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Conserved domains on  [gi|568999025|ref|XP_006523727|]
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phosphatidylinositol N-acetylglucosaminyltransferase subunit Q isoform X1 [Mus musculus]

Protein Classification

phosphatidylinositol N-acetylglucosaminyltransferase subunit Q/GPI1( domain architecture ID 10523437)

phosphatidylinositol N-acetylglucosaminyltransferase subunit Q (PIGQ)/GPI1 is part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis

EC:  2.4.1.198
Gene Ontology:  GO:0006506|GO:0000506
PubMed:  8910381|10373468

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Gpi1 pfam05024
N-acetylglucosaminyl transferase component (Gpi1); Glycosylphosphatidylinositol (GPI) ...
370-569 4.15e-96

N-acetylglucosaminyl transferase component (Gpi1); Glycosylphosphatidylinositol (GPI) represents an important anchoring molecule for cell surface proteins.The first step in its synthesis is the transfer of N-acetylglucosamine (GlcNAc) from UDP-N-acetylglucosamine to phosphatidylinositol (PI). This chemically simple step is genetically complex because three or four genes are required in both yeast (GPI1, GPI2 and GPI3) and mammals (GPI1, PIG A, PIG H and PIG C), respectively.


:

Pssm-ID: 461527  Cd Length: 273  Bit Score: 296.01  E-value: 4.15e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999025  370 ELGERRVAEELQHLLQWLMGAPAGLKMNRALDQVLGRFFLYHIHLWISYIHLMSPFIEHILWHVGLSACLGLTVALSIFS 449
Cdd:pfam05024  72 KLLREYLVDLLKKLLEWLMGNPAGLKLNTELNSFLGDLFLWIIDLWSTFLFILTPFLPLLLRLLGFSGFLGASFALSLLS 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999025  450 DIIALLTFHIYCFYVYGARLYCLKIYGLSSLWRLFRGKKWNVLRQRVDSCSYDLDQLFIGTLLFTILVFLLPTTALYYLV 529
Cdd:pfam05024 152 DLLSLLTLHIYCFYVISARLYRWQLQILGSLFRLFRGKKRNVLRNRVDSCDYDLDQLLLGTLLFTILLFLLPTVLVFYLV 231
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568999025  530 FTLLRLLVITVQGLIHLLVDLINSLPLYSLGLRLCRPYRL 569
Cdd:pfam05024 232 FALLRLAIILVQALLETLLALLNHFPLFALLLRLKDPKRL 271
 
Name Accession Description Interval E-value
Gpi1 pfam05024
N-acetylglucosaminyl transferase component (Gpi1); Glycosylphosphatidylinositol (GPI) ...
370-569 4.15e-96

N-acetylglucosaminyl transferase component (Gpi1); Glycosylphosphatidylinositol (GPI) represents an important anchoring molecule for cell surface proteins.The first step in its synthesis is the transfer of N-acetylglucosamine (GlcNAc) from UDP-N-acetylglucosamine to phosphatidylinositol (PI). This chemically simple step is genetically complex because three or four genes are required in both yeast (GPI1, GPI2 and GPI3) and mammals (GPI1, PIG A, PIG H and PIG C), respectively.


Pssm-ID: 461527  Cd Length: 273  Bit Score: 296.01  E-value: 4.15e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999025  370 ELGERRVAEELQHLLQWLMGAPAGLKMNRALDQVLGRFFLYHIHLWISYIHLMSPFIEHILWHVGLSACLGLTVALSIFS 449
Cdd:pfam05024  72 KLLREYLVDLLKKLLEWLMGNPAGLKLNTELNSFLGDLFLWIIDLWSTFLFILTPFLPLLLRLLGFSGFLGASFALSLLS 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999025  450 DIIALLTFHIYCFYVYGARLYCLKIYGLSSLWRLFRGKKWNVLRQRVDSCSYDLDQLFIGTLLFTILVFLLPTTALYYLV 529
Cdd:pfam05024 152 DLLSLLTLHIYCFYVISARLYRWQLQILGSLFRLFRGKKRNVLRNRVDSCDYDLDQLLLGTLLFTILLFLLPTVLVFYLV 231
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568999025  530 FTLLRLLVITVQGLIHLLVDLINSLPLYSLGLRLCRPYRL 569
Cdd:pfam05024 232 FALLRLAIILVQALLETLLALLNHFPLFALLLRLKDPKRL 271
 
Name Accession Description Interval E-value
Gpi1 pfam05024
N-acetylglucosaminyl transferase component (Gpi1); Glycosylphosphatidylinositol (GPI) ...
370-569 4.15e-96

N-acetylglucosaminyl transferase component (Gpi1); Glycosylphosphatidylinositol (GPI) represents an important anchoring molecule for cell surface proteins.The first step in its synthesis is the transfer of N-acetylglucosamine (GlcNAc) from UDP-N-acetylglucosamine to phosphatidylinositol (PI). This chemically simple step is genetically complex because three or four genes are required in both yeast (GPI1, GPI2 and GPI3) and mammals (GPI1, PIG A, PIG H and PIG C), respectively.


Pssm-ID: 461527  Cd Length: 273  Bit Score: 296.01  E-value: 4.15e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999025  370 ELGERRVAEELQHLLQWLMGAPAGLKMNRALDQVLGRFFLYHIHLWISYIHLMSPFIEHILWHVGLSACLGLTVALSIFS 449
Cdd:pfam05024  72 KLLREYLVDLLKKLLEWLMGNPAGLKLNTELNSFLGDLFLWIIDLWSTFLFILTPFLPLLLRLLGFSGFLGASFALSLLS 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999025  450 DIIALLTFHIYCFYVYGARLYCLKIYGLSSLWRLFRGKKWNVLRQRVDSCSYDLDQLFIGTLLFTILVFLLPTTALYYLV 529
Cdd:pfam05024 152 DLLSLLTLHIYCFYVISARLYRWQLQILGSLFRLFRGKKRNVLRNRVDSCDYDLDQLLLGTLLFTILLFLLPTVLVFYLV 231
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568999025  530 FTLLRLLVITVQGLIHLLVDLINSLPLYSLGLRLCRPYRL 569
Cdd:pfam05024 232 FALLRLAIILVQALLETLLALLNHFPLFALLLRLKDPKRL 271
 
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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