QRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDpNQIWIY----NEEHELV-LNSLLCLDMSETRSSD--PPRLMKC 553
Cdd:cd00161    1 GTYRIVNAASGKCLDVAGGSTANGAPVQQWTCNGGA-NQQWTLtpvgDGYYTIRnVASGKCLDVAGGSTANgaNVQQWTC 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153792095 554 HGsGGSQQWTF----GKNNRLYQVSVGQCLRAVDPLGQKGS-VAMAICDGSSSQQW 604
Cdd:cd00161   80 NG-GDNQQWRLepvgDGYYRIVNKHSGKCLDVSGGSTANGAnVQQWTCNGGANQQW 134
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
147-266 9.79e-12

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 66.30  E-value: 9.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 147 PPDLPAASVVICFYNEAfSALLRTVHSVIDRTPAHLLHEIILVDDDSdfddlKGELDEYVQKY--LPGKIKVIRNTKREG 224
Cdd:COG1215   25 PADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGS-----TDETAEIARELaaEYPRVRVIERPENGG 98
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 153792095 225 LIRGRMIGAAHATGEVLVFLDSHCEVNVMWLQPLLAAIREDR 266
Cdd:COG1215   99 KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG 140
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
483-605 1.72e-11

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: 61.69  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 483 GRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSL-LCLDMSETRSSdpprLMKCHGSGGSQQ 561
Cdd:cd23442    6 GQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSLqLCLDVRQEQVV----LQNCTKEKTSQK 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 153792095 562 WTFGKNNRLYQVSVGQCLRAVDPLGQKGsVAMAICDGSSSQQWH 605
Cdd:cd23442   82 WDFQETGRIVHILSGKCIEAVESENSKL-LFLSPCNGQRNQMWK 124
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
485-604 4.96e-11

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: 60.30  E-value: 4.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 485 LYHLQTNKCLVAQGRpsqkGGLVVLKACDYSDPNQIWIYNEEHELV-LNSLLCLDMSETRSSDPPRLMKCHGSGGSQQWT 563
Cdd:cd23385    5 IYNEDLGKCLAARSS----SSKVSLSTCNPNSPNQQWKWTSGHRLFnVGTGKCLGVSSSSPSSPLRLFECDSEDELQKWK 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 153792095 564 fGKNNRLYQVSVGQCLRAVDPLGQKGSVAmaiCDGSSSQQW 604
Cdd:cd23385   81 -CSKDGLLLLKGLGLLLLYDKSGKNVVVS---KGSGLSSRW 117
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
489-604 5.35e-11

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: 60.03  E-value: 5.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 489 QTNKCLVAQGRpsQKGGLVVLKACDYSDPNQIWIYNEEHeLVLNSLLCLDMSETRSSDPPRLMKCHGSGGSQQWTFGKNN 568
Cdd:cd23434    7 QGNLCLDTLGH--KAGGTVGLYPCHGTGGNQEWSFTKDG-QIKHDDLCLTVVDRAPGSLVTLQPCREDDSNQKWEQIENN 83
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 153792095 569 -RLYQVSVGQCLRAVDplGQKGSVAMAICDGSS-SQQW 604
Cdd:cd23434   84 sKLRHVGSNLCLDSRN--AKSGGLTVETCDPSSgSQQW 119
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
483-606 4.75e-10

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: 57.73  E-value: 4.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 483 GRLYHLQTNKCLVAQGRP-SQKGGLVvlkACDYSDPNQIWIYNEEHELVLNSLlCLDMSetRSSDPPRLMKCHGSGGSQQ 561
Cdd:cd23467    7 GEIRNVETNQCLDNMGRKeNEKVGIF---NCHGMGGNQVFSYTADKEIRTDDL-CLDVS--RLNGPVVMLKCHHMRGNQL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 153792095 562 WTFGKNN-RLYQVSVGQCLRavDPLGQKGSV-AMAICDGSSSQQWHL 606
Cdd:cd23467   81 WEYDAERlTLRHVNSNQCLD--EPSEEDKMVpTMKDCSGSRSQQWLL 125
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
483-605 7.69e-10

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


Pssm-ID: 467317 [Multi-domain]  Cd Length: 126  Bit Score: 56.97  E-value: 7.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 483 GRLYHLQTNKCLVAQGRPSQKGglVVLKAC--DYSDPNQIWIYNEEHELVL-NSLLCLDMSETRSSDPPRLMKCHGSGGS 559
Cdd:cd23439    3 GEIRNVGSGLCIDTKHGGENDE--VRLSKCvkDGGGGEQQFELTWHEDIRPkKRKVCFDVSSHTPGAPVILYACHGMKGN 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 153792095 560 QQWTFGKNNR-LYQVSVGQCLRAVDplgQKGSVAMAICDGSS-SQQWH 605
Cdd:cd23439   81 QLWKYRPNTKqLYHPVSGLCLDADP---GSGKVFMNHCDESSdTQKWT 125
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
483-604 8.20e-10

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: 56.96  E-value: 8.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 483 GRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSL--LCLdmsETRSSDPPRLMKCHGSG--- 557
Cdd:cd23435    5 GALRNKGSELCLDVNNPNGQGGKPVIMYGCHGLGGNQYFEYTSKGEIRHNIGkeLCL---HASGSDEVILQHCTSKGkdv 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 153792095 558 -GSQQWTFGKNNRLYQVSVGQCLRAVDPlgqkgSVAMAICDGSS-SQQW 604
Cdd:cd23435   82 pPEQKWLFTQDGTIRNPASGLCLHASGY-----KVLLRTCNPSDdSQKW 125
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
482-564 1.06e-09

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 3 (Pgant3) and similar proteins; Pgant3, also called pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant3 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers EA2 as a substrate and has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Pgant3 plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. It may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Together with Pgant35A, Pgant3 regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467338 [Multi-domain]  Cd Length: 121  Bit Score: 56.30  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 482 RGRLYHlqTNKCLVAQgrpsqKGGLVVLKACDYSDPNQIWIYNEEHELVLN--SLLCLDMSETRssDPPRLMKCHGSGGS 559
Cdd:cd23460   45 DGQIRQ--DHLCLTAD-----EGNKVTLRECADQLPSQEWSYDEKTGTIRHrsTGLCLTLDANN--DVVILKECDSNSLW 115

                 ....*
gi 153792095 560 QQWTF 564
Cdd:cd23460  116 QKWIF 120
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
487-604 1.84e-09

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: 55.87  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 487 HLQT-NKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVlNSLLCLDMSETRSSDPPRLMKChGSGGSQQWTFg 565
Cdd:cd23441    7 QIKQgNLCLDSDEQLFQGPALLILAPCSNSSDSQEWSFTKDGQLQ-TQGLCLTVDSSSKDLPVVLETC-SDDPKQKWTR- 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 153792095 566 KNNRLYQVSVGQCLravDPLGQKGsVAMAIC-DGSSSQQW 604
Cdd:cd23441   84 TGRQLVHSESGLCL---DSRKKKG-LVVSPCrSGAPSQKW 119
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
155-303 4.24e-09

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


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 55.59  E-value: 4.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 155 VVICFYNEAfSALLRTVHSVIDRTPAHLlhEIILVDDdsdfddlkGELD---EYVQKYL--PGKIKVIRNTKREGLIRGR 229
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDD--------GSTDgtlEILEEYAkkDPRVIRVINEENQGLAAAR 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792095 230 MIGAAHATGEVLVFLDSHCEVNVMWLQPLLAAIREDrhtvvcPVIDIISAD-TLAYSSSPVVRGGFNWGLHFKWD 303
Cdd:cd00761   70 NAGLKAARGEYILFLDADDLLLPDWLERLVAELLAD------PEADAVGGPgNLLFRRELLEEIGGFDEALLSGE 138
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
483-606 5.08e-09

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: 54.67  E-value: 5.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 483 GRLYHLQTNKCLVAQGRP-SQKGGLVvlkACDYSDPNQIWIYNEEHELVLNSLlCLDMSetRSSDPPRLMKCHGSGGSQQ 561
Cdd:cd23466    7 GEIRNVETNQCLDNMARKeNEKVGIF---NCHGMGGNQVFSYTANKEIRTDDL-CLDVS--KLNGPVMMLKCHHLKGNQL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 153792095 562 WTFGKNN-RLYQVSVGQCL-RAVDPLGQKGSvaMAICDGSSSQQWHL 606
Cdd:cd23466   81 WEYDPVKlTLLHVNSNQCLdKATEEDSQVPS--IRDCNGSRSQQWLL 125
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
491-604 6.12e-09

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: 54.33  E-value: 6.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 491 NKCLVAQGRPsqKGGLVVLKACDYSD----PNQIWIYNEEHELVL-NSLLCLDMSETRSsdppRLMKCHGSGGSQQWTFg 565
Cdd:cd23461   13 NLCLDILGRS--HGGPPVLAKCSSNKsmpgTFQNFSLTFHRQIKHgTSDDCLEVRGNNV----RLSRCHYQGGNQYWKY- 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 153792095 566 kNNRLYQVSVGQ----CLRAVDplgQKGSVAMAICDGSS-SQQW 604
Cdd:cd23461   86 -DYETHQLINGGqnnkCLEADV---ESLKITLSICDSDNvEQKW 125
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
147-340 7.52e-09

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 56.82  E-value: 7.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 147 PPDLPAASVVICFYNEAfsallrtvhSVIDRT---------PAHLLhEIILVdddsdfddLKGELD---EYVQKYLPGKI 214
Cdd:cd06439   25 PAYLPTVTIIIPAYNEE---------AVIEAKlenllaldyPRDRL-EIIVV--------SDGSTDgtaEIAREYADKGV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 215 KVIRNTKREGLIRGRMIGAAHATGEVLVFLDshceVNVMW----LQPLLAAIREDRHTVVCPVIDIISADTLAYSSspvv 290
Cdd:cd06439   87 KLLRFPERRGKAAALNRALALATGEIVVFTD----ANALLdpdaLRLLVRHFADPSVGAVSGELVIVDGGGSGSGE---- 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153792095 291 rggfnwGLHFKWDlvplSELGRAEGAtapIKSPTMA-GGLFAMNRQYFHEL 340
Cdd:cd06439  159 ------GLYWKYE----NWLKRAESR---LGSTVGAnGAIYAIRRELFRPL 196
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
522-605 9.08e-09

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: 53.76  E-value: 9.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 522 IYNEEHELvlnsllCLDMSEtrSSDPPRLMKCHGSGGSQQWTFGKNNRLYQVSVGQCLrAVDPLGQKGSVAMAICDGSS- 600
Cdd:cd23385    5 IYNEDLGK------CLAARS--SSSKVSLSTCNPNSPNQQWKWTSGHRLFNVGTGKCL-GVSSSSPSSPLRLFECDSEDe 75

                 ....*
gi 153792095 601 SQQWH 605
Cdd:cd23385   76 LQKWK 80
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
484-605 1.13e-08

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: 53.59  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 484 RLYHLQTNKCLVAQGrpsqkGGLVVLKACDySDPNQIWIY----NEEHELV-LNSLLCLDMSETRSsdpPRLMKChGSGG 558
Cdd:cd23415    4 RLRNVATGRCLDSNA-----GGNVYTGPCN-GGPYQRWTWsgvgDGTVTLRnAATGRCLDSNGNGG---VYTLPC-NGGS 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153792095 559 SQQWTF----GKNNRLYQVSVGQCLRAVDplgqKGSVAMAICDGSSSQQWH 605
Cdd:cd23415   74 YQRWRVtstsGGGVTLRNVATGRCLDSNG----SGGVYTRPCNGGSYQRWR 120
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
490-607 2.26e-08

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: 53.09  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 490 TNKCLVAQGRPSQKGGLVVLKAC-DYSDPNQIWIYNEEHELvLNSLLCLDMSETRSSdPPRLMKCHGS-GGSQQWTFGKN 567
Cdd:cd23459   15 TNLCLDTLQRDEDKGYNLGLYPCqGGLSSNQLFSLSKKGEL-RREESCADVQGTEES-KVILITCHGLeKFNQKWKHTKG 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 153792095 568 NRLYQVSVGQCLRAVdPLGQKGSVAMAICDGSSSQQWHLE 607
Cdd:cd23459   93 GQIVHLASGKCLDAE-GLKSGDDVTLAKCDGSLSQKWTFE 131
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
482-563 3.78e-08

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: 51.83  E-value: 3.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 482 RGRLYHLQTNKCLVAQGrpSQKGGLVVLKACDYSDPNQIWIYNeEHELVLNSLLCLDMSETRSSdpPRLMKCHGSGGSQQ 561
Cdd:cd23385   42 GHRLFNVGTGKCLGVSS--SSPSSPLRLFECDSEDELQKWKCS-KDGLLLLKGLGLLLLYDKSG--KNVVVSKGSGLSSR 116

                 ..
gi 153792095 562 WT 563
Cdd:cd23385  117 WK 118
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
490-604 8.69e-08

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: 51.18  E-value: 8.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 490 TNKCL-VAQGRPSQkGGLVVLKACDYSDpNQIWIYNEEHEL-VLNslLCLDMSETRSSD--PPRLMKCHGSGGsQQWTFG 565
Cdd:cd23451   10 AGKCLdVPGSSTAD-GNPVQIYTCNGTA-AQKWTLGTDGTLrVLG--KCLDVSGGGTANgtLVQLWDCNGTGA-QKWVPR 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 153792095 566 KNNRLYQVSVGQCLRAVDPLGQKGS-VAMAICDGSSSQQW 604
Cdd:cd23451   85 ADGTLYNPQSGKCLDAPGGSTTDGTqLQLYTCNGTAAQQW 124
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
154-378 1.75e-07

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: 52.62  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 154 SVVICFYNEA--FSALLRtvhSVIDRTPAHLLHEIILVDDdsdfddlkGELD---EYVQKY--LPGKIKVIRNTKReglI 226
Cdd:cd02525    3 SIIIPVRNEEkyIEELLE---SLLNQSYPKDLIEIIVVDG--------GSTDgtrEIVQEYaaKDPRIRLIDNPKR---I 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 227 R--GRMIGAAHATGEVLVFLDSHCEVNVMWLQPLLAAIREDrhtvvcpvidiiSADTLAYSSSPVVRGGFNWGLHFkwdl 304
Cdd:cd02525   69 QsaGLNIGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRT------------GADNVGGPMETIGESKFQKAIAV---- 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792095 305 VPLSELG-----RAEGATAPIKSPTMAGGlfAMNRQYFHELGQYDSGMDIwgGENLEISFRIWMCGGKLFIIPCSRVGH 378
Cdd:cd02525  133 AQSSPLGsggsaYRGGAVKIGYVDTVHHG--AYRREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYY 207
beta-trefoil_Ricin_SCDase_rpt2 cd23500
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
489-605 1.76e-07

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: 50.16  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 489 QTNKCLVAQGRPSQKGGLVVLKACDYSdPNQIWIYNEEHELV---LNSLLCLDMSETRSSD--PPRLMKCHGSGGSQQWT 563
Cdd:cd23500    9 RSGKCLSAANGSQLNGSLVQLDACHAS-AGQLWYFDPKKGTIrsaLDGNKCLAIPGGNTGNhtQLQLADCDASNPAQQFN 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 153792095 564 fgKNNRLYQvSVGQCLRAVDPLGQKGSVAMAICD--GSSSQQWH 605
Cdd:cd23500   88 --YDGGVFR-SRLNSNQVIDASGGSDGSELILYDyhGGSNQRWR 128
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
481-564 1.07e-06

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: 47.70  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 481 QRGRLYHLQTnkCLVAqgrPSQKGG-LVVLKACDYSDPNQIWIYNEEHELV--LNSLLCLDMSETRSSDPpRLMKCHGSG 557
Cdd:cd23434   41 KDGQIKHDDL--CLTV---VDRAPGsLVTLQPCREDDSNQKWEQIENNSKLrhVGSNLCLDSRNAKSGGL-TVETCDPSS 114

                 ....*..
gi 153792095 558 GSQQWTF 564
Cdd:cd23434  115 GSQQWKF 121
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
147-382 4.20e-06

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 48.14  E-value: 4.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095  147 PPDLpaaSVVICFYNEAfSALLRTVHSVIDRtpAHLLHEIILVDDDSDFDDLKgELDEYVQKYLPGKIKVIRNTKREGL- 225
Cdd:pfam13641   1 PPDV---SVVVPAFNED-SVLGRVLEAILAQ--PYPPVEVVVVVNPSDAETLD-VAEEIAARFPDVRLRVIRNARLLGPt 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095  226 --IRGRMIGAAHATGEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVV-CPVidiiSADTLAYSSSPVVRGGFnwGLHFKw 302
Cdd:pfam13641  74 gkSRGLNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVgTPV----FSLNRSTMLSALGALEF--ALRHL- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095  303 dlvplselgRAEGATAPIKSPTMAGGLFAMNRQYFHELGQYDSGMDIWggENLEISFRIWMCGGKLFIIPCSRVGHIFRK 382
Cdd:pfam13641 147 ---------RMMSLRLALGVLPLSGAGSAIRREVLKELGLFDPFFLLG--DDKSLGRRLRRHGWRVAYAPDAAVRTVFPT 215
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
535-604 4.55e-06

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467315 [Multi-domain]  Cd Length: 124  Bit Score: 46.13  E-value: 4.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792095 535 LCLDmseTRSSDPPRLMK---CHGSGGSQQWTFGKNNRLYQVSvgQCLravDPLGQKGSVAMAICDGSSSQQW 604
Cdd:cd23437   15 LCLD---TMGHQNGGPVGlypCHGMGGNQLFRLNEAGQLAVGE--QCL---TASGSGGKVKLRKCNLGETGKW 79
beta-trefoil_Ricin_GALNTL6 cd23477
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
545-607 6.34e-06

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


Pssm-ID: 467355  Cd Length: 148  Bit Score: 46.47  E-value: 6.34e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792095 545 SDPPRLMKCHGSGGSQQWTFGKNNRLYQVSVGQCLravDPLGQKGSVAMAICDGSS-SQQWHLE 607
Cdd:cd23477   77 NSPVTLYDCHGMKGNQLWSYRKDKTLFHPVSNSCM---DCNPADKKIFMNRCDPLSeTQQWIFE 137
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
155-378 7.46e-06

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 46.40  E-value: 7.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 155 VVICFYNEAfSALLRTVHSVIDRTPAHllHEIILVdddsdfddlkgelD--------EYVQKYLPgKIKVIRNTKREGLI 226
Cdd:cd04186    1 IIIVNYNSL-EYLKACLDSLLAQTYPD--FEVIVV-------------DnastdgsvELLRELFP-EVRLIRNGENLGFG 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 227 RGRMIGAAHATGEVLVFLDSHCEVNVMWLQPLLAAIREDRhtvvcpvidiisadtlayssspvvrggfNWGlhfkwdlvp 306
Cdd:cd04186   64 AGNNQGIREAKGDYVLLLNPDTVVEPGALLELLDAAEQDP----------------------------DVG--------- 106
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792095 307 lselgraegatapIKSPTMAGGLFAMNRQYFHELGQYDSGMDIWgGENLEISFRIWMCGGKLFIIPCSRVGH 378
Cdd:cd04186  107 -------------IVGPKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYH 164
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
519-604 1.55e-05

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: 44.36  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 519 QIWIYNEEHELvlnsllCLDMSETRSSDP-PRLMKCHGSGGSQQWTFGKNNRLYQvsVGQCLRAVdplgqKGSVAMAI-C 596
Cdd:cd23460    2 LGQIKHTESGL------CLDWAGESNGDKtVALKPCHGGGGNQFWMYTGDGQIRQ--DHLCLTAD-----EGNKVTLReC 68

                 ....*....
gi 153792095 597 DG-SSSQQW 604
Cdd:cd23460   69 ADqLPSQEW 77
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
535-605 2.64e-05

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: 43.93  E-value: 2.64e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792095 535 LCLDMSE--TRSSDPPRLMKCHGSGGSQQWTFGKNNRLYQVsvGQCLrAVDPLGQKGSVAMAICDGSSSQQWH 605
Cdd:cd23441   13 LCLDSDEqlFQGPALLILAPCSNSSDSQEWSFTKDGQLQTQ--GLCL-TVDSSSKDLPVVLETCSDDPKQKWT 82
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
535-608 3.68e-05

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


Pssm-ID: 467334 [Multi-domain]  Cd Length: 122  Bit Score: 43.50  E-value: 3.68e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792095 535 LCLDMSETRSSD-PPRLMKCHGSGgSQQWTFGKNNRL-YQVSVGQCLRAVDPLGQKGSVAMAICDGSSSQQWHLEG 608
Cdd:cd23456   12 LCLDVSGGATNGaNVVVYDCNNSN-SQKWYYDATGRLhSKANPGKCLDAGGENSNGANVVLWACNDSANQRWDFDG 86
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
535-606 4.50e-05

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: 43.49  E-value: 4.50e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792095 535 LCLDMSETRSSDPPRLM--KCHGsGGSQQWTFgKNNRLYQVSVGQCLRAVDPLGQKGS-VAMAICDGSSSQQWHL 606
Cdd:cd23418   15 RCLDVPGGSTTNGTRLIlwDCHG-GANQQFTF-TSAGELRVGGDKCLDAAGGGTTNGTpVVIWPCNGGANQKWRF 87
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
532-607 7.90e-05

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 42.74  E-value: 7.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 532 NSLLCLDMSETRSSD--PPRLMKCHGsGGSQQWTFGKNN----RLYQVSVGQCLRAVDPLGQKGS-VAMAICDGSSSQQW 604
Cdd:cd00161    9 ASGKCLDVAGGSTANgaPVQQWTCNG-GANQQWTLTPVGdgyyTIRNVASGKCLDVAGGSTANGAnVQQWTCNGGDNQQW 87

                 ...
gi 153792095 605 HLE 607
Cdd:cd00161   88 RLE 90
beta-trefoil_Ricin_hemolysin cd23423
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ...
491-562 1.01e-04

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: 41.98  E-value: 1.01e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792095 491 NKCLVAQGrpsqkGGLVVLKACDYSDPNQIWIYNEE--HELVLNSLLCLDMSETRSSdppRLMKCHGSgGSQQW 562
Cdd:cd23423   14 NRCLTVDN-----NGRVTLESCDSGDRNQSWILDSEgrYRSRVAPDLCLDADDDGLL---TLEQCSLS-LTQKW 78
beta-trefoil_Ricin_PTPRB-like cd23409
ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein ...
487-573 1.04e-04

ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e and similar proteins; PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, R-PTP-beta, vascular endothelial protein tyrosine phosphatase, or VE-PTP, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of 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, which requires the presence of plakoglobin. The subfamily corresponds to PTPRB isoform e, which contains an extra 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.


Pssm-ID: 467787  Cd Length: 117  Bit Score: 42.04  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 487 HLQTNKCLVAQGrpsqkggLVVLKACDYSDPNQIWIYNEEHELV-LNSLLCLDMSeTRSSDPPRLMKCHGSGGSQQWTFG 565
Cdd:cd23409    8 HVQKQQCLFGNK-------TVSVGKCNATSPNQQWQWTEDGKLLhVKSGQCLGIS-NSSAFHSRRAILLDCSQAPRWTCH 79

                 ....*...
gi 153792095 566 KNNRLYQV 573
Cdd:cd23409   80 ENEGLLEV 87
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
155-271 1.85e-04

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: 42.56  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 155 VVICFYNEAfsallRTVHSVIDRTPAHLL----HEIILVdddsdfddlkgelD------------EYVQKYlpGKIKVIR 218
Cdd:cd04179    1 VVIPAYNEE-----ENIPELVERLLAVLEegydYEIIVV-------------DdgstdgtaeiarELAARV--PRVRVIR 60
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153792095 219 NTKREGLIRGRMIGAAHATGEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVVC 271
Cdd:cd04179   61 LSRNFGKGAAVRAGFKAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVI 113
beta-trefoil_Ricin_SCDase_rpt1 cd23499
first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
484-606 2.33e-04

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: 41.28  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 484 RLYHLQTNKCLVAQGR---PSQkGGLVVLKACDYSDPNQIWIYNEEHELVLNSL---LCLDMSETRSSD-PPRLMKCHGS 556
Cdd:cd23499    4 RIVNRASGKCLDIPGNdndVVN-GANVILWDCADKSADQRWIYDAASGMLRNKAnpsYCLDNRGQAYNGgEVVLWQCEDS 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153792095 557 gGSQQWTFgKNNRLyqVSVGQCLRAVDPLG--QKGSVAMAICDGSSSQQWHL 606
Cdd:cd23499   83 -DNLRWTY-DNGVL--RSKHNPNIVLDAYGrdNNSQVGQWEYHGGANQQWEL 130
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
155-353 3.84e-04

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: 42.28  E-value: 3.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 155 VVICFYNEAFSaLLRTVHSVIDRTPAHLLHEIILV--------DDDSDFDDLKGELDEYV----QKYLPGKIKVIrnTKr 222
Cdd:cd04192    1 VVIAARNEAEN-LPRLLQSLSALDYPKEKFEVILVddhstdgtVQILEFAAAKPNFQLKIlnnsRVSISGKKNAL--TT- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 223 eglirgrmiGAAHATGEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVVC-PVIDIISADTLAYssspvvrggFNWglhFK 301
Cdd:cd04192   77 ---------AIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAgPVIYFKGKSLLAK---------FQR---LD 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153792095 302 WdlvpLSELGRAEGAtAPIKSPTMAGGL-FAMNRQYFHELGQYDSGMDIWGGE 353
Cdd:cd04192  136 W----LSLLGLIAGS-FGLGKPFMCNGAnMAYRKEAFFEVGGFEGNDHIASGD 183
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
483-525 4.01e-04

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467315 [Multi-domain]  Cd Length: 124  Bit Score: 40.36  E-value: 4.01e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 153792095 483 GRLYHLQTNKCLvaqgRPSQKGGLVVLKACDYSDPNQIWIYNE 525
Cdd:cd23437   86 GQIRHKGTGKCL----DLNEGTNKLILQPCDSSSPSQKWEFNE 124
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
535-607 4.79e-04

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


Pssm-ID: 467354  Cd Length: 150  Bit Score: 41.10  E-value: 4.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792095 535 LCLDMSETRSsdPPRLMKCHGSGGSQQWTFGKNNRLYQVSVGQCLravDPLGQKGSVAMAICDGSS-SQQWHLE 607
Cdd:cd23476   69 FCFDAISHNS--PVTLYDCHGMKGNQLWRYRKDKTLYHPVSNSCM---DCSESDHRIFMNTCNPSSpTQQWLFE 137
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
322-380 4.82e-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: 39.13  E-value: 4.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 153792095  322 SPTMAGGLFAMNRQYFHELGQYDSGMDIWGGENLEISFRIWMCGGKLFiIPCSRVGHIF 380
Cdd:pfam02709  16 YKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIE-RPPGDIGRYY 73
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
481-523 6.07e-04

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: 40.01  E-value: 6.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 153792095 481 QRGRLYHLQTNKCLVAqgrpsqKGGLVVLKACDYSDPNQIWIY 523
Cdd:cd23435   91 QDGTIRNPASGLCLHA------SGYKVLLRTCNPSDDSQKWTF 127
beta-trefoil_Ricin_EW29-like cd23449
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ...
489-607 6.37e-04

ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa galactose-binding lectin (EW29) and similar proteins; EW29 is a galactose-binding lectin from the earthworm Lumbricus terrestris. It contains two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The second ricin B-type lectin domain may harbor two sugar-binding pockets in subdomains alpha and gamma. EW29 uses these two sugar-binding sites for its function as a single domain-type hemagglutinin.


Pssm-ID: 467327 [Multi-domain]  Cd Length: 128  Bit Score: 39.97  E-value: 6.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 489 QTNKCLVAQGRPSQKGGLVVLKACDYSDP-NQIWIYNEEHELV---LNSLlCLDMSETRSSdppRLMKCHGSGGSQQWTF 564
Cdd:cd23449    9 LNGKVLDVEGANAKPGAKVIMWEKKGGAEdNQLWYEDEVTGTIrskLNDF-CLDASGDKGL---ILNPYDPSNPKQQWKI 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 153792095 565 GKNNRLYQVSVGQCLRAVDPLGQKGSVAMAI-CDGSSSQQWHLE 607
Cdd:cd23449   85 SGNKIQNRSNPDNVLDIKGGSKDDGARLCAWeYNGGPNQLWDFE 128
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
483-522 6.47e-04

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 39.80  E-value: 6.47e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 153792095   483 GRLYHLQTNKCLVAQGrpSQKGGLVVLKACDYSdPNQIWI 522
Cdd:smart00458  80 GTIRNPDSGKCLDVKD--GNTGTKVILWTCSGN-PNQKWI 116
beta-trefoil_Ricin_LY75 cd23411
ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and ...
527-604 6.70e-04

ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and similar proteins; Ly-75, also called C-type lectin domain family 13 member B, DEC-205, gp200-MR6, or CD205, 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. Ly-75 contains 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.


Pssm-ID: 467789  Cd Length: 116  Bit Score: 39.72  E-value: 6.70e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792095 527 HElvlNSLLCLDMSETRSSdpprLMKCHGSGGSQQWTFGKNNRLYQVSVGQCLrAVDPLGQKGSVAMAICDGSSSQQW 604
Cdd:cd23411    9 HE---NSGKCLKVENSQIS----AVDCKQSSESLQWKWVSEHRLFNLGSKQCL-GLDITKPSNTLKMFECDSKSVMLW 78
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
481-521 7.28e-04

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 39.82  E-value: 7.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 153792095  481 QRGRLYHLQTNKCLVAQGRPSQKGGlVVLKACDYSDPNQIW 521
Cdd:pfam00652  87 DGTQIRNPQSGKCLDVSGAGTSNGK-VILWTCDSGNPNQQW 126
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
154-262 7.41e-04

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 41.47  E-value: 7.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 154 SVVICFYNEAFSALLRTVHSVIDRTPAhllhEIILVDDdsdfddlkGELDEYVQK----YLPGKIKVI---RNTKREGLI 226
Cdd:cd06434    3 TVIIPVYDEDPDVFRECLRSILRQKPL----EIIVVTD--------GDDEPYLSIlsqtVKYGGIFVItvpHPGKRRALA 70
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 153792095 227 RGrmigAAHATGEVLVFLDSHcevnVMWLQPLLAAI 262
Cdd:cd06434   71 EG----IRHVTTDIVVLLDSD----TVWPPNALPEM 98
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
491-604 1.34e-03

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: 39.04  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095 491 NKCLVAQGRPSQKGGLVVLKACDYSDPnQIWIYNEEHELVLNSLlCLDMSETRSSDPP--RLMKCHGSGgSQQWTFGKNN 568
Cdd:cd23452   11 NKCIDVPNSSTTDGAPLQLWDCNGTNA-QKWTFASDGTLRALGK-CLDVAWGGTDNGTavQLWTCSGNP-AQQFVLSGAG 87
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 153792095 569 RLYQVSVGQCLRAVD-PLGQKGSVAMAICDGSSSQQW 604
Cdd:cd23452   88 DLVNPQANKCVDVSGgNSGNGTRLQLWECSGNANQKW 124
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
536-608 1.35e-03

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: 39.04  E-value: 1.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792095 536 CLDMSETRSSDPPRLM--KCHGSGgSQQWTFGKNNRLYqvSVGQCLRAVDPLGQKGS-VAMAICDGSSSQQWHLEG 608
Cdd:cd23452   13 CIDVPNSSTTDGAPLQlwDCNGTN-AQKWTFASDGTLR--ALGKCLDVAWGGTDNGTaVQLWTCSGNPAQQFVLSG 85
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
221-361 1.67e-03

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: 40.72  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792095  221 KREGLIRGRMIGAAHATGEVLVFLDSHCEVNVMWLQPLLA-----AIREDRHT-VVCPVIDIISADTlayssSPVVRGGF 294
Cdd:pfam10111  65 TTYSLAASRNRGTSHAIGEYISFIDGDCLWSPDKFEKQLKiatslALQENIQAaVVLPVTDLNDESS-----NFLRRGGD 139
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792095  295 nwglhFKWDLVPLSELGRAEGATAPIKSPTmaGGLFAMNRQYFHELGQYDSGMDIWGGENLEISFRI 361
Cdd:pfam10111 140 -----LTASGDVLRDLLVFYSPLAIFFAPN--SSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRL 199
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
481-524 2.00e-03

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: 38.58  E-value: 2.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 153792095 481 QRGRLYHLQTNKCLvaqgRPSQKGGLVVLKACDYSDPNQIWIYN 524
Cdd:cd23460   82 KTGTIRHRSTGLCL----TLDANNDVVILKECDSNSLWQKWIFQ 121
beta-trefoil_Ricin_LY75 cd23411
ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and ...
487-553 2.52e-03

ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and similar proteins; Ly-75, also called C-type lectin domain family 13 member B, DEC-205, gp200-MR6, or CD205, 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. Ly-75 contains 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.


Pssm-ID: 467789  Cd Length: 116  Bit Score: 38.18  E-value: 2.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792095 487 HLQTNKCLVAqgrpsqKGGLVVLKACDYSDPNQIWIYNEEHELV-LNSLLCLDMSETRSSDPPRLMKC 553
Cdd:cd23411    9 HENSGKCLKV------ENSQISAVDCKQSSESLQWKWVSEHRLFnLGSKQCLGLDITKPSNTLKMFEC 70
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
489-563 3.94e-03

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: 37.93  E-value: 3.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792095 489 QTNKCLVAQGRPSQKGGLVVLKAC----DYSDPNQIWIYNEEHElVLNSLLCLDMSETRSSDPPRLMKCHGSGGSQQWT 563
Cdd:cd23478   14 QRQNCLESRRVEGQELPNLSLSPCikskGVPAKSQEWAYTYNQQ-IRQQQLCLSVHTLFPGSPVVLVPCKEGDGKQRWT 91
beta-trefoil_Ricin_hemolysin cd23423
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ...
552-604 4.88e-03

ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar proteins; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cytolysis by forming heptameric pores in target host membranes. After binding to target membranes, the protein assembles into a heptameric pre-pore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation. Hemolysin may be called "cytolysin" or "cytolytic toxin", according to a specific action for certain cells. For example, this subfamily includes Vibrio vulnificus cytolysin that attack blood cell membranes and cause cell rupture, thereby liberating hemoglobins. Members of this subfamily contain a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a putative sugar-binding pocket.


Pssm-ID: 467301 [Multi-domain]  Cd Length: 119  Bit Score: 37.36  E-value: 4.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153792095 552 KCHGSGGSQQWTFGKNNRLyqVSV---GQCLRAVDPlgqkGSVAMAICDGSSSQQW 604
Cdd:cd23423   29 SCDSGDRNQSWILDSEGRY--RSRvapDLCLDADDD----GLLTLEQCSLSLTQKW 78
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
493-565 5.24e-03

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: 37.27  E-value: 5.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792095 493 CLVAQGRPSQkgglVVLKACDySDPNQIWIYNEEHEL--VLNSLLCLDMSETRSsdPPRLMKCHGSGGSQQWTFG 565
Cdd:cd23437   56 CLTASGSGGK----VKLRKCN-LGETGKWEYDEATGQirHKGTGKCLDLNEGTN--KLILQPCDSSSPSQKWEFN 123
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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