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Conserved domains on  [gi|296080768|ref|NP_001171676|]
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platelet-activating factor acetylhydrolase IB subunit alpha2 isoform c [Homo sapiens]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 85)

SGNH/GDSL hydrolase family protein is a hydrolytic enzyme such as an esterase or lipase; may have multifunctional properties including broad substrate specificity and regiospecificity; similar to plant GDSL esterase/lipase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SGNH_hydrolase super family cl01053
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 8-139 2.46e-74

SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


The actual alignment was detected with superfamily member cd01820:

Pssm-ID: 470049  Cd Length: 214  Bit Score: 221.01  E-value: 2.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080768   8 PAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQY--EIWRELFSPLHALNFGIGGDTTRHVLWRL 85
Cdd:cd01820    1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296080768  86 KNGELENIKPKVIVVWVGTNNHENT--AEEVAGGIEAIVQLINTRQPQAKIIVLII 139
Cdd:cd01820   81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEEIREKLPNAKILLLGL 136
 
Name Accession Description Interval E-value
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 8-139 2.46e-74

PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor (PAF) and PAF-AH are key players in inflammation and in atherosclerosis. PAF-AH is a calcium independent phospholipase A2 which exhibits strong substrate specificity towards PAF, hydrolyzing an acetyl ester at the sn-2 position. PAF-AH also degrades a family of oxidized PAF-like phospholipids with short sn-2 residues. In addition, PAF and PAF-AH are associated with neural migration and mammalian reproduction.


Pssm-ID: 238858  Cd Length: 214  Bit Score: 221.01  E-value: 2.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080768   8 PAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQY--EIWRELFSPLHALNFGIGGDTTRHVLWRL 85
Cdd:cd01820    1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296080768  86 KNGELENIKPKVIVVWVGTNNHENT--AEEVAGGIEAIVQLINTRQPQAKIIVLII 139
Cdd:cd01820   81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEEIREKLPNAKILLLGL 136
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 36-153 4.75e-17

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 73.91  E-value: 4.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080768  36 KDKEPDVLFVGDSMVQLMQQYEI--WRELF------SPLHALNFGIGGDTTRHVLWRLKnGELENIKPKVIVVWVGTNN- 106
Cdd:COG2755    5 AGKPLRIVALGDSITAGYGASRErgWPALLarrlaaADVRVVNAGISGATTADLLARLD-RDLLALKPDLVVIELGTNDl 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 296080768 107 ---HENTAEEVAGGIEAIVQLINTRQPQAKIIVLIIYWQDEQDYHERKVQ 153
Cdd:COG2755   84 lrgLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYLNERIE 133
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 44-141 6.61e-13

GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.


Pssm-ID: 463889  Cd Length: 176  Bit Score: 62.56  E-value: 6.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080768   44 FVGDSMVQ---LMQQYEIWRELFSPLHA--------LNFGIGGDTTRHvLWRLKNGELENIKPKVIVVWVGTNN--HENT 110
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLArrlgadvvNNLGISGATTRL-DLLERLDDVLRLKPDLVVILLGTNDlgRGVS 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 296080768  111 AEEVAGGIEAIVQLINTRQPQAKIIVLIIYW 141
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLP 110
 
Name Accession Description Interval E-value
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 8-139 2.46e-74

PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor (PAF) and PAF-AH are key players in inflammation and in atherosclerosis. PAF-AH is a calcium independent phospholipase A2 which exhibits strong substrate specificity towards PAF, hydrolyzing an acetyl ester at the sn-2 position. PAF-AH also degrades a family of oxidized PAF-like phospholipids with short sn-2 residues. In addition, PAF and PAF-AH are associated with neural migration and mammalian reproduction.


Pssm-ID: 238858  Cd Length: 214  Bit Score: 221.01  E-value: 2.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080768   8 PAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQY--EIWRELFSPLHALNFGIGGDTTRHVLWRL 85
Cdd:cd01820    1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296080768  86 KNGELENIKPKVIVVWVGTNNHENT--AEEVAGGIEAIVQLINTRQPQAKIIVLII 139
Cdd:cd01820   81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEEIREKLPNAKILLLGL 136
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 36-153 4.75e-17

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 73.91  E-value: 4.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080768  36 KDKEPDVLFVGDSMVQLMQQYEI--WRELF------SPLHALNFGIGGDTTRHVLWRLKnGELENIKPKVIVVWVGTNN- 106
Cdd:COG2755    5 AGKPLRIVALGDSITAGYGASRErgWPALLarrlaaADVRVVNAGISGATTADLLARLD-RDLLALKPDLVVIELGTNDl 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 296080768 107 ---HENTAEEVAGGIEAIVQLINTRQPQAKIIVLIIYWQDEQDYHERKVQ 153
Cdd:COG2755   84 lrgLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYLNERIE 133
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 41-136 5.14e-14

sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238866  Cd Length: 169  Bit Score: 65.38  E-value: 5.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080768  41 DVLFVGDSMVQLMQqyeiWRELFSPLHALNFGIGGDTTRHVLWRLKngELENIKPKVIVVWVGTNN--HENTAEEVAGGI 118
Cdd:cd01828    1 ALVFLGDSLTEGGP----WALLFPDVKVANRGISGDTTRGLLARLD--EDVALQPKAIFIMIGINDlaQGTSDEDIVANY 74

                         90
                 ....*....|....*...
gi 296080768 119 EAIVQLINTRQPQAKIIV 136
Cdd:cd01828   75 RTILEKLRKHFPNIKIVV 92
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 44-141 6.61e-13

GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.


Pssm-ID: 463889  Cd Length: 176  Bit Score: 62.56  E-value: 6.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080768   44 FVGDSMVQ---LMQQYEIWRELFSPLHA--------LNFGIGGDTTRHvLWRLKNGELENIKPKVIVVWVGTNN--HENT 110
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLArrlgadvvNNLGISGATTRL-DLLERLDDVLRLKPDLVVILLGTNDlgRGVS 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 296080768  111 AEEVAGGIEAIVQLINTRQPQAKIIVLIIYW 141
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLP 110
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 42-153 2.65e-10

SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 238141 [Multi-domain]  Cd Length: 187  Bit Score: 55.88  E-value: 2.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080768  42 VLFVGDSMVQLMQ-------QYEIWRELFSPLHAL----NFGIGGDTTRHVLWRLKNGELENI-KPKVIVVWVGTN---- 105
Cdd:cd00229    1 ILVIGDSITAGYGassgstfYSLLLYLLLLAGGPGveviNLGVSGATTADALRRLGLRLALLKdKPDLVIIELGTNdlgr 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 296080768 106 NHENTAEEVAGGIEAIVQLINTRQPQAKIIVLIIYWQDEQDYHERKVQ 153
Cdd:cd00229   81 GGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRAL 128
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 42-137 2.33e-08

Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the Saccharomyces cerevisiae IAH1. IAH1 may be the major esterase that hydrolyses isoamyl acetate in sake mash. The SGNH-family of hydrolases is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases


Pssm-ID: 238876  Cd Length: 199  Bit Score: 50.71  E-value: 2.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080768  42 VLFvGDSMVQLM--QQYEIW----RELFSP-LHALNFGIGGDTTRHVLWRLKNGELE--NIKPKVIVVWVGTNN---HEN 109
Cdd:cd01838    3 VLF-GDSITQFSfdQGEFGFgaalADVYSRkLDVINRGFSGYNTRWALKVLPKIFLEekLAQPDLVTIFFGANDaalPGQ 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 296080768 110 TA----EEVAGGIEAIVQLINTRQPQAKIIVL 137
Cdd:cd01838   82 PQhvplDEYKENLRKIVSHLKSLSPKTKVILI 113
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 42-147 2.66e-06

SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238872  Cd Length: 191  Bit Score: 44.98  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080768  42 VLFVGDSMVQLMQqYEIWRELF-------SPLHALNFGIGGDTTRHVLWRLKNGELEnIKPKVIVVWVGTN------NHE 108
Cdd:cd01834    4 IVFIGNSITDRGG-YVGYVETYlaarypeLKLTFRNLGWSGDTVSDLAARRDRDVLP-AKPDVVSIMFGINdsfrgfDDP 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 296080768 109 NTAEEVAGGIEAIVQLINTRQPQAKIIVLIIYWQDEQDY 147
Cdd:cd01834   82 VGLEKFKTNLRRLIDRLKNKESAPRIVLVSPIAYEANED 120
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 69-124 4.16e-05

Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 239945  Cd Length: 183  Bit Score: 41.54  E-value: 4.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 296080768  69 LNFGIGGDTTRHVLWRLKNgELENIKPKVIVVWVGTNN--HENTAEEVAGGIEAIVQL 124
Cdd:cd04501   35 INRGINGDTTSQMLVRFYE-DVIALKPAVVIIMGGTNDiiVNTSLEMIKDNIRSMVEL 91
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 40-146 5.33e-04

NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases. E. coli NnaC appears to be involved in polysaccharide synthesis.


Pssm-ID: 238879  Cd Length: 174  Bit Score: 38.46  E-value: 5.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080768  40 PDVLFVGDSMVQLMQQYEIwreLFSPLHALNFGIGGDTTRhvlWRLKNGELENI--KPKVIVVWVGTNN--HENTAEEVA 115
Cdd:cd01841    1 KNIVFIGDSLFEGWPLYEA---EGKGKTVNNLGIAGISSR---QYLEHIEPQLIqkNPSKVFLFLGTNDigKEVSSNQFI 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 296080768 116 GGIEAIVQLINTRQPQAKIIVLIIYWQDEQD 146
Cdd:cd01841   75 KWYRDIIEQIREEFPNTKIYLLSVLPVLEED 105
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
42-126 1.97e-03

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 37.17  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080768   42 VLFVGDSMVQLMQQY--------EIWRELFS---------PLHALNFGIGGDTTR------HVLWRLKNGELENIKPKVI 98
Cdd:pfam00657   1 IVAFGDSLTDGGGDGpggrfswgDLLADFLArklgvpgsgYNHGANFAIGGATIEdlpiqlEQLLRLISDVKDQAKPDLV 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 296080768   99 VVWVGTN---NHENTAEEVAGGI-EAIVQLIN 126
Cdd:pfam00657  81 TIFIGANdlcNFLSSPARSKKRVpDLLDELRA 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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