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Conserved domains on  [gi|1844517512|ref|XP_727761|]
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uncharacterized protein PY17X_1249800 [Plasmodium yoelii]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Gpi1 super family cl04893
N-acetylglucosaminyl transferase component (Gpi1); Glycosylphosphatidylinositol (GPI) ...
416-483 3.89e-03

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.


The actual alignment was detected with superfamily member pfam05024:

Pssm-ID: 461527  Cd Length: 273  Bit Score: 39.08  E-value: 3.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844517512 416 IIATILFIILLSLcitFPTVIeIFlgYFAFsyASAAFGCISLIGLIvyEMIISK-----LFKIYRKIVFKYRM 483
Cdd:pfam05024 209 LLGTLLFTILLFL---LPTVL-VF--YLVF--ALLRLAIILVQALL--ETLLALlnhfpLFALLLRLKDPKRL 271
 
Name Accession Description Interval E-value
Gpi1 pfam05024
N-acetylglucosaminyl transferase component (Gpi1); Glycosylphosphatidylinositol (GPI) ...
416-483 3.89e-03

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: 39.08  E-value: 3.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844517512 416 IIATILFIILLSLcitFPTVIeIFlgYFAFsyASAAFGCISLIGLIvyEMIISK-----LFKIYRKIVFKYRM 483
Cdd:pfam05024 209 LLGTLLFTILLFL---LPTVL-VF--YLVF--ALLRLAIILVQALL--ETLLALlnhfpLFALLLRLKDPKRL 271
 
Name Accession Description Interval E-value
Gpi1 pfam05024
N-acetylglucosaminyl transferase component (Gpi1); Glycosylphosphatidylinositol (GPI) ...
416-483 3.89e-03

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: 39.08  E-value: 3.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844517512 416 IIATILFIILLSLcitFPTVIeIFlgYFAFsyASAAFGCISLIGLIvyEMIISK-----LFKIYRKIVFKYRM 483
Cdd:pfam05024 209 LLGTLLFTILLFL---LPTVL-VF--YLVF--ALLRLAIILVQALL--ETLLALlnhfpLFALLLRLKDPKRL 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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