LARGE xylosyl- and glucuronyltransferase 1 isoform X2 [Ictidomys tridecemlineatus]
Protein Classification
bZIP transcription factor( domain architecture ID 10406117)
basic leucine zipper (bZIP) transcription factor binds to the promoter regions of genes to control their expression; similar to Crassostrea hongkongensis NFIL3 (nuclear factor interleukin 3-regulated) that mediates a variety of immune responses
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| GT8_LARGE_C | cd06431 | LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in ... |
203-482 | 0e+00 | ||||||
LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis; The catalytic domain of LARGE is a putative glycosyltransferase. Mutations of LARGE in mouse and human cause dystroglycanopathies, a disease associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. LARGE needs to both physically interact with alpha-dystroglycan and function as a glycosyltransferase in order to stimulate alpha-dystroglycan hyperglycosylation. LARGE localizes to the Golgi apparatus and contains three conserved DxD motifs. While two of the motifs are indispensible for glycosylation function, one is important for localization of th eenzyme. LARGE was originally named because it covers approximately large trunck of genomic DNA, more than 600bp long. The predicted protein structure contains an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif, and two putative catalytic domains. This catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis. : Pssm-ID: 133053 Cd Length: 280 Bit Score: 587.90 E-value: 0e+00
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| Glyco_transf_49 super family | cl16461 | Glycosyl-transferase for dystroglycan; This glycosyl-transferase brings about the ... |
538-808 | 8.76e-53 | ||||||
Glycosyl-transferase for dystroglycan; This glycosyl-transferase brings about the glycosylation of the alpha-dystroglycan subunit. Dystroglycan is an integral member of the skeletal muscular dystrophin glycoprotein complex, which links dystrophin to proteins in the extracellular matrix. The actual alignment was detected with superfamily member pfam13896: Pssm-ID: 464027 Cd Length: 327 Bit Score: 186.69 E-value: 8.76e-53
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| bZIP super family | cl21462 | Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
120-154 | 2.38e-04 | ||||||
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. The actual alignment was detected with superfamily member cd14812: Pssm-ID: 473870 [Multi-domain] Cd Length: 52 Bit Score: 39.50 E-value: 2.38e-04
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| Name | Accession | Description | Interval | E-value | ||||||
| GT8_LARGE_C | cd06431 | LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in ... |
203-482 | 0e+00 | ||||||
LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis; The catalytic domain of LARGE is a putative glycosyltransferase. Mutations of LARGE in mouse and human cause dystroglycanopathies, a disease associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. LARGE needs to both physically interact with alpha-dystroglycan and function as a glycosyltransferase in order to stimulate alpha-dystroglycan hyperglycosylation. LARGE localizes to the Golgi apparatus and contains three conserved DxD motifs. While two of the motifs are indispensible for glycosylation function, one is important for localization of th eenzyme. LARGE was originally named because it covers approximately large trunck of genomic DNA, more than 600bp long. The predicted protein structure contains an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif, and two putative catalytic domains. This catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis. Pssm-ID: 133053 Cd Length: 280 Bit Score: 587.90 E-value: 0e+00
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| Glyco_transf_49 | pfam13896 | Glycosyl-transferase for dystroglycan; This glycosyl-transferase brings about the ... |
538-808 | 8.76e-53 | ||||||
Glycosyl-transferase for dystroglycan; This glycosyl-transferase brings about the glycosylation of the alpha-dystroglycan subunit. Dystroglycan is an integral member of the skeletal muscular dystrophin glycoprotein complex, which links dystrophin to proteins in the extracellular matrix. Pssm-ID: 464027 Cd Length: 327 Bit Score: 186.69 E-value: 8.76e-53
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| RfaJ | COG1442 | Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ... |
199-451 | 6.51e-23 | ||||||
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 441051 [Multi-domain] Cd Length: 301 Bit Score: 100.05 E-value: 6.51e-23
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| Glyco_transf_8 | pfam01501 | Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ... |
218-451 | 8.36e-18 | ||||||
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase. Pssm-ID: 279798 [Multi-domain] Cd Length: 252 Bit Score: 83.91 E-value: 8.36e-18
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| bZIP_u3 | cd14812 | Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
120-154 | 2.38e-04 | ||||||
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269874 [Multi-domain] Cd Length: 52 Bit Score: 39.50 E-value: 2.38e-04
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| Name | Accession | Description | Interval | E-value | ||||||
| GT8_LARGE_C | cd06431 | LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in ... |
203-482 | 0e+00 | ||||||
LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis; The catalytic domain of LARGE is a putative glycosyltransferase. Mutations of LARGE in mouse and human cause dystroglycanopathies, a disease associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. LARGE needs to both physically interact with alpha-dystroglycan and function as a glycosyltransferase in order to stimulate alpha-dystroglycan hyperglycosylation. LARGE localizes to the Golgi apparatus and contains three conserved DxD motifs. While two of the motifs are indispensible for glycosylation function, one is important for localization of th eenzyme. LARGE was originally named because it covers approximately large trunck of genomic DNA, more than 600bp long. The predicted protein structure contains an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif, and two putative catalytic domains. This catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis. Pssm-ID: 133053 Cd Length: 280 Bit Score: 587.90 E-value: 0e+00
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| Glyco_transf_8 | cd00505 | Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ... |
203-455 | 1.29e-87 | ||||||
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis; Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+. Pssm-ID: 132996 [Multi-domain] Cd Length: 246 Bit Score: 277.79 E-value: 1.29e-87
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| Glyco_transf_49 | pfam13896 | Glycosyl-transferase for dystroglycan; This glycosyl-transferase brings about the ... |
538-808 | 8.76e-53 | ||||||
Glycosyl-transferase for dystroglycan; This glycosyl-transferase brings about the glycosylation of the alpha-dystroglycan subunit. Dystroglycan is an integral member of the skeletal muscular dystrophin glycoprotein complex, which links dystrophin to proteins in the extracellular matrix. Pssm-ID: 464027 Cd Length: 327 Bit Score: 186.69 E-value: 8.76e-53
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| RfaJ | COG1442 | Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ... |
199-451 | 6.51e-23 | ||||||
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 441051 [Multi-domain] Cd Length: 301 Bit Score: 100.05 E-value: 6.51e-23
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| Glyco_transf_8 | pfam01501 | Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ... |
218-451 | 8.36e-18 | ||||||
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase. Pssm-ID: 279798 [Multi-domain] Cd Length: 252 Bit Score: 83.91 E-value: 8.36e-18
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| GT8_A4GalT_like | cd04194 | A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ... |
203-451 | 2.57e-17 | ||||||
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS. Pssm-ID: 133037 [Multi-domain] Cd Length: 248 Bit Score: 82.26 E-value: 2.57e-17
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| GT8_like_2 | cd06430 | GT8_like_2 represents a subfamily of GT8 with unknown function; A subfamily of ... |
203-447 | 1.01e-13 | ||||||
GT8_like_2 represents a subfamily of GT8 with unknown function; A subfamily of glycosyltransferase family 8 with unknown function: Glycosyltransferase family 8 comprises enzymes with a number of known activities; lipopolysaccharide galactosyltransferase lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase and inositol 1-alpha-galactosyltransferase. It is classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. Pssm-ID: 133052 Cd Length: 304 Bit Score: 72.88 E-value: 1.01e-13
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| bZIP_u3 | cd14812 | Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
120-154 | 2.38e-04 | ||||||
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269874 [Multi-domain] Cd Length: 52 Bit Score: 39.50 E-value: 2.38e-04
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| GT8_like_1 | cd06429 | GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ... |
203-451 | 3.19e-04 | ||||||
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of glycosyltransferase family 8 with unknown function: Glycosyltransferase family 8 comprises enzymes with a number of known activities; lipopolysaccharide galactosyltransferase lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase and inositol 1-alpha-galactosyltransferase. It is classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. Pssm-ID: 133051 [Multi-domain] Cd Length: 257 Bit Score: 43.15 E-value: 3.19e-04
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| GT8_HUGT1_C_like | cd06432 | The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain ... |
203-421 | 4.60e-04 | ||||||
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain of glycoprotein glucosyltransferase (UGT). UGT is a large glycoprotein whose C-terminus contains the catalytic activity. This catalytic C-terminal domain is highly homologous to Glycosyltransferase Family 8 (GT 8) and contains the DXD motif that coordinates donor sugar binding, characteristic for Family 8 glycosyltransferases. GT 8 proteins are retaining enzymes based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. The non-catalytic N-terminal portion of the human UTG1 (HUGT1) has been shown to monitor the protein folding status and activate its glucosyltransferase activity. Pssm-ID: 133054 Cd Length: 248 Bit Score: 42.76 E-value: 4.60e-04
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| bZIP_XBP1 | cd14691 | Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a ... |
118-154 | 7.75e-03 | ||||||
Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a DNA-binding and dimerization domain; XBP1, a member of the Basic leucine zipper (bZIP) family, is the key transcription factor that orchestrates the unfolded protein response (UPR). It is the most conserved component of the UPR and is critical for cell fate determination in response to ER stress. The inositol-requiring enzyme 1 (IRE1)-XBP1 pathway is one of the three major sensors at the ER membrane that initiates the UPR upon activation. IRE1, a type I transmembrane protein kinase and endoribonuclease, oligomerizes upon ER stress leading to its increased activity. It splices the XBP1 mRNA, producing a variant that translocates to the nucleus and activates its target genes, which are involved in protein folding, degradation, and trafficking. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269839 [Multi-domain] Cd Length: 58 Bit Score: 35.26 E-value: 7.75e-03
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