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Conserved domains on  [gi|568934465|ref|XP_006504134|]
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dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4 isoform X1 [Mus musculus]

Protein Classification

dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4( domain architecture ID 10562922)

dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4 is the subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ost4 pfam10215
Oligosaccaryltransferase; Ost4 is a very short, approximately 30 residues, enzyme found from ...
1-34 6.31e-10

Oligosaccaryltransferase; Ost4 is a very short, approximately 30 residues, enzyme found from fungi to vertebrates. It is a member of the ER oligosaccaryltansferase complex, EC 2.4.1.119, that catalyzes the asparagine-linked glycosylation of proteins. It appears to be an integral membrane protein that mediates the en bloc transfer of a preassembled high-mannose oligosaccharide onto asparagine residues of nascent polypeptides as they enter the lumen of the rough endoplasmic reticulum (RER).


:

Pssm-ID: 431142  Cd Length: 34  Bit Score: 47.17  E-value: 6.31e-10
                         10        20        30
                 ....*....|....*....|....*....|....
gi 568934465   1 MITDVQLAIFANMLGVSLFLLVVLYHYVAVNNPK 34
Cdd:pfam10215  1 MISDNQLYTLANFLGSAAMLLIVLYHFVEVNAKK 34
 
Name Accession Description Interval E-value
Ost4 pfam10215
Oligosaccaryltransferase; Ost4 is a very short, approximately 30 residues, enzyme found from ...
1-34 6.31e-10

Oligosaccaryltransferase; Ost4 is a very short, approximately 30 residues, enzyme found from fungi to vertebrates. It is a member of the ER oligosaccaryltansferase complex, EC 2.4.1.119, that catalyzes the asparagine-linked glycosylation of proteins. It appears to be an integral membrane protein that mediates the en bloc transfer of a preassembled high-mannose oligosaccharide onto asparagine residues of nascent polypeptides as they enter the lumen of the rough endoplasmic reticulum (RER).


Pssm-ID: 431142  Cd Length: 34  Bit Score: 47.17  E-value: 6.31e-10
                         10        20        30
                 ....*....|....*....|....*....|....
gi 568934465   1 MITDVQLAIFANMLGVSLFLLVVLYHYVAVNNPK 34
Cdd:pfam10215  1 MISDNQLYTLANFLGSAAMLLIVLYHFVEVNAKK 34
 
Name Accession Description Interval E-value
Ost4 pfam10215
Oligosaccaryltransferase; Ost4 is a very short, approximately 30 residues, enzyme found from ...
1-34 6.31e-10

Oligosaccaryltransferase; Ost4 is a very short, approximately 30 residues, enzyme found from fungi to vertebrates. It is a member of the ER oligosaccaryltansferase complex, EC 2.4.1.119, that catalyzes the asparagine-linked glycosylation of proteins. It appears to be an integral membrane protein that mediates the en bloc transfer of a preassembled high-mannose oligosaccharide onto asparagine residues of nascent polypeptides as they enter the lumen of the rough endoplasmic reticulum (RER).


Pssm-ID: 431142  Cd Length: 34  Bit Score: 47.17  E-value: 6.31e-10
                         10        20        30
                 ....*....|....*....|....*....|....
gi 568934465   1 MITDVQLAIFANMLGVSLFLLVVLYHYVAVNNPK 34
Cdd:pfam10215  1 MISDNQLYTLANFLGSAAMLLIVLYHFVEVNAKK 34
 
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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