Beta-1,4-N-acetylgalactosaminyltransferase [Caenorhabditis elegans]
Protein Classification
beta-1,4-galactosyltransferase( domain architecture ID 10097028)
beta-1,4-galactosyltransferase is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| b4GalT | cd00899 | Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ... |
158-375 | 7.86e-111 | ||||
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids; Beta-4-Galactosyltransferase transfers galactose from uridine diphosphogalactose to the terminal beta-N-acetylglucosamine residues, hereby forming the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids. At least seven homologous beta-4-galactosyltransferase isoforms have been identified that use different types of glycoproteins and glycolipids as substrates. Of the seven identified members of the beta-1,4-galactosyltransferase subfamily (beta1,4-Gal-T1 to -T7), b1,4-Gal-T1 is most characterized (biochemically). It is a Golgi-resident type II membrane enzyme with a cytoplasmic domain, membrane spanning region, and a stem region and catalytic domain facing the lumen. : Pssm-ID: 132999 [Multi-domain] Cd Length: 219 Bit Score: 323.38 E-value: 7.86e-111
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| Name | Accession | Description | Interval | E-value | ||||
| b4GalT | cd00899 | Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ... |
158-375 | 7.86e-111 | ||||
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids; Beta-4-Galactosyltransferase transfers galactose from uridine diphosphogalactose to the terminal beta-N-acetylglucosamine residues, hereby forming the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids. At least seven homologous beta-4-galactosyltransferase isoforms have been identified that use different types of glycoproteins and glycolipids as substrates. Of the seven identified members of the beta-1,4-galactosyltransferase subfamily (beta1,4-Gal-T1 to -T7), b1,4-Gal-T1 is most characterized (biochemically). It is a Golgi-resident type II membrane enzyme with a cytoplasmic domain, membrane spanning region, and a stem region and catalytic domain facing the lumen. Pssm-ID: 132999 [Multi-domain] Cd Length: 219 Bit Score: 323.38 E-value: 7.86e-111
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| Glyco_transf_7N | pfam13733 | N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of ... |
136-244 | 6.45e-48 | ||||
N-terminal region of glycosyl transferase group 7; This is the N-terminal half 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: 463972 Cd Length: 125 Bit Score: 158.78 E-value: 6.45e-48
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| Name | Accession | Description | Interval | E-value | ||||
| b4GalT | cd00899 | Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ... |
158-375 | 7.86e-111 | ||||
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids; Beta-4-Galactosyltransferase transfers galactose from uridine diphosphogalactose to the terminal beta-N-acetylglucosamine residues, hereby forming the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids. At least seven homologous beta-4-galactosyltransferase isoforms have been identified that use different types of glycoproteins and glycolipids as substrates. Of the seven identified members of the beta-1,4-galactosyltransferase subfamily (beta1,4-Gal-T1 to -T7), b1,4-Gal-T1 is most characterized (biochemically). It is a Golgi-resident type II membrane enzyme with a cytoplasmic domain, membrane spanning region, and a stem region and catalytic domain facing the lumen. Pssm-ID: 132999 [Multi-domain] Cd Length: 219 Bit Score: 323.38 E-value: 7.86e-111
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| Glyco_transf_7N | pfam13733 | N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of ... |
136-244 | 6.45e-48 | ||||
N-terminal region of glycosyl transferase group 7; This is the N-terminal half 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: 463972 Cd Length: 125 Bit Score: 158.78 E-value: 6.45e-48
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| Glyco_transf_7C | pfam02709 | N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ... |
249-325 | 1.31e-33 | ||||
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: 120.02 E-value: 1.31e-33
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| GT2_Chondriotin_Pol_N | cd06420 | N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ... |
205-304 | 5.66e-07 | ||||
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix. Pssm-ID: 133042 [Multi-domain] Cd Length: 182 Bit Score: 49.50 E-value: 5.66e-07
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