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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

DPM2 domain-containing protein (domain architecture ID 10538127)

DPM2 domain-containing protein

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 2.24e-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: 399936  Cd Length: 76  Bit Score: 84.20  E-value: 2.24e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6753672     5 TDQAVGFGLVAVSLIIFTYYTTWVILLPFIDSQHVIHKYFLPRAYAVLLPLAAGLLLLLFVGLFITYVMLKSQK 78
Cdd:pfam07297  1 SDRLVGLLLLAVALSVFTYYTIWVIVLPFVDDDHPIHSYFLPREYAIRIPVILLVVGLSFVGTFIGLVMIKSKK 74
 
Name Accession Description Interval E-value
DPM2 pfam07297
Dolichol phosphate-mannose biosynthesis regulatory protein (DPM2); This family consists of ...
5-78 2.24e-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: 399936  Cd Length: 76  Bit Score: 84.20  E-value: 2.24e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6753672     5 TDQAVGFGLVAVSLIIFTYYTTWVILLPFIDSQHVIHKYFLPRAYAVLLPLAAGLLLLLFVGLFITYVMLKSQK 78
Cdd:pfam07297  1 SDRLVGLLLLAVALSVFTYYTIWVIVLPFVDDDHPIHSYFLPREYAIRIPVILLVVGLSFVGTFIGLVMIKSKK 74
 
Name Accession Description Interval E-value
DPM2 pfam07297
Dolichol phosphate-mannose biosynthesis regulatory protein (DPM2); This family consists of ...
5-78 2.24e-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: 399936  Cd Length: 76  Bit Score: 84.20  E-value: 2.24e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6753672     5 TDQAVGFGLVAVSLIIFTYYTTWVILLPFIDSQHVIHKYFLPRAYAVLLPLAAGLLLLLFVGLFITYVMLKSQK 78
Cdd:pfam07297  1 SDRLVGLLLLAVALSVFTYYTIWVIVLPFVDDDHPIHSYFLPREYAIRIPVILLVVGLSFVGTFIGLVMIKSKK 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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