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Conserved domains on  [gi|285812757|tpg|DAA08655|]
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TPA: Ids2p [Saccharomyces cerevisiae S288C]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
185-308 3.61e-11

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.


The actual alignment was detected with superfamily member cd02537:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 240  Bit Score: 63.05  E-value: 3.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812757 185 RAWITILHdsSAESLQAVIVLAESLKNVNSQYNLWVLHSSEVNAF---QLAQVGIKtLIIDEYINlfmnfgtgsgfSASS 261
Cdd:cd02537    1 EAYVTLLT--NDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEEsreALEEVGWI-VREVEPID-----------PPDS 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 285812757 262 QSTETKGELNFKWCKLFLfFSLIDrFELICYLSPTCLVLQNIDELLE 308
Cdd:cd02537   67 ANLLKRPRFKDTYTKLRL-WNLTE-YDKVVFLDADTLVLRNIDELFD 111
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
185-308 3.61e-11

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.


Pssm-ID: 133018 [Multi-domain]  Cd Length: 240  Bit Score: 63.05  E-value: 3.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812757 185 RAWITILHdsSAESLQAVIVLAESLKNVNSQYNLWVLHSSEVNAF---QLAQVGIKtLIIDEYINlfmnfgtgsgfSASS 261
Cdd:cd02537    1 EAYVTLLT--NDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEEsreALEEVGWI-VREVEPID-----------PPDS 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 285812757 262 QSTETKGELNFKWCKLFLfFSLIDrFELICYLSPTCLVLQNIDELLE 308
Cdd:cd02537   67 ANLLKRPRFKDTYTKLRL-WNLTE-YDKVVFLDADTLVLRNIDELFD 111
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
185-308 3.61e-11

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.


Pssm-ID: 133018 [Multi-domain]  Cd Length: 240  Bit Score: 63.05  E-value: 3.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812757 185 RAWITILHdsSAESLQAVIVLAESLKNVNSQYNLWVLHSSEVNAF---QLAQVGIKtLIIDEYINlfmnfgtgsgfSASS 261
Cdd:cd02537    1 EAYVTLLT--NDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEEsreALEEVGWI-VREVEPID-----------PPDS 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 285812757 262 QSTETKGELNFKWCKLFLfFSLIDrFELICYLSPTCLVLQNIDELLE 308
Cdd:cd02537   67 ANLLKRPRFKDTYTKLRL-WNLTE-YDKVVFLDADTLVLRNIDELFD 111
 
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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