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Conserved domains on  [gi|1394198839|ref|NP_001350858|]
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phosphatidylinositol glycan anchor biosynthesis class C, isoform C [Drosophila melanogaster]

Protein Classification

phosphatidylinositol N-acetylglucosaminyltransferase subunit C family protein( domain architecture ID 10534078)

phosphatidylinositol N-acetylglucosaminyltransferase subunit C (PIGC) family protein is a subunit of the protein complex which catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of glycosylphosphatidylinositol (GPI) biosynthesis in eukaryotes

Gene Ontology:  GO:0006506|GO:0000506
PubMed:  8806613

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
GPI2 pfam06432
Phosphatidylinositol N-acetylglucosaminyltransferase; Glycosylphosphatidylinositol (GPI) ...
12-270 3.52e-89

Phosphatidylinositol N-acetylglucosaminyltransferase; 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 step involves products of three or four genes in both yeast (GPI1, GPI2 and GPI3) and mammals (GPI1, PIG A, PIG H and PIG C), respectively.


:

Pssm-ID: 428940  Cd Length: 267  Bit Score: 267.12  E-value: 3.52e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394198839  12 WVKNLYSNREYPDNYTDASFLKDLRTNLHCRIYTFGEAIAGITVLNNQISCITGFLILYQLMLSDSVSPTTILVPSCGIT 91
Cdd:pfam06432   1 WKKVLYEKQPYPDNYTDETFLEELRRNPNVRPYDYWPLVADSLVISQHLSSVVIFVLVFVYIYQGRLSPVSLVLISSVLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394198839  92 GIGYLCYRGRSLSWALLG--EDSKTLVTVVLFGYLFSPMLHTLTQAISTDTIYTMTFFVLLGNLIFGHYGLDVAMVSKAV 169
Cdd:pfam06432  81 LLGYILWDLWVGQPRRSSrlKTLKSAILIFFTLLGLSPVLKTLTKSTSSDSIWALSFWLLLLHLFFHDYSYGNAKLSSSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394198839 170 SLNAAIFGAICLASRLPTSYHAFVLLVEAAVFFVLYPIM------TEANWHAGFMLPIFAICCMALYCISRPVLYLYAST 243
Cdd:pfam06432 161 STNAALFASVVLASRLPSTLHVFALLLFSIELFALFPIFrrslrhRSWRLHVVLTLALVLLASGLLGSLSGTLAVLYLLL 240
                         250       260
                  ....*....|....*....|....*..
gi 1394198839 244 TIFINFVCPFIFVWQQQYKFNIHGPWD 270
Cdd:pfam06432 241 VLFITFVCPWWLIRLQKYKNEIHGPWD 267
 
Name Accession Description Interval E-value
GPI2 pfam06432
Phosphatidylinositol N-acetylglucosaminyltransferase; Glycosylphosphatidylinositol (GPI) ...
12-270 3.52e-89

Phosphatidylinositol N-acetylglucosaminyltransferase; 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 step involves products of three or four genes in both yeast (GPI1, GPI2 and GPI3) and mammals (GPI1, PIG A, PIG H and PIG C), respectively.


Pssm-ID: 428940  Cd Length: 267  Bit Score: 267.12  E-value: 3.52e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394198839  12 WVKNLYSNREYPDNYTDASFLKDLRTNLHCRIYTFGEAIAGITVLNNQISCITGFLILYQLMLSDSVSPTTILVPSCGIT 91
Cdd:pfam06432   1 WKKVLYEKQPYPDNYTDETFLEELRRNPNVRPYDYWPLVADSLVISQHLSSVVIFVLVFVYIYQGRLSPVSLVLISSVLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394198839  92 GIGYLCYRGRSLSWALLG--EDSKTLVTVVLFGYLFSPMLHTLTQAISTDTIYTMTFFVLLGNLIFGHYGLDVAMVSKAV 169
Cdd:pfam06432  81 LLGYILWDLWVGQPRRSSrlKTLKSAILIFFTLLGLSPVLKTLTKSTSSDSIWALSFWLLLLHLFFHDYSYGNAKLSSSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394198839 170 SLNAAIFGAICLASRLPTSYHAFVLLVEAAVFFVLYPIM------TEANWHAGFMLPIFAICCMALYCISRPVLYLYAST 243
Cdd:pfam06432 161 STNAALFASVVLASRLPSTLHVFALLLFSIELFALFPIFrrslrhRSWRLHVVLTLALVLLASGLLGSLSGTLAVLYLLL 240
                         250       260
                  ....*....|....*....|....*..
gi 1394198839 244 TIFINFVCPFIFVWQQQYKFNIHGPWD 270
Cdd:pfam06432 241 VLFITFVCPWWLIRLQKYKNEIHGPWD 267
 
Name Accession Description Interval E-value
GPI2 pfam06432
Phosphatidylinositol N-acetylglucosaminyltransferase; Glycosylphosphatidylinositol (GPI) ...
12-270 3.52e-89

Phosphatidylinositol N-acetylglucosaminyltransferase; 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 step involves products of three or four genes in both yeast (GPI1, GPI2 and GPI3) and mammals (GPI1, PIG A, PIG H and PIG C), respectively.


Pssm-ID: 428940  Cd Length: 267  Bit Score: 267.12  E-value: 3.52e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394198839  12 WVKNLYSNREYPDNYTDASFLKDLRTNLHCRIYTFGEAIAGITVLNNQISCITGFLILYQLMLSDSVSPTTILVPSCGIT 91
Cdd:pfam06432   1 WKKVLYEKQPYPDNYTDETFLEELRRNPNVRPYDYWPLVADSLVISQHLSSVVIFVLVFVYIYQGRLSPVSLVLISSVLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394198839  92 GIGYLCYRGRSLSWALLG--EDSKTLVTVVLFGYLFSPMLHTLTQAISTDTIYTMTFFVLLGNLIFGHYGLDVAMVSKAV 169
Cdd:pfam06432  81 LLGYILWDLWVGQPRRSSrlKTLKSAILIFFTLLGLSPVLKTLTKSTSSDSIWALSFWLLLLHLFFHDYSYGNAKLSSSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394198839 170 SLNAAIFGAICLASRLPTSYHAFVLLVEAAVFFVLYPIM------TEANWHAGFMLPIFAICCMALYCISRPVLYLYAST 243
Cdd:pfam06432 161 STNAALFASVVLASRLPSTLHVFALLLFSIELFALFPIFrrslrhRSWRLHVVLTLALVLLASGLLGSLSGTLAVLYLLL 240
                         250       260
                  ....*....|....*....|....*..
gi 1394198839 244 TIFINFVCPFIFVWQQQYKFNIHGPWD 270
Cdd:pfam06432 241 VLFITFVCPWWLIRLQKYKNEIHGPWD 267
 
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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