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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749624 796 PVVRASGVLINMALGKCVSIENITVTLEDCDGSSQLQQFNYTWVRLIKHGEWCVAPIPEKGSLTLYHCDNRNNRLKWLHK 875
Cdd:cd23436    1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 158749624 876 SASAFhPELVDHIVFENYQQLLCMEGNFSQKTLKLAACNPMELQQKWKFEKYY 928
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 158749624 796 PVVRASGVLINMALGKCVSIENITVTLEDCDGSSQLQQFNYTWVRLIKHGEWCVAPIPEKGSLTLYHCDNRNNRLKWLHK 875
Cdd:cd23436    1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 158749624 876 SASAFhPELVDHIVFENYQQLLCMEGNFSQKTLKLAACNPMELQQKWKFEKYY 928
Cdd:cd23436   81 SLIAF-PELMDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749624   805 INMALGKCVSI--ENITVTLEDCDGSSQLQQFNYTWVRLIKH--GEWCVAPIPEKGS-LTLYHCDNRNNRLKWLHKSASA 879
Cdd:smart00458   2 ISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGStVTLYSCDGTNDNQYWEVNKDGT 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 158749624   880 FHpelvdhivfeNYQQLLCMEGNFSQK--TLKLAACNPmELQQKWKFE 925
Cdd:smart00458  82 IR----------NPDSGKCLDVKDGNTgtKVILWTCSG-NPNQKWIFE 118

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749624  800 ASGVLINMALGKCVSIE-----NITVTLEDCDGSSQLQQFNYTWVRLIKH--GEWC--VAPIPEKGSLTLYHCDNRNNRL 870
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPggssaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCldVGSTADGAKVVLWPCHPGNGNQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 158749624  871 KWLHKSASafhpelvDHIVfeNYQQLLCME---GNFSQKTLKLAACNPMELQQKW 922
Cdd:pfam00652  81 RWRYDEDG-------TQIR--NPQSGKCLDvsgAGTSNGKVILWTCDSGNPNQQW 126

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 158749624 796 PVVRASGVLINMALGKCVSIENITVTLEDCDGSSQLQQFNYTWVRLIKHGEWCVAPIPEKGSLTLYHCDNRNNRLKWLHK 875
Cdd:cd23436    1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 158749624 876 SASAFhPELVDHIVFENYQQLLCMEGNFSQKTLKLAACNPMELQQKWKFEKYY 928
Cdd:cd23436   81 SLIAF-PELMDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749624   805 INMALGKCVSI--ENITVTLEDCDGSSQLQQFNYTWVRLIKH--GEWCVAPIPEKGS-LTLYHCDNRNNRLKWLHKSASA 879
Cdd:smart00458   2 ISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGStVTLYSCDGTNDNQYWEVNKDGT 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 158749624   880 FHpelvdhivfeNYQQLLCMEGNFSQK--TLKLAACNPmELQQKWKFE 925
Cdd:smart00458  82 IR----------NPDSGKCLDVKDGNTgtKVILWTCSG-NPNQKWIFE 118

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749624 502 LLRSVHSVLNRSPPHLikEILLVDDFSTKEYLkADLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSHV 581
Cdd:cd00761   12 LERCLESLLAQTYPNF--EVIVVDDGSTDGTL-EILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEYILFLDADD 88

                         90       100
                 ....*....|....*....|...
gi 158749624 582 ECNVGWLEPLLERVYLNRKKVAC 604
Cdd:cd00761   89 LLLPDWLERLVAELLADPEADAV 111

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749624  800 ASGVLINMALGKCVSIE-----NITVTLEDCDGSSQLQQFNYTWVRLIKH--GEWC--VAPIPEKGSLTLYHCDNRNNRL 870
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPggssaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCldVGSTADGAKVVLWPCHPGNGNQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 158749624  871 KWLHKSASafhpelvDHIVfeNYQQLLCME---GNFSQKTLKLAACNPMELQQKW 922
Cdd:pfam00652  81 RWRYDEDG-------TQIR--NPQSGKCLDvsgAGTSNGKVILWTCDSGNPNQQW 126

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 158749624 798 VRASGVLINMALGKCV----SIENITVTLEDCDGSSQLQQFNYTWVRLIKHGEWCVAPIPEKGSLTLYHCDNRNNRlKWL 873
Cdd:cd23437    2 NLAWGEIRNLGTGLCLdtmgHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETG-KWE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158749624 874 HKSASafhpELVDHIVFEnyqqlLCMEGNFSQKTLKLAACNPMELQQKWKF 924
Cdd:cd23437   81 YDEAT----GQIRHKGTG-----KCLDLNEGTNKLILQPCDSSSPSQKWEF 122

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749624 800 ASGVLINMAL-GKCVSIENI----TVTLEDCDGS----SQLQQFNYTWVRLIKHG--EWCVAPipEKGSLTLYHCdnrnn 868
Cdd:cd23461    2 ASGVIQSVAFpNLCLDILGRshggPPVLAKCSSNksmpGTFQNFSLTFHRQIKHGtsDDCLEV--RGNNVRLSRC----- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158749624 869 rlkwlHKSASA--FHPELVDHIVFENYQQLLCMEGNFSQKTLKLAACNPMELQQKWKF 924
Cdd:cd23461   75 -----HYQGGNqyWKYDYETHQLINGGQNNKCLEADVESLKITLSICDSDNVEQKWKW 127

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749624 800 ASGVLINMALGKCVS------IENITVTLEDCDGSSQLQQFNYTWVRLIKHGEWCVAPIPEKGSLTLYHCDNRNNRLKWL 873
Cdd:cd23462    4 AYGEIRNLAGKLCLDapgrkkELNKPVGLYPCHGQGGNQYWMLTKDGEIRRDDLCLDYAGGSGDVTLYPCHGMKGNQFWI 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 158749624 874 HKSASAfhpelvdHIVFENYQqlLCMEGNFSQKTLKLAACNPMELQQKWKFE 925
Cdd:cd23462   84 YDEETK-------QIVHGTSK--KCLELSDDSSKLVMEPCNGSSPRQQWEFE 126

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 158749624 501 ALLRSVHSVLNRSPPHlikEILLVDDFSTkeylkaD-----LDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLT 575
Cdd:cd04179   14 ELVERLLAVLEEGYDY---EIIVVDDGST------DgtaeiARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARGDIVV 84

                 ....
gi 158749624 576 FLDS 579
Cdd:cd04179   85 TMDA 88

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749624 796 PVVRASGVLINMALGKCVSIENIT----VTLEDC----DGSS--QLQQFNYTWVRLIKHGE------WCVAPIPEKGSLT 859
Cdd:cd23476    2 PPAAAWGEIRNVGTGLCADTKHGAlgspLRLEGCvkgrGEAAwnNGQVFTFGWREDIRPGDpqhtkkFCFDAISHNSPVT 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158749624 860 LYHCDN-RNNRLKWLHKSASAFHPelvdhiVFENyqqllCMEGNFSQKTLKLAACNPMELQQKWKFEK 926
Cdd:cd23476   82 LYDCHGmKGNQLWRYRKDKTLYHP------VSNS-----CMDCSESDHRIFMNTCNPSSPTQQWLFEH 138

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749624 802 GVLINMALGKCV-----SIENITVTLEDCDGSSQLQQFNYTWVRLIKHGEWCVAPIpEKGSLTLYHCDNRNNRLKWLHKs 876
Cdd:cd23460    3 GQIKHTESGLCLdwageSNGDKTVALKPCHGGGGNQFWMYTGDGQIRQDHLCLTAD-EGNKVTLRECADQLPSQEWSYD- 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 158749624 877 asafhpELVDHIVfeNYQQLLCMEGNFSQKTLKLAACNPMELQQKWKF 924
Cdd:cd23460   81 ------EKTGTIR--HRSTGLCLTLDANNDVVILKECDSNSLWQKWIF 120

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 158749624 520 EILLVDDFSTKEYLKAdLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD---SH 580
Cdd:cd06442   29 EIIVVDDNSPDGTAEI-VRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDadlSH 91

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158749624 804 LINMALGKCVSIENIT--VTLEDCDGSSQLQQFNYTWVRLIKHGEW--C--VAPIPEKGSLTLYHCDNRNNRLKW 872
Cdd:cd23385    5 IYNEDLGKCLAARSSSskVSLSTCNPNSPNQQWKWTSGHRLFNVGTgkClgVSSSSPSSPLRLFECDSEDELQKW 79

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 158749624 490 IIMCFVDEVWSaLLRSVHSVLNRSPPHLIKEILLVDDFS---TKEYLKADLDKymsQFPKVRILRLKERH--GLIRARLA 564
Cdd:cd04192    1 VVIAARNEAEN-LPRLLQSLSALDYPKEKFEVILVDDHStdgTVQILEFAAAK---PNFQLKILNNSRVSisGKKNALTT 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158749624 565 GAQNATGDVLTFLDShvECNV--GWLEPLLERVYLNR-KKVACPVIEVIND 612
Cdd:cd04192   77 AIKAAKGDWIVTTDA--DCVVpsNWLLTFVAFIQKEQiGLVAGPVIYFKGK 125

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 158749624  661 AGGLFSIDKSYFYELGTYDPGLDVWGGENMELSFKVWMCGGEIEiIPCSRVGHIF 715
Cdd:pfam02709  20 FGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIE-RPPGDIGRYY 73

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158749624 806 NMALGKCVSI---ENITVTLEDCDGSSQLQQFNYTWVRLI---KHGEWC--VAPIPEKGSLTLYHCDNRNN 868
Cdd:cd23412    9 NVQLEKCIQVdhgESERVSLAECKPHSEHQQWSWDPETRAlssLHTGECltVLKIQEFGSVRLEPCGSREP 79

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749624 504 RSVHSVLNRSPPHLikEILLVDDFSTKEYLKADLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSHVEC 583
Cdd:cd06423   14 RTIESLLALDYPKL--EVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRHAKGDIVVVLDADTIL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749624 584 NVGWLEPLLERVYLNRKKVA-CPVIEVINDKD--------MSYMTVDNFQRGVFTWpmnfgwktippdvvaKNGIketdi 654
Cdd:cd06423   92 EPDALKRLVVPFFADPKVGAvQGRVRVRNGSEnlltrlqaIEYLSIFRLGRRAQSA---------------LGGV----- 151

                        170       180
                 ....*....|....*....|....*..
gi 158749624 655 ircPVMAGGLFSIDKSYFYELGTYDPG 681
Cdd:cd06423  152 ---LVLSGAFGAFRREALREVGGWDED 175