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Conserved domains on  [gi|1720365023|ref|XP_030101613|]
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UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like protein 1 isoform X3 [Mus musculus]

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 ...
9-134 3.07e-97

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 cd06913:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 219  Bit Score: 283.58  E-value: 3.07e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365023   9 DDVMMPQRVRMQYEAAGQHPTSIIGCQVRRDPPDSTERYTRWINHLTSDQLLTQVFTSHGPTVIMPTWFCSRAWFSHVGP 88
Cdd:cd06913    94 DDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPTWFCSREWFSHVGP 173
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720365023  89 FDEGGQGVPEDLLFFYEHLRKGGGVFRVDHSLLLYRYHLYAATHSV 134
Cdd:cd06913   174 FDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
 
Name Accession Description Interval E-value
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
9-134 3.07e-97

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 283.58  E-value: 3.07e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365023   9 DDVMMPQRVRMQYEAAGQHPTSIIGCQVRRDPPDSTERYTRWINHLTSDQLLTQVFTSHGPTVIMPTWFCSRAWFSHVGP 88
Cdd:cd06913    94 DDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPTWFCSREWFSHVGP 173
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720365023  89 FDEGGQGVPEDLLFFYEHLRKGGGVFRVDHSLLLYRYHLYAATHSV 134
Cdd:cd06913   174 FDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
 
Name Accession Description Interval E-value
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
9-134 3.07e-97

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 283.58  E-value: 3.07e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365023   9 DDVMMPQRVRMQYEAAGQHPTSIIGCQVRRDPPDSTERYTRWINHLTSDQLLTQVFTSHGPTVIMPTWFCSRAWFSHVGP 88
Cdd:cd06913    94 DDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPTWFCSREWFSHVGP 173
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720365023  89 FDEGGQGVPEDLLFFYEHLRKGGGVFRVDHSLLLYRYHLYAATHSV 134
Cdd:cd06913   174 FDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
 
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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