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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123 336 PIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHK 415
Cdd:cd23436     1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1049480123 416 STSVFhPELVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYY 468
Cdd:cd23436    81 SLIAF-PELMDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123 336 PIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHK 415
Cdd:cd23436     1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1049480123 416 STSVFhPELVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYY 468
Cdd:cd23436    81 SLIAF-PELMDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123 340 ASGVLINVALGKCISIE-----NTTVILEDCDGSKELQQFNYTWLRLIKC--GEWCIA--PIPDKGAVRLHPCDNRNKGL 410
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPggssaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDvgSTADGAKVVLWPCHPGNGNQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1049480123 411 KWLHKSTSvfhpelvNHIVfeNNQQLLCLEGNFSQKILK---VAACDPVKPYQKW 462
Cdd:pfam00652  81 RWRYDEDG-------TQIR--NPQSGKCLDVSGAGTSNGkviLWTCDSGNPNQQW 126

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123  345 INVALGKCISI--ENTTVILEDCDGSKELQQFNYTWLRLIKC--GEWCIAPIPDKGA-VRLHPCDNRNKGLKWLHKSTSV 419
Cdd:smart00458   2 ISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGStVTLYSCDGTNDNQYWEVNKDGT 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1049480123  420 FHpelvnhivfeNNQQLLCLEGNFSQKILKVAA--CDPvKPYQKWKFE 465
Cdd:smart00458  82 IR----------NPDSGKCLDVKDGNTGTKVILwtCSG-NPNQKWIFE 118

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123 336 PIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHK 415
Cdd:cd23436     1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1049480123 416 STSVFhPELVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYY 468
Cdd:cd23436    81 SLIAF-PELMDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123 340 ASGVLINVALGKCISIE-----NTTVILEDCDGSKELQQFNYTWLRLIKC--GEWCIA--PIPDKGAVRLHPCDNRNKGL 410
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPggssaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDvgSTADGAKVVLWPCHPGNGNQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1049480123 411 KWLHKSTSvfhpelvNHIVfeNNQQLLCLEGNFSQKILK---VAACDPVKPYQKW 462
Cdd:pfam00652  81 RWRYDEDG-------TQIR--NPQSGKCLDVSGAGTSNGkviLWTCDSGNPNQQW 126

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123  345 INVALGKCISI--ENTTVILEDCDGSKELQQFNYTWLRLIKC--GEWCIAPIPDKGA-VRLHPCDNRNKGLKWLHKSTSV 419
Cdd:smart00458   2 ISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGStVTLYSCDGTNDNQYWEVNKDGT 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1049480123  420 FHpelvnhivfeNNQQLLCLEGNFSQKILKVAA--CDPvKPYQKWKFE 465
Cdd:smart00458  82 IR----------NPDSGKCLDVKDGNTGTKVILwtCSG-NPNQKWIFE 118

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123  23 NNLPTTSVIMCFVDEvWSTLLRSVHSVINRSPPHLIKEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHGLIRAR 102
Cdd:COG1215    26 ADLPRVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIARELAAEYPRVRVIERPENGGKAAAL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123 103 LAGAQNATGDVLTFLDSHVECNVGWLEPLLErvYLSRKKVACPvievindkdmsymtvdnfqrgifvwpmnfgwrtippd 182
Cdd:COG1215   104 NAGLKAARGDIVVFLDADTVLDPDWLRRLVA--AFADPGVGAS------------------------------------- 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049480123 183 viaknriketdtircpvmaGGLFSIDKSYFFELGTYDPGLdvwGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND 258
Cdd:COG1215   145 -------------------GANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPET 198

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123 338 VRASGVLINVALGKCI----SIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGlKWL 413
Cdd:cd23437     2 NLAWGEIRNLGTGLCLdtmgHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETG-KWE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1049480123 414 HkstsvfhpelvnhivFENNQQL------LCLEGNFSQKILKVAACDPVKPYQKWKF 464
Cdd:cd23437    81 Y---------------DEATGQIrhkgtgKCLDLNEGTNKLILQPCDSSSPSQKWEF 122

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123  26 PTTSVIM--CFVDEVWstLLRSVHSVINRSPPHLikEILLVDDFSTKDYLKDNLDKYMSQFPKVRILRLKERHGLIRARL 103
Cdd:cd04184     1 PLISIVMpvYNTPEKY--LREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATN 76

                          90
                  ....*....|....*.
gi 1049480123 104 AGAQNATGDVLTFLDS 119
Cdd:cd04184    77 SALELATGEFVALLDH 92

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123 350 GKCI----SIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPI-PDKGA-VRLHPCDNRNKGLKWLHkstsvfhpe 423
Cdd:cd23434     9 NLCLdtlgHKAGGTVGLYPCHGTGGNQEWSFTKDGQIKHDDLCLTVVdRAPGSlVTLQPCREDDSNQKWEQ--------- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1049480123 424 lvnhivFENNQQL------LCLEG-NFSQKILKVAACDPVKPYQKWKF 464
Cdd:cd23434    80 ------IENNSKLrhvgsnLCLDSrNAKSGGLTVETCDPSSGSQQWKF 121

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123  42 LLRSVHSVINRSPPHlikEILLVDDFSTkdylkDN----LDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFL 117
Cdd:cd04179    15 LVERLLAVLEEGYDY---EIIVVDDGST-----DGtaeiARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARGDIVVTM 86

                  ..
gi 1049480123 118 DS 119
Cdd:cd04179    87 DA 88

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123  42 LLRSVHSVINRSPPHLikEILLVDDFSTkdylkDN----LDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFL 117
Cdd:cd04187    15 LYERLKAVLESLGYDY--EIIFVDDGST-----DRtleiLRELAARDPRVKVIRLSRNFGQQAALLAGLDHARGDAVITM 87

                  ..
gi 1049480123 118 DS 119
Cdd:cd04187    88 DA 89

putative glycosyl transferase; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1049480123  60 EILLVDDFSTkDYLKDNLDKYMSQFPKVRILRlKERHGLIRARLAGAQNATGDVLTFLD 118
Cdd:PRK10073   37 EIIIVNDGST-DNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAVATGKYVAFPD 93

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1049480123  60 EILLVDDfSTKDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD---SH 120
Cdd:cd06442    29 EIIVVDD-NSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDadlSH 91

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123 356 ENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGA--VRLHPCDNRNKgLKWLHKSTSVFHpelvnhivFENN 433
Cdd:cd23441    24 GPALLILAPCSNSSDSQEWSFTKDGQLQTQGLCLTVDSSSKDlpVVLETCSDDPK-QKWTRTGRQLVH--------SESG 94

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1049480123 434 qqlLCLEgNFSQKILKVAACDPVKPYQKWKFE 465
Cdd:cd23441    95 ---LCLD-SRKKKGLVVSPCRSGAPSQKWDFT 122

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123 344 LINVALGKCISIENTT--VILEDCDGSKELQQFNYTW---LRLIKCGEwCIA--PIPDKGAVRLHPCDNRNKGLKWlhks 416
Cdd:cd23385     5 IYNEDLGKCLAARSSSskVSLSTCNPNSPNQQWKWTSghrLFNVGTGK-CLGvsSSSPSSPLRLFECDSEDELQKW---- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1049480123 417 tsvfhpELVNHIVFENNQQLLCLEGNFSQKILKVaaCDPVKPYQKWK 463
Cdd:cd23385    80 ------KCSKDGLLLLKGLGLLLLYDKSGKNVVV--SKGSGLSSRWK 118

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123 360 VILEDCDGSKELQQFNYTW---LRLIKCGEWCIAPIPDkGAVRLHPCDNRNKGL----KWLHK-STSVFHPelvnhivfe 431
Cdd:cd23435    29 VIMYGCHGLGGNQYFEYTSkgeIRHNIGKELCLHASGS-DEVILQHCTSKGKDVppeqKWLFTqDGTIRNP--------- 98

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1049480123 432 nnQQLLCLEGnfSQKILKVAACDPVKPYQKWKFE 465
Cdd:cd23435    99 --ASGLCLHA--SGYKVLLRTCNPSDDSQKWTFI 128

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049480123  39 WSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYmsqFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD 118
Cdd:cd04186     9 LEYLKACLDSLLAQTYPDF--EVIVVDNAST-DGSVELLREL---FPEVRLIRNGENLGFGAGNNQGIREAKGDYVLLLN 82

                          90       100
                  ....*....|....*....|....*.
gi 1049480123 119 SHVECNVGWLEPLLERvYLSRKKVAC 144
Cdd:cd04186    83 PDTVVEPGALLELLDA-AEQDPDVGI 107