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Conserved domains on  [gi|1972305486|ref|NP_001379717|]
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Platelet-activating factor acetylhydrolase homolog 2 [Caenorhabditis elegans]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 4-186 3.77e-100

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam03403:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 372  Bit Score: 293.58  E-value: 3.77e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972305486   4 YISSPQVLTRQVSGQFQVGCKDLMIDGTVlgdRGLFMRLYFPTDsQAADISSYPLWLPKPQYAHGLGEYLGQSSQKMNVI 83
Cdd:pfam03403   1 AGSSGQVKIPAGNGPYPVGCTDLMIGHTL---RGSFLRLYYPSD-QADEDREDTLWIPNKEYFQGLSEFLGTSSWLGNRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972305486  84 TSTVVGEKREDCIENAQMSTKcDKWPIVVFSHGLGGSRTFYSTYCTSLASHGYVVAAVEHKDHSACWTYQLTEKNGELVE 163
Cdd:pfam03403  77 FALLVGSLTLPASWNSPFKTG-EKYPLIVFSHGLGAFRTIYSAICIELASHGFVVAAVEHRDRSASATYFFKDKPAAEEE 155

                         170       180
                  ....*....|....*....|...
gi 1972305486 164 QPIKIKLIEKNEKNEFKIRNQQV 186
Cdd:pfam03403 156 QKSWIYLRKVKEEEEFHLRNEQV 178
 
Name Accession Description Interval E-value
PAF-AH_p_II pfam03403
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor ...
 4-186 3.77e-100

Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor acetylhydrolase (PAF-AH) is a subfamily of phospholipases A2, responsible for inactivation of platelet-activating factor through cleavage of an acetyl group. Three known PAF-AHs are the brain heterotrimeric PAF-AH Ib, whose catalytic beta and gamma subunits are aligned in pfam02266, the extracellular, plasma PAF-AH (pPAF-AH), and the intracellular PAF-AH isoform II (PAF-AH II). This family aligns pPAF-AH and PAF-AH II, whose similarity was previously noted.


Pssm-ID: 397462 [Multi-domain]  Cd Length: 372  Bit Score: 293.58  E-value: 3.77e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972305486   4 YISSPQVLTRQVSGQFQVGCKDLMIDGTVlgdRGLFMRLYFPTDsQAADISSYPLWLPKPQYAHGLGEYLGQSSQKMNVI 83
Cdd:pfam03403   1 AGSSGQVKIPAGNGPYPVGCTDLMIGHTL---RGSFLRLYYPSD-QADEDREDTLWIPNKEYFQGLSEFLGTSSWLGNRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972305486  84 TSTVVGEKREDCIENAQMSTKcDKWPIVVFSHGLGGSRTFYSTYCTSLASHGYVVAAVEHKDHSACWTYQLTEKNGELVE 163
Cdd:pfam03403  77 FALLVGSLTLPASWNSPFKTG-EKYPLIVFSHGLGAFRTIYSAICIELASHGFVVAAVEHRDRSASATYFFKDKPAAEEE 155

                         170       180
                  ....*....|....*....|...
gi 1972305486 164 QPIKIKLIEKNEKNEFKIRNQQV 186
Cdd:pfam03403 156 QKSWIYLRKVKEEEEFHLRNEQV 178
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
107-148 2.32e-13

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 67.05  E-value: 2.32e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972305486 107 KWPIVVFSHGLGGSRTFYSTYCTSLASHGYVVAAVEHKDHSA 148
Cdd:COG4188    61 PFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSNA 102
PLN00021 PLN00021
chlorophyllase
 106-140 6.33e-04

chlorophyllase


Pssm-ID: 177659  Cd Length: 313  Bit Score: 39.26  E-value: 6.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1972305486 106 DKWPIVVFSHGLGGSRTFYSTYCTSLASHGYVVAA 140
Cdd:PLN00021   50 GTYPVLLFLHGYLLYNSFYSQLLQHIASHGFIVVA 84
 
Name Accession Description Interval E-value
PAF-AH_p_II pfam03403
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor ...
 4-186 3.77e-100

Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor acetylhydrolase (PAF-AH) is a subfamily of phospholipases A2, responsible for inactivation of platelet-activating factor through cleavage of an acetyl group. Three known PAF-AHs are the brain heterotrimeric PAF-AH Ib, whose catalytic beta and gamma subunits are aligned in pfam02266, the extracellular, plasma PAF-AH (pPAF-AH), and the intracellular PAF-AH isoform II (PAF-AH II). This family aligns pPAF-AH and PAF-AH II, whose similarity was previously noted.


Pssm-ID: 397462 [Multi-domain]  Cd Length: 372  Bit Score: 293.58  E-value: 3.77e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972305486   4 YISSPQVLTRQVSGQFQVGCKDLMIDGTVlgdRGLFMRLYFPTDsQAADISSYPLWLPKPQYAHGLGEYLGQSSQKMNVI 83
Cdd:pfam03403   1 AGSSGQVKIPAGNGPYPVGCTDLMIGHTL---RGSFLRLYYPSD-QADEDREDTLWIPNKEYFQGLSEFLGTSSWLGNRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972305486  84 TSTVVGEKREDCIENAQMSTKcDKWPIVVFSHGLGGSRTFYSTYCTSLASHGYVVAAVEHKDHSACWTYQLTEKNGELVE 163
Cdd:pfam03403  77 FALLVGSLTLPASWNSPFKTG-EKYPLIVFSHGLGAFRTIYSAICIELASHGFVVAAVEHRDRSASATYFFKDKPAAEEE 155

                         170       180
                  ....*....|....*....|...
gi 1972305486 164 QPIKIKLIEKNEKNEFKIRNQQV 186
Cdd:pfam03403 156 QKSWIYLRKVKEEEEFHLRNEQV 178
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
107-148 2.32e-13

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 67.05  E-value: 2.32e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972305486 107 KWPIVVFSHGLGGSRTFYSTYCTSLASHGYVVAAVEHKDHSA 148
Cdd:COG4188    61 PFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSNA 102
Chlorophyllase2 pfam12740
Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC: ...
 103-141 1.64e-04

Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC:3.1.1.14) enzymes. Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of an ester bond to yield chlorophyllide and phytol. The family includes both plant and Amphioxus members.


Pssm-ID: 432755  Cd Length: 254  Bit Score: 41.15  E-value: 1.64e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1972305486 103 TKCDKWPIVVFSHGLGGSRTFYSTYCTSLASHGYVVAAV 141
Cdd:pfam12740  12 TEAGTYPVLLFLHGYLLYNSFYSQLLQHIASHGFIVVAP 50
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
107-142 4.61e-04

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.56  E-value: 4.61e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1972305486 107 KWPIVVFSHGLGGSRTFYSTYCTSLASHGYVVAAVE 142
Cdd:COG0412    28 PRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPD 63
PLN00021 PLN00021
chlorophyllase
 106-140 6.33e-04

chlorophyllase


Pssm-ID: 177659  Cd Length: 313  Bit Score: 39.26  E-value: 6.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1972305486 106 DKWPIVVFSHGLGGSRTFYSTYCTSLASHGYVVAA 140
Cdd:PLN00021   50 GTYPVLLFLHGYLLYNSFYSQLLQHIASHGFIVVA 84
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 111-142 2.04e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 36.35  E-value: 2.04e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1972305486 111 VVFSHGLGGSRTFYSTYCTSLASHGYVVAAVE 142
Cdd:COG1075     8 VVLVHGLGGSAASWAPLAPRLRAAGYPVYALN 39
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
109-143 2.56e-03

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 37.29  E-value: 2.56e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1972305486 109 PIVVFSHGLGGSRTFYSTYCTSLASHGYVVAAVEH 143
Cdd:COG2267    29 GTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDL 63
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 107-143 3.69e-03

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 36.82  E-value: 3.69e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1972305486 107 KWPIVVFSHGLGGSRTFYSTYCTSLASHGYVVAAVEH 143
Cdd:COG1073    36 KYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDY 72
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
107-141 6.56e-03

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 36.15  E-value: 6.56e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1972305486 107 KWPIVVFSHGLGGSRT-FYSTYCTSLASHGYVVAAV 141
Cdd:COG1506    22 KYPVVVYVHGGPGSRDdSFLPLAQALASRGYAVLAP 57
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
109-147 8.28e-03

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 35.89  E-value: 8.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972305486 109 PIVVFSHGLGGSrtFYSTYCTSLASH----GYVVAAVEHKDHS 147
Cdd:COG0429    62 PLVVLLHGLEGS--SDSHYARGLARAlyarGWDVVRLNFRGCG 102
 
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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