NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4503365|ref|NP_003854|]
View 

dolichol phosphate-mannose biosynthesis regulatory protein isoform 1 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 2.98e-25

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: 89.20  E-value: 2.98e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503365     5 TDQVVGLGLVAVSLIIFTYYTAWVILLPFIDSQHVIHKYFLPRAYAVAIPLAAGLLLLLFVGLFISYVMLKTKR 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 2.98e-25

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: 89.20  E-value: 2.98e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503365     5 TDQVVGLGLVAVSLIIFTYYTAWVILLPFIDSQHVIHKYFLPRAYAVAIPLAAGLLLLLFVGLFISYVMLKTKR 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 2.98e-25

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: 89.20  E-value: 2.98e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503365     5 TDQVVGLGLVAVSLIIFTYYTAWVILLPFIDSQHVIHKYFLPRAYAVAIPLAAGLLLLLFVGLFISYVMLKTKR 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH