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Conserved domains on  [gi|1034616779|ref|XP_016860482|]
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GPI inositol-deacylase isoform X1 [Homo sapiens]

Protein Classification

GPI inositol-deacylase( domain architecture ID 10544848)

GPI inositol-deacylase is involved in inositol deacylation of GPI-anchored proteins

CATH:  3.40.50.1820
EC:  3.1.-.-
Gene Ontology:  GO:0016788
PubMed:  19508187|12369917
SCOP:  3000102

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 1-128 4.27e-48

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


:

Pssm-ID: 369540  Cd Length: 233  Bit Score: 169.85  E-value: 4.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616779   1 MGGLVARALLTLKNFKHDLINLLITQATPHVAPVMPLDRFITDFYTTVNNYWILNARHI------NLTTLSVAGGFRDYQ 74
Cdd:pfam07819 100 MGGIVARAALTLPNYIPQSVNTIITLSSPHAKPPLTFDGDILKFYERLNAFWRKLYNDGdsnnlsNVLLVSITGGIRDYM 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034616779  75 VRSGLTFLPKLSHHTSALSVVSSAVPKTWVSTDHLSIVWCKQLQLTTVRAFFDL 128
Cdd:pfam07819 180 VPDDYTSLEGLVPSTNGLSVFTSAIPDVWTSIDHLAIVWCNQLRRVVARALFEY 233
 
Name Accession Description Interval E-value
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 1-128 4.27e-48

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


Pssm-ID: 369540  Cd Length: 233  Bit Score: 169.85  E-value: 4.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616779   1 MGGLVARALLTLKNFKHDLINLLITQATPHVAPVMPLDRFITDFYTTVNNYWILNARHI------NLTTLSVAGGFRDYQ 74
Cdd:pfam07819 100 MGGIVARAALTLPNYIPQSVNTIITLSSPHAKPPLTFDGDILKFYERLNAFWRKLYNDGdsnnlsNVLLVSITGGIRDYM 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034616779  75 VRSGLTFLPKLSHHTSALSVVSSAVPKTWVSTDHLSIVWCKQLQLTTVRAFFDL 128
Cdd:pfam07819 180 VPDDYTSLEGLVPSTNGLSVFTSAIPDVWTSIDHLAIVWCNQLRRVVARALFEY 233
 
Name Accession Description Interval E-value
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 1-128 4.27e-48

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


Pssm-ID: 369540  Cd Length: 233  Bit Score: 169.85  E-value: 4.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616779   1 MGGLVARALLTLKNFKHDLINLLITQATPHVAPVMPLDRFITDFYTTVNNYWILNARHI------NLTTLSVAGGFRDYQ 74
Cdd:pfam07819 100 MGGIVARAALTLPNYIPQSVNTIITLSSPHAKPPLTFDGDILKFYERLNAFWRKLYNDGdsnnlsNVLLVSITGGIRDYM 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034616779  75 VRSGLTFLPKLSHHTSALSVVSSAVPKTWVSTDHLSIVWCKQLQLTTVRAFFDL 128
Cdd:pfam07819 180 VPDDYTSLEGLVPSTNGLSVFTSAIPDVWTSIDHLAIVWCNQLRRVVARALFEY 233
 
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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