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Conserved domains on  [gi|6323937|ref|NP_014008|]
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N-acetylglucosaminylphosphatidylinositol deacetylase [Saccharomyces cerevisiae S288C]

Protein Classification

PIG-L family deacetylase( domain architecture ID 10495428)

PIG-L (phosphatidylinositol glycan class L) family deacetylase catalyzes the removal of an acetyl group from a specific acetylated substrate; similar to Homo sapiens N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase

CATH:  3.40.50.10320
EC:  3.5.1.-
Gene Ontology:  GO:0006506|GO:0000225
PubMed:  24970229
SCOP:  4001164

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PIG-L pfam02585
GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an ...
59-183 3.88e-17

GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an N-acetylglucosaminylphosphatidylinositol de-N-acetylase (EC:3.5.1.89) that catalyzes the second step in GPI biosynthesis.


:

Pssm-ID: 426852  Cd Length: 128  Bit Score: 76.18  E-value: 3.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323937     59 LVIAHPDDEVMFFSPIISQLNSYFPRTVpfnIICLSKGNA----------EGLGETRVRELNESAALLlhneRAVSVQVM 128
Cdd:pfam02585   2 VVSAHPDDEELGAGGTIARLAAAGVEVH---VVCLTDGEAgsgggsleegEELGEIRRAEARAAAEIL----GVDDVEFL 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6323937    129 DFQDGMDEIWDIDSITSSLsQKIdIKNHNlNQIIVTFDSYGVsNHINHKSCYAAV 183
Cdd:pfam02585  75 DYPDGGLEYWDLEELLDAL-ADL-IRRYR-PDVVVTPDPDGG-GHPDHRATGRAV 125
 
Name Accession Description Interval E-value
PIG-L pfam02585
GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an ...
59-183 3.88e-17

GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an N-acetylglucosaminylphosphatidylinositol de-N-acetylase (EC:3.5.1.89) that catalyzes the second step in GPI biosynthesis.


Pssm-ID: 426852  Cd Length: 128  Bit Score: 76.18  E-value: 3.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323937     59 LVIAHPDDEVMFFSPIISQLNSYFPRTVpfnIICLSKGNA----------EGLGETRVRELNESAALLlhneRAVSVQVM 128
Cdd:pfam02585   2 VVSAHPDDEELGAGGTIARLAAAGVEVH---VVCLTDGEAgsgggsleegEELGEIRRAEARAAAEIL----GVDDVEFL 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6323937    129 DFQDGMDEIWDIDSITSSLsQKIdIKNHNlNQIIVTFDSYGVsNHINHKSCYAAV 183
Cdd:pfam02585  75 DYPDGGLEYWDLEELLDAL-ADL-IRRYR-PDVVVTPDPDGG-GHPDHRATGRAV 125
LmbE COG2120
N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];
59-196 2.82e-06

N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];


Pssm-ID: 441723 [Multi-domain]  Cd Length: 201  Bit Score: 47.23  E-value: 2.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323937   59 LVI-AHPDDEVMFFSPIISQLNSyfpRTVPFNIICLSKGNA---------EGLGETRVRELNESAALLlhneRAVSVQVM 128
Cdd:COG2120   3 LVVaAHPDDEELGCGGTIARLAA---AGHEVTVVTLTDGEAgspggpplrEELAEIRRAEARAAAAIL----GVSDVEFL 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323937  129 DFQDGMDEiWDIDSITSSLSQKI-DIKNHnlnqIIVTFDSYGvsNHINHKSCYAAVKKLVDDYAQPKTK 196
Cdd:COG2120  76 GYPDGGLE-GPLEELRRALARLIrEVRPD----VVLTPDPGD--GHPDHRAVGRAVLAAARLAGLPKIL 137
 
Name Accession Description Interval E-value
PIG-L pfam02585
GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an ...
59-183 3.88e-17

GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an N-acetylglucosaminylphosphatidylinositol de-N-acetylase (EC:3.5.1.89) that catalyzes the second step in GPI biosynthesis.


Pssm-ID: 426852  Cd Length: 128  Bit Score: 76.18  E-value: 3.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323937     59 LVIAHPDDEVMFFSPIISQLNSYFPRTVpfnIICLSKGNA----------EGLGETRVRELNESAALLlhneRAVSVQVM 128
Cdd:pfam02585   2 VVSAHPDDEELGAGGTIARLAAAGVEVH---VVCLTDGEAgsgggsleegEELGEIRRAEARAAAEIL----GVDDVEFL 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6323937    129 DFQDGMDEIWDIDSITSSLsQKIdIKNHNlNQIIVTFDSYGVsNHINHKSCYAAV 183
Cdd:pfam02585  75 DYPDGGLEYWDLEELLDAL-ADL-IRRYR-PDVVVTPDPDGG-GHPDHRATGRAV 125
LmbE COG2120
N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];
59-196 2.82e-06

N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];


Pssm-ID: 441723 [Multi-domain]  Cd Length: 201  Bit Score: 47.23  E-value: 2.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323937   59 LVI-AHPDDEVMFFSPIISQLNSyfpRTVPFNIICLSKGNA---------EGLGETRVRELNESAALLlhneRAVSVQVM 128
Cdd:COG2120   3 LVVaAHPDDEELGCGGTIARLAA---AGHEVTVVTLTDGEAgspggpplrEELAEIRRAEARAAAAIL----GVSDVEFL 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323937  129 DFQDGMDEiWDIDSITSSLSQKI-DIKNHnlnqIIVTFDSYGvsNHINHKSCYAAVKKLVDDYAQPKTK 196
Cdd:COG2120  76 GYPDGGLE-GPLEELRRALARLIrEVRPD----VVLTPDPGD--GHPDHRAVGRAVLAAARLAGLPKIL 137
 
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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