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Conserved domains on  [gi|1701944547|ref|NP_001358404|]
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polypeptide N-acetylgalactosaminyltransferase 11 isoform 8 [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 ...
154-410 4.22e-163

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: 465.91  E-value: 4.22e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 154 SVVICFYNEAFSALLRTVHSVIDRTPAHLLHEIILVDDDSDF-------------------------------------- 195
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKpelkllleeyykkylpkvkvlrlkkreglirariagar 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 196 ---GEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVVCPVIDIISADTLAYS-SSPVVRGGFNWGLHFKWDLVPLSELgRA 271
Cdd:cd02510    81 aatGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRgSSGDARGGFDWSLHFKWLPLPEEER-RR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 272 EGATAPIKSPTMAGGLFAMNRQYFHELGQYDSGMDIWGGENLEISFRIWMCGGKLFIIPCSRVGHIFR-KRRPYGSPEGQ 350
Cdd:cd02510   160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 351 DTMTHNSLRLAHVWLDEYKEQYFSLRPDLKTKSYGNISERVELRKKLGCKSFKWYLDNVY 410
Cdd:cd02510   240 GTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
436-564 6.21e-64

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: 6.21e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 436 KVLQRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSLLCLDMSETRsSDPPRLMKCHGSG 515
Cdd:cd23440     1 KVIRKGQLKHAGSGLCLVAEDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLLCLDSSETS-SDFPRLMKCHGSG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1701944547 516 GSQQWTFGKNNRLYQVSVGQCLRAVDPlGQKGSVAMAICDGSSSQQWHL 564
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 ...
154-410 4.22e-163

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: 465.91  E-value: 4.22e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 154 SVVICFYNEAFSALLRTVHSVIDRTPAHLLHEIILVDDDSDF-------------------------------------- 195
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKpelkllleeyykkylpkvkvlrlkkreglirariagar 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 196 ---GEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVVCPVIDIISADTLAYS-SSPVVRGGFNWGLHFKWDLVPLSELgRA 271
Cdd:cd02510    81 aatGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRgSSGDARGGFDWSLHFKWLPLPEEER-RR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 272 EGATAPIKSPTMAGGLFAMNRQYFHELGQYDSGMDIWGGENLEISFRIWMCGGKLFIIPCSRVGHIFR-KRRPYGSPEGQ 350
Cdd:cd02510   160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 351 DTMTHNSLRLAHVWLDEYKEQYFSLRPDLKTKSYGNISERVELRKKLGCKSFKWYLDNVY 410
Cdd:cd02510   240 GTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
436-564 6.21e-64

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: 6.21e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 436 KVLQRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSLLCLDMSETRsSDPPRLMKCHGSG 515
Cdd:cd23440     1 KVIRKGQLKHAGSGLCLVAEDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLLCLDSSETS-SDFPRLMKCHGSG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1701944547 516 GSQQWTFGKNNRLYQVSVGQCLRAVDPlGQKGSVAMAICDGSSSQQWHL 564
Cdd:cd23440    80 GSQQWRFKKDNRLYNPASGQCLAASKN-GTSGYVTMDICSDSPSQKWVF 127
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
441-562 7.94e-28

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 108.00  E-value: 7.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 441 GRLYHLQTNKCLVAQGRpSQKGGLVVLKACDYSDPNQIWIYNEEHEL-VLNSLLCLDMSETRSSDPPRLMKCHGSGGSQQ 519
Cdd:pfam00652   3 GRIRNRASGKCLDVPGG-SSAGGPVGLYPCHGSNGNQLWTLTGDGTIrSVASDLCLDVGSTADGAKVVLWPCHPGNGNQR 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1701944547 520 WTFGKNNR-LYQVSVGQCLRAVDPLGQKGSVAMAICD-GSSSQQW 562
Cdd:pfam00652  82 WRYDEDGTqIRNPQSGKCLDVSGAGTSNGKVILWTCDsGNPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
445-565 8.86e-25

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 99.12  E-value: 8.86e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547  445 HLQTNKCLVAQGRPSQkgglVVLKACDYSDPNQIWIYNEEHEL-VLNSLLCLDMSETRSSdPPRLMKCHGSGGSQQWTFG 523
Cdd:smart00458   3 SGNTGKCLDVNGNKNP----VGLFDCHGTGGNQLWKLTSDGAIrIKDTDLCLTANGNTGS-TVTLYSCDGTNDNQYWEVN 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1701944547  524 KNNRLYQVSVGQCLRAVDPLGQKgSVAMAICDGSSSQQWHLE 565
Cdd:smart00458  78 KDGTIRNPDSGKCLDVKDGNTGT-KVILWTCSGNPNQKWIFE 118
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
154-293 4.39e-19

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: 84.75  E-value: 4.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 154 SVVICFYNEAfSALLRTVHSVIDRTpaHLLHEIILVDDDSD--------------------------------------- 194
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGSTdgtveiaeeyakkdprvrvirlpenrgkagarnaglraa 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 195 FGEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVVCPVIDIISADTLAYssspvvrggfNWGLHFKWDLVPLSELGRAEGA 274
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY----------RRASRITLSRLPFFLGLRLLGL 147
                         170
                  ....*....|....*....
gi 1701944547 275 TAPIKSPTMAGGLFAMNRQ 293
Cdd:pfam00535 148 NLPFLIGGFALYRREALEE 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
147-339 3.69e-09

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: 58.21  E-value: 3.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 147 PPDLPAASVVICFYNEAfSALLRTVHSVIDRTPAHLLHEIILVDDDSD--FGEVLV-FLDSHCEVNVMWLQP-------L 216
Cdd:COG1215    25 PADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGSTdeTAEIAReLAAEYPRVRVIERPEnggkaaaL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 217 LAAIREDRHTVVCpVIDiisADTLAyssSPvvrggfNWglhfkwdlvpLSELgraegaTAPIKSPT--MAGGLFAMNRQY 294
Cdd:COG1215   104 NAGLKAARGDIVV-FLD---ADTVL---DP------DW----------LRRL------VAAFADPGvgASGANLAFRREA 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1701944547 295 FHELGQYDSGMdiwGGENLEISFRIWMCGGKLFIIPCSRVGHIFR 339
Cdd:COG1215   155 LEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYEEAP 196
 
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 ...
154-410 4.22e-163

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: 465.91  E-value: 4.22e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 154 SVVICFYNEAFSALLRTVHSVIDRTPAHLLHEIILVDDDSDF-------------------------------------- 195
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKpelkllleeyykkylpkvkvlrlkkreglirariagar 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 196 ---GEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVVCPVIDIISADTLAYS-SSPVVRGGFNWGLHFKWDLVPLSELgRA 271
Cdd:cd02510    81 aatGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRgSSGDARGGFDWSLHFKWLPLPEEER-RR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 272 EGATAPIKSPTMAGGLFAMNRQYFHELGQYDSGMDIWGGENLEISFRIWMCGGKLFIIPCSRVGHIFR-KRRPYGSPEGQ 350
Cdd:cd02510   160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 351 DTMTHNSLRLAHVWLDEYKEQYFSLRPDLKTKSYGNISERVELRKKLGCKSFKWYLDNVY 410
Cdd:cd02510   240 GTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
436-564 6.21e-64

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: 6.21e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 436 KVLQRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSLLCLDMSETRsSDPPRLMKCHGSG 515
Cdd:cd23440     1 KVIRKGQLKHAGSGLCLVAEDEVSQKGSLLVLRPCSRNDKKQLWYYTEDGELRLANLLCLDSSETS-SDFPRLMKCHGSG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1701944547 516 GSQQWTFGKNNRLYQVSVGQCLRAVDPlGQKGSVAMAICDGSSSQQWHL 564
Cdd:cd23440    80 GSQQWRFKKDNRLYNPASGQCLAASKN-GTSGYVTMDICSDSPSQKWVF 127
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
441-562 7.94e-28

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 108.00  E-value: 7.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 441 GRLYHLQTNKCLVAQGRpSQKGGLVVLKACDYSDPNQIWIYNEEHEL-VLNSLLCLDMSETRSSDPPRLMKCHGSGGSQQ 519
Cdd:pfam00652   3 GRIRNRASGKCLDVPGG-SSAGGPVGLYPCHGSNGNQLWTLTGDGTIrSVASDLCLDVGSTADGAKVVLWPCHPGNGNQR 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1701944547 520 WTFGKNNR-LYQVSVGQCLRAVDPLGQKGSVAMAICD-GSSSQQW 562
Cdd:pfam00652  82 WRYDEDGTqIRNPQSGKCLDVSGAGTSNGKVILWTCDsGNPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
445-565 8.86e-25

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 99.12  E-value: 8.86e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547  445 HLQTNKCLVAQGRPSQkgglVVLKACDYSDPNQIWIYNEEHEL-VLNSLLCLDMSETRSSdPPRLMKCHGSGGSQQWTFG 523
Cdd:smart00458   3 SGNTGKCLDVNGNKNP----VGLFDCHGTGGNQLWKLTSDGAIrIKDTDLCLTANGNTGS-TVTLYSCDGTNDNQYWEVN 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1701944547  524 KNNRLYQVSVGQCLRAVDPLGQKgSVAMAICDGSSSQQWHLE 565
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 ...
436-565 1.41e-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: 96.28  E-value: 1.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 436 KVLQRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSlLCLDMSETrsSDPPRLMKCHGSG 515
Cdd:cd23462     1 EALAYGEIRNLAGKLCLDAPGRKKELNKPVGLYPCHGQGGNQYWMLTKDGEIRRDD-LCLDYAGG--SGDVTLYPCHGMK 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1701944547 516 GSQQWTFGK-NNRLYQVSVGQCLRAVDPlgqKGSVAMAICDGSSS-QQWHLE 565
Cdd:cd23462    78 GNQFWIYDEeTKQIVHGTSKKCLELSDD---SSKLVMEPCNGSSPrQQWEFE 126
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
441-566 1.77e-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: 84.29  E-value: 1.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 441 GRLYHLQTNKCLVAQGRpsQKGGLVVLKACDYSDPNQIWIYNEEHELVlNSLLCLDMSetRSSDPPRLMKCHGSGGSQQW 520
Cdd:cd23433     7 GEIRNVETNLCLDTMGR--KAGEKVGLSSCHGQGGNQVFSYTAKGEIR-SDDLCLDAS--RKGGPVKLEKCHGMGGNQEW 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1701944547 521 TFGKN-NRLYQVSVGQCLRAVDPlGQKGSVAMAICDGSSSQQWHLEG 566
Cdd:cd23433    82 EYDKEtKQIRHVNSGLCLTAPNE-DDPNEPVLRPCDGGPSQKWELEG 127
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
154-293 4.39e-19

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: 84.75  E-value: 4.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 154 SVVICFYNEAfSALLRTVHSVIDRTpaHLLHEIILVDDDSD--------------------------------------- 194
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGSTdgtveiaeeyakkdprvrvirlpenrgkagarnaglraa 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 195 FGEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVVCPVIDIISADTLAYssspvvrggfNWGLHFKWDLVPLSELGRAEGA 274
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY----------RRASRITLSRLPFFLGLRLLGL 147
                         170
                  ....*....|....*....
gi 1701944547 275 TAPIKSPTMAGGLFAMNRQ 293
Cdd:pfam00535 148 NLPFLIGGFALYRREALEE 166
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
441-562 2.58e-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: 75.17  E-value: 2.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 441 GRLYHLQTNKCLVAQGRPSQkGGLVVLKACDYSDPNQIWIYNEEHELVlNSLLCLDmseTRSSDPPRLMKCHGSGGSQQW 520
Cdd:cd23460     3 GQIKHTESGLCLDWAGESNG-DKTVALKPCHGGGGNQFWMYTGDGQIR-QDHLCLT---ADEGNKVTLRECADQLPSQEW 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1701944547 521 TF-GKNNRLYQVSVGQCLRAVDplgQKGSVAMAICDGSS-SQQW 562
Cdd:cd23460    78 SYdEKTGTIRHRSTGLCLTLDA---NNDVVILKECDSNSlWQKW 118
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
449-562 4.49e-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: 4.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 449 NKCLVAQGRPSQKGGLVVLKACDYSDpNQIWIYNEEHELVLNSLLCLDMS--ETRSSDPPRLMKCHGsGGSQQWTFGKNN 526
Cdd:cd23418    14 GRCLDVPGGSTTNGTRLILWDCHGGA-NQQFTFTSAGELRVGGDKCLDAAggGTTNGTPVVIWPCNG-GANQKWRFNSDG 91
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1701944547 527 RLYQVSVGQCLRAvdPLGQKGSVAMAI---CDGSSSQQW 562
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 ...
439-562 6.27e-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: 6.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 439 QRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDpNQIWIY----NEEHELV-LNSLLCLDMSETRSSD--PPRLMKC 511
Cdd:cd00161     1 GTYRIVNAASGKCLDVAGGSTANGAPVQQWTCNGGA-NQQWTLtpvgDGYYTIRnVASGKCLDVAGGSTANgaNVQQWTC 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1701944547 512 HGsGGSQQWTF----GKNNRLYQVSVGQCLRAVDPLGQKGS-VAMAICDGSSSQQW 562
Cdd:cd00161    80 NG-GDNQQWRLepvgDGYYRIVNKHSGKCLDVSGGSTANGAnVQQWTCNGGANQQW 134
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
441-563 2.01e-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: 61.30  E-value: 2.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 441 GRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSL-LCLDMSETRSSdpprLMKCHGSGGSQQ 519
Cdd:cd23442     6 GQLYNTGTGYCADYIHGWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSLqLCLDVRQEQVV----LQNCTKEKTSQK 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1701944547 520 WTFGKNNRLYQVSVGQCLRAVDPLGQKGsVAMAICDGSSSQQWH 563
Cdd:cd23442    82 WDFQETGRIVHILSGKCIEAVESENSKL-LFLSPCNGQRNQMWK 124
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
447-562 6.55e-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: 59.64  E-value: 6.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 447 QTNKCLVAQGRpsQKGGLVVLKACDYSDPNQIWIYNEEHeLVLNSLLCLDMSETRSSDPPRLMKCHGSGGSQQWTFGKNN 526
Cdd:cd23434     7 QGNLCLDTLGH--KAGGTVGLYPCHGTGGNQEWSFTKDG-QIKHDDLCLTVVDRAPGSLVTLQPCREDDSNQKWEQIENN 83
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1701944547 527 -RLYQVSVGQCLRAVDplGQKGSVAMAICDGSS-SQQW 562
Cdd:cd23434    84 sKLRHVGSNLCLDSRN--AKSGGLTVETCDPSSgSQQW 119
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
443-562 7.59e-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: 59.53  E-value: 7.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 443 LYHLQTNKCLVAQGRpsqkGGLVVLKACDYSDPNQIWIYNEEHELV-LNSLLCLDMSETRSSDPPRLMKCHGSGGSQQWT 521
Cdd:cd23385     5 IYNEDLGKCLAARSS----SSKVSLSTCNPNSPNQQWKWTSGHRLFnVGTGKCLGVSSSSPSSPLRLFECDSEDELQKWK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1701944547 522 fGKNNRLYQVSVGQCLRAVDPLGQKGSVAmaiCDGSSSQQW 562
Cdd:cd23385    81 -CSKDGLLLLKGLGLLLLYDKSGKNVVVS---KGSGLSSRW 117
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
441-564 4.38e-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: 4.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 441 GRLYHLQTNKCLVAQGRP-SQKGGLVvlkACDYSDPNQIWIYNEEHELVLNSLlCLDMSetRSSDPPRLMKCHGSGGSQQ 519
Cdd:cd23467     7 GEIRNVETNQCLDNMGRKeNEKVGIF---NCHGMGGNQVFSYTADKEIRTDDL-CLDVS--RLNGPVVMLKCHHMRGNQL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1701944547 520 WTFGKNN-RLYQVSVGQCLRavDPLGQKGSV-AMAICDGSSSQQWHL 564
Cdd:cd23467    81 WEYDAERlTLRHVNSNQCLD--EPSEEDKMVpTMKDCSGSRSQQWLL 125
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
441-562 8.91e-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: 8.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 441 GRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSL--LCLdmsETRSSDPPRLMKCHGSG--- 515
Cdd:cd23435     5 GALRNKGSELCLDVNNPNGQGGKPVIMYGCHGLGGNQYFEYTSKGEIRHNIGkeLCL---HASGSDEVILQHCTSKGkdv 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1701944547 516 -GSQQWTFGKNNRLYQVSVGQCLRAVDPlgqkgSVAMAICDGSS-SQQW 562
Cdd:cd23435    82 pPEQKWLFTQDGTIRNPASGLCLHASGY-----KVLLRTCNPSDdSQKW 125
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
441-563 1.07e-09

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: 56.58  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 441 GRLYHLQTNKCLVAQGRPSQKGglVVLKAC--DYSDPNQIWIYNEEHELVL-NSLLCLDMSETRSSDPPRLMKCHGSGGS 517
Cdd:cd23439     3 GEIRNVGSGLCIDTKHGGENDE--VRLSKCvkDGGGGEQQFELTWHEDIRPkKRKVCFDVSSHTPGAPVILYACHGMKGN 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1701944547 518 QQWTFGKNNR-LYQVSVGQCLRAVDplgQKGSVAMAICDGSS-SQQWH 563
Cdd:cd23439    81 QLWKYRPNTKqLYHPVSGLCLDADP---GSGKVFMNHCDESSdTQKWT 125
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
440-522 1.13e-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: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 440 RGRLYHlqTNKCLVAQgrpsqKGGLVVLKACDYSDPNQIWIYNEEHELVLN--SLLCLDMSETRssDPPRLMKCHGSGGS 517
Cdd:cd23460    45 DGQIRQ--DHLCLTAD-----EGNKVTLRECADQLPSQEWSYDEKTGTIRHrsTGLCLTLDANN--DVVILKECDSNSLW 115

                  ....*
gi 1701944547 518 QQWTF 522
Cdd:cd23460   116 QKWIF 120
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
445-562 2.31e-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: 55.49  E-value: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 445 HLQT-NKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVlNSLLCLDMSETRSSDPPRLMKChGSGGSQQWTFg 523
Cdd:cd23441     7 QIKQgNLCLDSDEQLFQGPALLILAPCSNSSDSQEWSFTKDGQLQ-TQGLCLTVDSSSKDLPVVLETC-SDDPKQKWTR- 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1701944547 524 KNNRLYQVSVGQCLravDPLGQKGsVAMAIC-DGSSSQQW 562
Cdd:cd23441    84 TGRQLVHSESGLCL---DSRKKKG-LVVSPCrSGAPSQKW 119
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
147-339 3.69e-09

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: 58.21  E-value: 3.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 147 PPDLPAASVVICFYNEAfSALLRTVHSVIDRTPAHLLHEIILVDDDSD--FGEVLV-FLDSHCEVNVMWLQP-------L 216
Cdd:COG1215    25 PADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGSTdeTAEIAReLAAEYPRVRVIERPEnggkaaaL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 217 LAAIREDRHTVVCpVIDiisADTLAyssSPvvrggfNWglhfkwdlvpLSELgraegaTAPIKSPT--MAGGLFAMNRQY 294
Cdd:COG1215   104 NAGLKAARGDIVV-FLD---ADTVL---DP------DW----------LRRL------VAAFADPGvgASGANLAFRREA 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1701944547 295 FHELGQYDSGMdiwGGENLEISFRIWMCGGKLFIIPCSRVGHIFR 339
Cdd:COG1215   155 LEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYEEAP 196
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
441-564 4.69e-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: 4.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 441 GRLYHLQTNKCLVAQGRP-SQKGGLVvlkACDYSDPNQIWIYNEEHELVLNSLlCLDMSetRSSDPPRLMKCHGSGGSQQ 519
Cdd:cd23466     7 GEIRNVETNQCLDNMARKeNEKVGIF---NCHGMGGNQVFSYTANKEIRTDDL-CLDVS--KLNGPVMMLKCHHLKGNQL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1701944547 520 WTFGKNN-RLYQVSVGQCL-RAVDPLGQKGSvaMAICDGSSSQQWHL 564
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 ...
449-562 9.24e-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: 53.95  E-value: 9.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 449 NKCLVAQGRPsqKGGLVVLKACDYSD----PNQIWIYNEEHELVL-NSLLCLDMSETRSsdppRLMKCHGSGGSQQWTFg 523
Cdd:cd23461    13 NLCLDILGRS--HGGPPVLAKCSSNKsmpgTFQNFSLTFHRQIKHgTSDDCLEVRGNNV----RLSRCHYQGGNQYWKY- 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1701944547 524 kNNRLYQVSVGQ----CLRAVDplgQKGSVAMAICDGSS-SQQW 562
Cdd:cd23461    86 -DYETHQLINGGqnnkCLEADV---ESLKITLSICDSDNvEQKW 125
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
480-563 1.36e-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: 52.99  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 480 IYNEEHELvlnsllCLDMSEtrSSDPPRLMKCHGSGGSQQWTFGKNNRLYQVSVGQCLrAVDPLGQKGSVAMAICDGSS- 558
Cdd:cd23385     5 IYNEDLGK------CLAARS--SSSKVSLSTCNPNSPNQQWKWTSGHRLFNVGTGKCL-GVSSSSPSSPLRLFECDSEDe 75

                  ....*
gi 1701944547 559 SQQWH 563
Cdd:cd23385    76 LQKWK 80
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
151-376 1.45e-08

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 55.00  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 151 PAASVVICFYNEAfSALLRTVHSVIDRTPAHllHEIILVDDDSDFGEVlvfldshcevnvmwlqPLLAAIREDRHTVVCp 230
Cdd:COG1216     3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPP--FEVIVVDNGSTDGTA----------------ELLAALAFPRVRVIR- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 231 vidiiSADTLAYSsspvvrGGFNWGLHF---KW------DLVPLSE-LGRAEGATApiksptmagglFAMNRQYFHELGQ 300
Cdd:COG1216    63 -----NPENLGFA------AARNLGLRAaggDYllflddDTVVEPDwLERLLAAAC-----------LLIRREVFEEVGG 120
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1701944547 301 YDSGMDIWGGEnLEISFRIWMCGGKLFIIPCSRVGHIFRKRRpyGSPEGQDTMTHNSLRLAHVWLDEYKEQYFSLR 376
Cdd:COG1216   121 FDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASS--GPLLRAYYLGRNRLLFLRKHGPRPLLRLALLR 193
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
442-563 1.72e-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: 52.82  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 442 RLYHLQTNKCLVAQGrpsqkGGLVVLKACDySDPNQIWIY----NEEHELV-LNSLLCLDMSETRSsdpPRLMKChGSGG 516
Cdd:cd23415     4 RLRNVATGRCLDSNA-----GGNVYTGPCN-GGPYQRWTWsgvgDGTVTLRnAATGRCLDSNGNGG---VYTLPC-NGGS 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1701944547 517 SQQWTF----GKNNRLYQVSVGQCLRAVDplgqKGSVAMAICDGSSSQQWH 563
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 ...
448-565 2.81e-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: 52.71  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 448 TNKCLVAQGRPSQKGGLVVLKAC-DYSDPNQIWIYNEEHELvLNSLLCLDMSETRSSdPPRLMKCHGS-GGSQQWTFGKN 525
Cdd:cd23459    15 TNLCLDTLQRDEDKGYNLGLYPCqGGLSSNQLFSLSKKGEL-RREESCADVQGTEES-KVILITCHGLeKFNQKWKHTKG 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1701944547 526 NRLYQVSVGQCLRAVdPLGQKGSVAMAICDGSSSQQWHLE 565
Cdd:cd23459    93 GQIVHLASGKCLDAE-GLKSGDDVTLAKCDGSLSQKWTFE 131
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
154-330 3.04e-08

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 54.32  E-value: 3.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 154 SVVICFYNEAfSALLRTVHSVIDRTPAHLlhEIILVDDDSD-----------------------------------F--- 195
Cdd:COG0463     5 SVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTdgtaeilrelaakdprirvirlernrgkgaarnagLaaa 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 196 -GEVLVFLDSHCEVNVMWLQPLLAAIREDRHtvvcpviDIISADTLAYSSSPVVRGGFNWGLHFKWDLVPLselgraega 274
Cdd:COG0463    82 rGDYIAFLDADDQLDPEKLEELVAALEEGPA-------DLVYGSRLIREGESDLRRLGSRLFNLVRLLTNL--------- 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1701944547 275 tapiksPTMAGGLFAMNRQYFHELGqYDSGMdiwgGENLEIsFRIWMCGGKLFIIP 330
Cdd:COG0463   146 ------PDSTSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVP 189
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
440-521 5.19e-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: 51.44  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 440 RGRLYHLQTNKCLVAQGrpSQKGGLVVLKACDYSDPNQIWIYNeEHELVLNSLLCLDMSETRSSdpPRLMKCHGSGGSQQ 519
Cdd:cd23385    42 GHRLFNVGTGKCLGVSS--SSPSSPLRLFECDSEDELQKWKCS-KDGLLLLKGLGLLLLYDKSG--KNVVVSKGSGLSSR 116

                  ..
gi 1701944547 520 WT 521
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 ...
448-562 8.01e-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: 8.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 448 TNKCL-VAQGRPSQkGGLVVLKACDYSDpNQIWIYNEEHEL-VLNslLCLDMSETRSSD--PPRLMKCHGSGGsQQWTFG 523
Cdd:cd23451    10 AGKCLdVPGSSTAD-GNPVQIYTCNGTA-AQKWTLGTDGTLrVLG--KCLDVSGGGTANgtLVQLWDCNGTGA-QKWVPR 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1701944547 524 KNNRLYQVSVGQCLRAVDPLGQKGS-VAMAICDGSSSQQW 562
Cdd:cd23451    85 ADGTLYNPQSGKCLDAPGGSTTDGTqLQLYTCNGTAAQQW 124
beta-trefoil_Ricin_SCDase_rpt2 cd23500
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
447-563 1.63e-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: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 447 QTNKCLVAQGRPSQKGGLVVLKACDYSdPNQIWIYNEEHELV---LNSLLCLDMSETRSSD--PPRLMKCHGSGGSQQWT 521
Cdd:cd23500     9 RSGKCLSAANGSQLNGSLVQLDACHAS-AGQLWYFDPKKGTIrsaLDGNKCLAIPGGNTGNhtQLQLADCDASNPAQQFN 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1701944547 522 fgKNNRLYQvSVGQCLRAVDPLGQKGSVAMAICD--GSSSQQWH 563
Cdd:cd23500    88 --YDGGVFR-SRLNSNQVIDASGGSDGSELILYDyhGGSNQRWR 128
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
439-522 1.15e-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: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 439 QRGRLYHLQTnkCLVAQGRPSqkGGLVVLKACDYSDPNQIWIYNEEHELV--LNSLLCLDMSETRSSDPpRLMKCHGSGG 516
Cdd:cd23434    41 KDGQIKHDDL--CLTVVDRAP--GSLVTLQPCREDDSNQKWEQIENNSKLrhVGSNLCLDSRNAKSGGL-TVETCDPSSG 115

                  ....*.
gi 1701944547 517 SQQWTF 522
Cdd:cd23434   116 SQQWKF 121
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
493-562 4.24e-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: 4.24e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1701944547 493 LCLDmseTRSSDPPRLMK---CHGSGGSQQWTFGKNNRLYQVSvgQCLravDPLGQKGSVAMAICDGSSSQQW 562
Cdd:cd23437    15 LCLD---TMGHQNGGPVGlypCHGMGGNQLFRLNEAGQLAVGE--QCL---TASGSGGKVKLRKCNLGETGKW 79
beta-trefoil_Ricin_GALNTL6 cd23477
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
503-565 7.48e-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: 46.08  E-value: 7.48e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1701944547 503 SDPPRLMKCHGSGGSQQWTFGKNNRLYQVSVGQCLravDPLGQKGSVAMAICDGSS-SQQWHLE 565
Cdd:cd23477    77 NSPVTLYDCHGMKGNQLWSYRKDKTLFHPVSNSCM---DCNPADKKIFMNRCDPLSeTQQWIFE 137
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
477-562 1.61e-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: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 477 QIWIYNEEHELvlnsllCLDMSETRSSDP-PRLMKCHGSGGSQQWTFGKNNRLYQvsVGQCLRAVdplgqKGSVAMAI-C 554
Cdd:cd23460     2 LGQIKHTESGL------CLDWAGESNGDKtVALKPCHGGGGNQFWMYTGDGQIRQ--DHLCLTAD-----EGNKVTLReC 68

                  ....*....
gi 1701944547 555 DG-SSSQQW 562
Cdd:cd23460    69 ADqLPSQEW 77
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
493-563 3.05e-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: 43.54  E-value: 3.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1701944547 493 LCLDMSE--TRSSDPPRLMKCHGSGGSQQWTFGKNNRLYQVsvGQCLrAVDPLGQKGSVAMAICDGSSSQQWH 563
Cdd:cd23441    13 LCLDSDEqlFQGPALLILAPCSNSSDSQEWSFTKDGQLQTQ--GLCL-TVDSSSKDLPVVLETCSDDPKQKWT 82
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
493-564 4.75e-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: 43.11  E-value: 4.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1701944547 493 LCLDMSETRSSDPPRLM--KCHGsGGSQQWTFgKNNRLYQVSVGQCLRAVDPLGQKGS-VAMAICDGSSSQQWHL 564
Cdd:cd23418    15 RCLDVPGGSTTNGTRLIlwDCHG-GANQQFTF-TSAGELRVGGDKCLDAAGGGTTNGTpVVIWPCNGGANQKWRF 87
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
493-566 5.15e-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: 43.11  E-value: 5.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1701944547 493 LCLDMSETRSSD-PPRLMKCHGSGgSQQWTFGKNNRL-YQVSVGQCLRAVDPLGQKGSVAMAICDGSSSQQWHLEG 566
Cdd:cd23456    12 LCLDVSGGATNGaNVVVYDCNNSN-SQKWYYDATGRLhSKANPGKCLDAGGENSNGANVVLWACNDSANQRWDFDG 86
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
490-565 7.28e-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: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 490 NSLLCLDMSETRSSD--PPRLMKCHGsGGSQQWTFGKNN----RLYQVSVGQCLRAVDPLGQKGS-VAMAICDGSSSQQW 562
Cdd:cd00161     9 ASGKCLDVAGGSTANgaPVQQWTCNG-GANQQWTLTPVGdgyyTIRNVASGKCLDVAGGSTANGAnVQQWTCNGGDNQQW 87

                  ...
gi 1701944547 563 HLE 565
Cdd:cd00161    88 RLE 90
beta-trefoil_Ricin_hemolysin cd23423
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ...
449-520 9.28e-05

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


Pssm-ID: 467301 [Multi-domain]  Cd Length: 119  Bit Score: 41.98  E-value: 9.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1701944547 449 NKCLVAQGrpsqkGGLVVLKACDYSDPNQIWIYNEE--HELVLNSLLCLDMSETRSSdppRLMKCHGSgGSQQW 520
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 ...
445-531 1.03e-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: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 445 HLQTNKCLVAQGrpsqkggLVVLKACDYSDPNQIWIYNEEHELV-LNSLLCLDMSeTRSSDPPRLMKCHGSGGSQQWTFG 523
Cdd:cd23409     8 HVQKQQCLFGNK-------TVSVGKCNATSPNQQWQWTEDGKLLhVKSGQCLGIS-NSSAFHSRRAILLDCSQAPRWTCH 79

                  ....*...
gi 1701944547 524 KNNRLYQV 531
Cdd:cd23409    80 ENEGLLEV 87
beta-trefoil_Ricin_SCDase_rpt1 cd23499
first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
442-564 2.98e-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: 40.90  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 442 RLYHLQTNKCLVAQGRPSQ--KGGLVVLKACDYSDPNQIWIYNEEHELVLNSL---LCLDMSETRSSD-PPRLMKCHGSg 515
Cdd:cd23499     4 RIVNRASGKCLDIPGNDNDvvNGANVILWDCADKSADQRWIYDAASGMLRNKAnpsYCLDNRGQAYNGgEVVLWQCEDS- 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1701944547 516 GSQQWTFgKNNRLyqVSVGQCLRAVDPLG--QKGSVAMAICDGSSSQQWHL 564
Cdd:cd23499    83 DNLRWTY-DNGVL--RSKHNPNIVLDAYGrdNNSQVGQWEYHGGANQQWEL 130
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
441-483 3.77e-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: 3.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1701944547 441 GRLYHLQTNKCLvaqgRPSQKGGLVVLKACDYSDPNQIWIYNE 483
Cdd:cd23437    86 GQIRHKGTGKCL----DLNEGTNKLILQPCDSSSPSQKWEFNE 124
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
280-338 4.43e-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: 4.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1701944547 280 SPTMAGGLFAMNRQYFHELGQYDSGMDIWGGENLEISFRIWMCGGKLFiIPCSRVGHIF 338
Cdd:pfam02709  16 YKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIE-RPPGDIGRYY 73
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
493-565 5.65e-04

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


Pssm-ID: 467354  Cd Length: 150  Bit Score: 40.72  E-value: 5.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1701944547 493 LCLDMSETRSsdPPRLMKCHGSGGSQQWTFGKNNRLYQVSVGQCLravDPLGQKGSVAMAICDGSS-SQQWHLE 565
Cdd:cd23476    69 FCFDAISHNS--PVTLYDCHGMKGNQLWRYRKDKTLYHPVSNSCM---DCSESDHRIFMNTCNPSSpTQQWLFE 137
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
439-481 5.99e-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: 5.99e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1701944547 439 QRGRLYHLQTNKCLVAqgrpsqKGGLVVLKACDYSDPNQIWIY 481
Cdd:cd23435    91 QDGTIRNPASGLCLHA------SGYKVLLRTCNPSDDSQKWTF 127
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
441-480 6.90e-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: 6.90e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1701944547  441 GRLYHLQTNKCLVAQGrpSQKGGLVVLKACDYSdPNQIWI 480
Cdd:smart00458  80 GTIRNPDSGKCLDVKD--GNTGTKVILWTCSGN-PNQKWI 116
beta-trefoil_Ricin_EW29-like cd23449
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ...
447-565 7.19e-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: 7.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 447 QTNKCLVAQGRPSQKGGLVVLKACDYSDP-NQIWIYNEEHELV---LNSLlCLDMSETRSSdppRLMKCHGSGGSQQWTF 522
Cdd:cd23449     9 LNGKVLDVEGANAKPGAKVIMWEKKGGAEdNQLWYEDEVTGTIrskLNDF-CLDASGDKGL---ILNPYDPSNPKQQWKI 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1701944547 523 GKNNRLYQVSVGQCLRAVDPLGQKGSVAMAI-CDGSSSQQWHLE 565
Cdd:cd23449    85 SGNKIQNRSNPDNVLDIKGGSKDDGARLCAWeYNGGPNQLWDFE 128
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
439-479 7.91e-04

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 39.82  E-value: 7.91e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1701944547 439 QRGRLYHLQTNKCLVAQGRPSQKGGlVVLKACDYSDPNQIW 479
Cdd:pfam00652  87 DGTQIRNPQSGKCLDVSGAGTSNGK-VILWTCDSGNPNQQW 126
beta-trefoil_Ricin_LY75 cd23411
ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and ...
485-562 8.35e-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: 39.34  E-value: 8.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1701944547 485 HElvlNSLLCLDMSETRSSdpprLMKCHGSGGSQQWTFGKNNRLYQVSVGQCLrAVDPLGQKGSVAMAICDGSSSQQW 562
Cdd:cd23411     9 HE---NSGKCLKVENSQIS----AVDCKQSSESLQWKWVSEHRLFNLGSKQCL-GLDITKPSNTLKMFECDSKSVMLW 78
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
449-562 1.23e-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: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944547 449 NKCLVAQGRPSQKGGLVVLKACDYSDPnQIWIYNEEHELVLNSLlCLDMSETRSSDPP--RLMKCHGSGgSQQWTFGKNN 526
Cdd:cd23452    11 NKCIDVPNSSTTDGAPLQLWDCNGTNA-QKWTFASDGTLRALGK-CLDVAWGGTDNGTavQLWTCSGNP-AQQFVLSGAG 87
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1701944547 527 RLYQVSVGQCLRAVD-PLGQKGSVAMAICDGSSSQQW 562
Cdd:cd23452    88 DLVNPQANKCVDVSGgNSGNGTRLQLWECSGNANQKW 124
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
494-566 1.25e-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: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1701944547 494 CLDMSETRSSDPPRLM--KCHGSGgSQQWTFGKNNRLYqvSVGQCLRAVDPLGQKGS-VAMAICDGSSSQQWHLEG 566
Cdd:cd23452    13 CIDVPNSSTTDGAPLQlwDCNGTN-AQKWTFASDGTLR--ALGKCLDVAWGGTDNGTaVQLWTCSGNPAQQFVLSG 85
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
439-482 2.05e-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: 38.19  E-value: 2.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1701944547 439 QRGRLYHLQTNKCLvaqgRPSQKGGLVVLKACDYSDPNQIWIYN 482
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 ...
445-511 2.90e-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: 37.80  E-value: 2.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1701944547 445 HLQTNKCLVAqgrpsqKGGLVVLKACDYSDPNQIWIYNEEHELV-LNSLLCLDMSETRSSDPPRLMKC 511
Cdd:cd23411     9 HENSGKCLKV------ENSQISAVDCKQSSESLQWKWVSEHRLFnLGSKQCLGLDITKPSNTLKMFEC 70
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
447-521 4.23e-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: 4.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1701944547 447 QTNKCLVAQGRPSQKGGLVVLKAC----DYSDPNQIWIYNEEHElVLNSLLCLDMSETRSSDPPRLMKCHGSGGSQQWT 521
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 ...
510-562 4.50e-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: 4.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1701944547 510 KCHGSGGSQQWTFGKNNRLyqVSV---GQCLRAVDPlgqkGSVAMAICDGSSSQQW 562
Cdd:cd23423    29 SCDSGDRNQSWILDSEGRY--RSRvapDLCLDADDD----GLLTLEQCSLSLTQKW 78
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
451-523 4.88e-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: 4.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1701944547 451 CLVAQGRPSQkgglVVLKACDySDPNQIWIYNEEHEL--VLNSLLCLDMSETRSsdPPRLMKCHGSGGSQQWTFG 523
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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