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Conserved domains on  [gi|91701345|gb|ABE41673|]
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O-mannosyl N-acetylglucosaminyltransferase, partial [Dolichotis patagonum]

Protein Classification

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 ...
1-35 9.94e-06

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 cd02514:

Pssm-ID: 472172  Cd Length: 334  Bit Score: 39.23  E-value: 9.94e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 91701345   1 FVPDTEGHIYVAFIqmeKEDDFTTWTQ-LAKCLHIW 35
Cdd:cd02514 274 FVPDTEGKVRVVYT---GRDDFKTWAKaFGVMDDLK 306
 
Name Accession Description Interval E-value
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
1-35 9.94e-06

GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13.


Pssm-ID: 133007  Cd Length: 334  Bit Score: 39.23  E-value: 9.94e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 91701345   1 FVPDTEGHIYVAFIqmeKEDDFTTWTQ-LAKCLHIW 35
Cdd:cd02514 274 FVPDTEGKVRVVYT---GRDDFKTWAKaFGVMDDLK 306
 
Name Accession Description Interval E-value
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
1-35 9.94e-06

GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13.


Pssm-ID: 133007  Cd Length: 334  Bit Score: 39.23  E-value: 9.94e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 91701345   1 FVPDTEGHIYVAFIqmeKEDDFTTWTQ-LAKCLHIW 35
Cdd:cd02514 274 FVPDTEGKVRVVYT---GRDDFKTWAKaFGVMDDLK 306
 
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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