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Conserved domains on  [gi|6753672|ref|NP_034203|]
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dolichol phosphate-mannose biosynthesis regulatory protein [Mus musculus]

Protein Classification

dolichol phosphate-mannose biosynthesis regulatory protein( domain architecture ID 10538127)

dolichol phosphate-mannose biosynthesis regulatory protein (DPM2) regulates the biosynthesis of dolichol phosphate-mannose

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPM2 pfam07297
Dolichol phosphate-mannose biosynthesis regulatory protein (DPM2); This family consists of ...
 5-78 1.98e-23

Dolichol phosphate-mannose biosynthesis regulatory protein (DPM2); This family consists of several eukaryotic dolichol phosphate-mannose biosynthesis regulatory (DPM2) proteins. Biosynthesis of glycosylphosphatidylinositol and N-glycan precursor is dependent upon a mannosyl donor, dolichol phosphate-mannose (DPM). DPM2, an 84 amino acid membrane protein expressed in the endoplasmic reticulum (ER), makes a complex with DPM1 that is essential for the ER localization and stable expression of DPM1. Moreover, DPM2 enhances binding of dolichol phosphate, a substrate of DPM synthase. Biosynthesis of DPM in mammalian cells is regulated by DPM2.


:

Pssm-ID: 462138  Cd Length: 75  Bit Score: 84.58  E-value: 1.98e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6753672     5 TDQAVGFGLVAVSLIIFTYYTTWVILLPFIDSQHVIHKYFLPRAYAVLLPLAAGLLLLLFVGLFITYVMLKSQK 78
Cdd:pfam07297  1 SDRLVGLLLLATALSVFTYYTVWVIVLPFVDDDHPIHSYFLPREYAIRIPVILLVVGLSFVGTFIGLVMIKSKK 74
 
Name Accession Description Interval E-value
DPM2 pfam07297
Dolichol phosphate-mannose biosynthesis regulatory protein (DPM2); This family consists of ...
 5-78 1.98e-23

Dolichol phosphate-mannose biosynthesis regulatory protein (DPM2); This family consists of several eukaryotic dolichol phosphate-mannose biosynthesis regulatory (DPM2) proteins. Biosynthesis of glycosylphosphatidylinositol and N-glycan precursor is dependent upon a mannosyl donor, dolichol phosphate-mannose (DPM). DPM2, an 84 amino acid membrane protein expressed in the endoplasmic reticulum (ER), makes a complex with DPM1 that is essential for the ER localization and stable expression of DPM1. Moreover, DPM2 enhances binding of dolichol phosphate, a substrate of DPM synthase. Biosynthesis of DPM in mammalian cells is regulated by DPM2.


Pssm-ID: 462138  Cd Length: 75  Bit Score: 84.58  E-value: 1.98e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6753672     5 TDQAVGFGLVAVSLIIFTYYTTWVILLPFIDSQHVIHKYFLPRAYAVLLPLAAGLLLLLFVGLFITYVMLKSQK 78
Cdd:pfam07297  1 SDRLVGLLLLATALSVFTYYTVWVIVLPFVDDDHPIHSYFLPREYAIRIPVILLVVGLSFVGTFIGLVMIKSKK 74
 
Name Accession Description Interval E-value
DPM2 pfam07297
Dolichol phosphate-mannose biosynthesis regulatory protein (DPM2); This family consists of ...
 5-78 1.98e-23

Dolichol phosphate-mannose biosynthesis regulatory protein (DPM2); This family consists of several eukaryotic dolichol phosphate-mannose biosynthesis regulatory (DPM2) proteins. Biosynthesis of glycosylphosphatidylinositol and N-glycan precursor is dependent upon a mannosyl donor, dolichol phosphate-mannose (DPM). DPM2, an 84 amino acid membrane protein expressed in the endoplasmic reticulum (ER), makes a complex with DPM1 that is essential for the ER localization and stable expression of DPM1. Moreover, DPM2 enhances binding of dolichol phosphate, a substrate of DPM synthase. Biosynthesis of DPM in mammalian cells is regulated by DPM2.


Pssm-ID: 462138  Cd Length: 75  Bit Score: 84.58  E-value: 1.98e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6753672     5 TDQAVGFGLVAVSLIIFTYYTTWVILLPFIDSQHVIHKYFLPRAYAVLLPLAAGLLLLLFVGLFITYVMLKSQK 78
Cdd:pfam07297  1 SDRLVGLLLLATALSVFTYYTVWVIVLPFVDDDHPIHSYFLPREYAIRIPVILLVVGLSFVGTFIGLVMIKSKK 74
 
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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