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Conserved domains on  [gi|46240862|ref|NP_079265|]
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GPI inositol-deacylase isoform 1 [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 ...
82-302 3.38e-102

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: 317.77  E-value: 3.38e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46240862    82 PLTGIPVLFLPGNAGSYKQVRSIGSIA------LRKAEDIDFKYHFDFFSVNFNEELVALYGGSLQKQTKFVHECIKTIL 155
Cdd:pfam07819   1 ELSGIPVLFIPGNAGSYKQVRSIASVAanlyqvLRKLLQNDNGFHLDFFSVDFNEELSAFHGRTLLDQAEYLNDAIRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46240862   156 KLYKGQEFAPKSVAIIGHSMGGLVARALLTLKNFKHDLINLLITQATPHVAPVMPLDRFITDFYTTVNNYWILNARHI-- 233
Cdd:pfam07819  81 SLYASGRPGPTSVILIGHSMGGIVARAALTLPNYIPQSVNTIITLSSPHAKPPLTFDGDILKFYERLNAFWRKLYNDGds 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46240862   234 ----NLTTLSVAGGFRDYQVRSGLTFLPKLSHHTSALSVVSSAVPKTWVSTDHLSIVWCKQLQLTTVRAFFDL 302
Cdd:pfam07819 161 nnlsNVLLVSITGGIRDYMVPDDYTSLEGLVPSTNGLSVFTSAIPDVWTSIDHLAIVWCNQLRRVVARALFEY 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 ...
82-302 3.38e-102

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: 317.77  E-value: 3.38e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46240862    82 PLTGIPVLFLPGNAGSYKQVRSIGSIA------LRKAEDIDFKYHFDFFSVNFNEELVALYGGSLQKQTKFVHECIKTIL 155
Cdd:pfam07819   1 ELSGIPVLFIPGNAGSYKQVRSIASVAanlyqvLRKLLQNDNGFHLDFFSVDFNEELSAFHGRTLLDQAEYLNDAIRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46240862   156 KLYKGQEFAPKSVAIIGHSMGGLVARALLTLKNFKHDLINLLITQATPHVAPVMPLDRFITDFYTTVNNYWILNARHI-- 233
Cdd:pfam07819  81 SLYASGRPGPTSVILIGHSMGGIVARAALTLPNYIPQSVNTIITLSSPHAKPPLTFDGDILKFYERLNAFWRKLYNDGds 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46240862   234 ----NLTTLSVAGGFRDYQVRSGLTFLPKLSHHTSALSVVSSAVPKTWVSTDHLSIVWCKQLQLTTVRAFFDL 302
Cdd:pfam07819 161 nnlsNVLLVSITGGIRDYMVPDDYTSLEGLVPSTNGLSVFTSAIPDVWTSIDHLAIVWCNQLRRVVARALFEY 233
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
84-204 1.58e-10

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 58.69  E-value: 1.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46240862  84 TGIPVLFLPGNAGSYKQVRSIGSiALRKAedidfkyHFDFFSVNFNeelvaLYGGSLQKQTKFVHECIKTILKLYKGQEf 163
Cdd:COG1075   4 TRYPVVLVHGLGGSAASWAPLAP-RLRAA-------GYPVYALNYP-----STNGSIEDSAEQLAAFVDAVLAATGAEK- 69
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 46240862 164 apksVAIIGHSMGGLVARALLTlKNFKHDLINLLITQATPH 204
Cdd:COG1075  70 ----VDLVGHSMGGLVARYYLK-RLGGAAKVARVVTLGTPH 105
 
Name Accession Description Interval E-value
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
82-302 3.38e-102

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: 317.77  E-value: 3.38e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46240862    82 PLTGIPVLFLPGNAGSYKQVRSIGSIA------LRKAEDIDFKYHFDFFSVNFNEELVALYGGSLQKQTKFVHECIKTIL 155
Cdd:pfam07819   1 ELSGIPVLFIPGNAGSYKQVRSIASVAanlyqvLRKLLQNDNGFHLDFFSVDFNEELSAFHGRTLLDQAEYLNDAIRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46240862   156 KLYKGQEFAPKSVAIIGHSMGGLVARALLTLKNFKHDLINLLITQATPHVAPVMPLDRFITDFYTTVNNYWILNARHI-- 233
Cdd:pfam07819  81 SLYASGRPGPTSVILIGHSMGGIVARAALTLPNYIPQSVNTIITLSSPHAKPPLTFDGDILKFYERLNAFWRKLYNDGds 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46240862   234 ----NLTTLSVAGGFRDYQVRSGLTFLPKLSHHTSALSVVSSAVPKTWVSTDHLSIVWCKQLQLTTVRAFFDL 302
Cdd:pfam07819 161 nnlsNVLLVSITGGIRDYMVPDDYTSLEGLVPSTNGLSVFTSAIPDVWTSIDHLAIVWCNQLRRVVARALFEY 233
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
84-204 1.58e-10

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 58.69  E-value: 1.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46240862  84 TGIPVLFLPGNAGSYKQVRSIGSiALRKAedidfkyHFDFFSVNFNeelvaLYGGSLQKQTKFVHECIKTILKLYKGQEf 163
Cdd:COG1075   4 TRYPVVLVHGLGGSAASWAPLAP-RLRAA-------GYPVYALNYP-----STNGSIEDSAEQLAAFVDAVLAATGAEK- 69
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 46240862 164 apksVAIIGHSMGGLVARALLTlKNFKHDLINLLITQATPH 204
Cdd:COG1075  70 ----VDLVGHSMGGLVARYYLK-RLGGAAKVARVVTLGTPH 105
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
87-212 9.18e-03

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 39.02  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46240862    87 PVLFLPGNAGSYKQVRSIgsiaLRKAEDIDFKYH-FDFFSVNFNEELVALYGGSlqkqTKFVHECIKTILKLYKGQEfap 165
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKL----APALARDGFRVIaLDLRGFGKSSRPKAQDDYR----TDDLAEDLEYILEALGLEK--- 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 46240862   166 ksVAIIGHSMGGLVARALLTLKNfkhDLINLLITQATPHVAPVMPLD 212
Cdd:pfam00561  71 --VNLVGHSMGGLIALAYAAKYP---DRVKALVLLGALDPPHELDEA 112
 
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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