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Conserved domains on  [gi|594064447|ref|XP_006056241|]
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phosphatidylinositol N-acetylglucosaminyltransferase subunit H isoform X2 [Bubalus bubalis]

Protein Classification

PIG-H family GPI synthesis protein( domain architecture ID 10562800)

PIG-H family GPI synthesis protein such as human phosphatidylinositol N-acetylglucosaminyltransferase subunit H, part of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes 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:0017176

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIG-H pfam10181
GPI-GlcNAc transferase complex, PIG-H component; PIG-H is a family of conserved proteins that ...
99-167 1.21e-20

GPI-GlcNAc transferase complex, PIG-H component; PIG-H is a family of conserved proteins that complexes with three other proteins to form the GPI-GnT (glycosylphosphatidylinositol anchor biosynthesis transferase) complex. It appears to be a peripheral membrane protein facing the cytoplasm involved in the first step in GPI anchor formation.


:

Pssm-ID: 462983  Cd Length: 67  Bit Score: 80.96  E-value: 1.21e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594064447   99 TLLIIDSLGIQMTSS-YASGKESTTFIEMDKVKDVIINEAIYM-KVIYYLCILLKDPVEphgiSQVVPIFQ 167
Cdd:pfam10181   1 SLLVIRGLGVQLSTTkYLSGFSSTRFIPLDKIRDIVINEGFRGfQVIFYLAIIVKGEEE----ASLVVVFP 67
 
Name Accession Description Interval E-value
PIG-H pfam10181
GPI-GlcNAc transferase complex, PIG-H component; PIG-H is a family of conserved proteins that ...
99-167 1.21e-20

GPI-GlcNAc transferase complex, PIG-H component; PIG-H is a family of conserved proteins that complexes with three other proteins to form the GPI-GnT (glycosylphosphatidylinositol anchor biosynthesis transferase) complex. It appears to be a peripheral membrane protein facing the cytoplasm involved in the first step in GPI anchor formation.


Pssm-ID: 462983  Cd Length: 67  Bit Score: 80.96  E-value: 1.21e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594064447   99 TLLIIDSLGIQMTSS-YASGKESTTFIEMDKVKDVIINEAIYM-KVIYYLCILLKDPVEphgiSQVVPIFQ 167
Cdd:pfam10181   1 SLLVIRGLGVQLSTTkYLSGFSSTRFIPLDKIRDIVINEGFRGfQVIFYLAIIVKGEEE----ASLVVVFP 67
 
Name Accession Description Interval E-value
PIG-H pfam10181
GPI-GlcNAc transferase complex, PIG-H component; PIG-H is a family of conserved proteins that ...
99-167 1.21e-20

GPI-GlcNAc transferase complex, PIG-H component; PIG-H is a family of conserved proteins that complexes with three other proteins to form the GPI-GnT (glycosylphosphatidylinositol anchor biosynthesis transferase) complex. It appears to be a peripheral membrane protein facing the cytoplasm involved in the first step in GPI anchor formation.


Pssm-ID: 462983  Cd Length: 67  Bit Score: 80.96  E-value: 1.21e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594064447   99 TLLIIDSLGIQMTSS-YASGKESTTFIEMDKVKDVIINEAIYM-KVIYYLCILLKDPVEphgiSQVVPIFQ 167
Cdd:pfam10181   1 SLLVIRGLGVQLSTTkYLSGFSSTRFIPLDKIRDIVINEGFRGfQVIFYLAIIVKGEEE----ASLVVVFP 67
 
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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