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Conserved domains on  [gi|15231218|ref|NP_190811|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EDS1_EP super family cl39505
Enhanced disease susceptibility 1 protein EP domain; The plant specific protein family, which ...
 316-524 2.55e-75

Enhanced disease susceptibility 1 protein EP domain; The plant specific protein family, which comprises EDS1 (Enhanced disease susceptibility 1), PAD4 (Phytoalexin deficient4) and SAG101 (Senescence-associated gene 101), is involved in innate immunity. Signaling by intracellular immune receptors with NB-ARC domain (pfam00931) relies on this protein family. C-terminus of Arabidopsis EDS1 and PAD4 proteins did not have recognizable sequence homology to other domains and therefore named EP domain (EDS1-PAD4). A combination of an N-terminal lipase_3 domain (pfam01764) and the C-terminal EP-domain is the defining feature of this family. Structurally, EP domain comprises exclusively of alpha-helices (PDB:4NFU). Structure-function analysis of Arabidopsis proteins showed that EDS1 forms heterodimers with PAD4 or SAG101, chiefly through the N-terminal lipase_3 domain. These heterodimers are essential for plant defense signaling. The EP domain is not stable without the lipase_3 domain, but is required for immunity. Mutations of conserved residues in the EP domain of EDS1 strongly affect its immune signaling function.


The actual alignment was detected with superfamily member pfam18117:

Pssm-ID: 407951  Cd Length: 214  Bit Score: 237.29  E-value: 2.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231218   316 EIQWYKDRCDasEEQLGYYDFFKRYSLKRDFKVNMSRIRLAKFWDTVIKMVETNELPFDFHLGKKWIYASQFYQLLAEPL 395
Cdd:pfam18117   2 QLEWYKKTCE--LQGIGYYDSFKQKSSRRDFKANVSRLKLANYWDEVVEMAEKYPLPDGFELRKKWLYAGTNYRRLVEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231218   396 DIANFYKNRDIKTGGHYLEGNRPKRYEVIDKWQKGVKVP--EECVRSRYASTTQDTCFWAKLEQAKEWLDEArkeSSDPQ 473
Cdd:pfam18117  80 DIAEYYRNGKNDDTGDYMSKGRSKRYKLLEKWLEARKKGdkSSKERSKPASLTQDSCFWAHVEEARILCKLL---ESSGG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15231218   474 RRSLLREKIVPFESYANTLVTKKEVSLDVKAKNSSYSVWeanLKEFKCKMG 524
Cdd:pfam18117 157 EREDLKEKLLKFERYVMGLIKNKEVSPDIFLEGSSFMQW---WKEYKLPLG 204
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 112-186 9.61e-22

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 pfam01764:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 139  Bit Score: 91.17  E-value: 9.61e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231218   112 VVITGHSTGGALAAFTALWLLSQSSPPSFRVFCITFGSPLLGNQSLSTSISrSRLAHNFCHVVSIHDLVPRSSNE 186
Cdd:pfam01764  65 IVVTGHSLGGALASLAALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHD-SQGPKFSYRVVHQRDIVPRLPPI 138
 
Name Accession Description Interval E-value
EDS1_EP pfam18117
Enhanced disease susceptibility 1 protein EP domain; The plant specific protein family, which ...
 316-524 2.55e-75

Enhanced disease susceptibility 1 protein EP domain; The plant specific protein family, which comprises EDS1 (Enhanced disease susceptibility 1), PAD4 (Phytoalexin deficient4) and SAG101 (Senescence-associated gene 101), is involved in innate immunity. Signaling by intracellular immune receptors with NB-ARC domain (pfam00931) relies on this protein family. C-terminus of Arabidopsis EDS1 and PAD4 proteins did not have recognizable sequence homology to other domains and therefore named EP domain (EDS1-PAD4). A combination of an N-terminal lipase_3 domain (pfam01764) and the C-terminal EP-domain is the defining feature of this family. Structurally, EP domain comprises exclusively of alpha-helices (PDB:4NFU). Structure-function analysis of Arabidopsis proteins showed that EDS1 forms heterodimers with PAD4 or SAG101, chiefly through the N-terminal lipase_3 domain. These heterodimers are essential for plant defense signaling. The EP domain is not stable without the lipase_3 domain, but is required for immunity. Mutations of conserved residues in the EP domain of EDS1 strongly affect its immune signaling function.


Pssm-ID: 407951  Cd Length: 214  Bit Score: 237.29  E-value: 2.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231218   316 EIQWYKDRCDasEEQLGYYDFFKRYSLKRDFKVNMSRIRLAKFWDTVIKMVETNELPFDFHLGKKWIYASQFYQLLAEPL 395
Cdd:pfam18117   2 QLEWYKKTCE--LQGIGYYDSFKQKSSRRDFKANVSRLKLANYWDEVVEMAEKYPLPDGFELRKKWLYAGTNYRRLVEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231218   396 DIANFYKNRDIKTGGHYLEGNRPKRYEVIDKWQKGVKVP--EECVRSRYASTTQDTCFWAKLEQAKEWLDEArkeSSDPQ 473
Cdd:pfam18117  80 DIAEYYRNGKNDDTGDYMSKGRSKRYKLLEKWLEARKKGdkSSKERSKPASLTQDSCFWAHVEEARILCKLL---ESSGG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15231218   474 RRSLLREKIVPFESYANTLVTKKEVSLDVKAKNSSYSVWeanLKEFKCKMG 524
Cdd:pfam18117 157 EREDLKEKLLKFERYVMGLIKNKEVSPDIFLEGSSFMQW---WKEYKLPLG 204
Lipase_3 pfam01764
Lipase (class 3);
112-186 9.61e-22

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 91.17  E-value: 9.61e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231218   112 VVITGHSTGGALAAFTALWLLSQSSPPSFRVFCITFGSPLLGNQSLSTSISrSRLAHNFCHVVSIHDLVPRSSNE 186
Cdd:pfam01764  65 IVVTGHSLGGALASLAALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHD-SQGPKFSYRVVHQRDIVPRLPPI 138
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 112-232 1.30e-14

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 71.38  E-value: 1.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231218 112 VVITGHSTGGALAAFTALWLlsQSSPPSFRVFCITFGSPLLGNQSLSTSISRSRLAHNFCHVVSIHDLVPRSS--NEQFW 189
Cdd:cd00741  30 IHVTGHSLGGALAGLAGLDL--RGRGLGRLVRVYTFGPPRVGNAAFAEDRLDPSDALFVDRIVNDNDIVPRLPpgGEGYP 107

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15231218 190 PFGT--YLFCSDKGGVCLDNAGSVRLMFNILNTTATQNTEEHQRY 232
Cdd:cd00741 108 HGGAefYINGGKSQPGCCKNVLEAVDIDFGNIGLSGNGLCDHLRY 152
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
112-182 1.94e-07

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 52.45  E-value: 1.94e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231218 112 VVITGHSTGGALAAFTALWLlsQSSPPSFRVFCITFGSPLLGNQSLSTSISRsRLAHNFCHVVSiHDLVPR 182
Cdd:COG3675  90 LYVTGHSLGGALATLAAADL--ERNYIFPVRGLYTFGQPRVGDRSFAKYYNL-HVPNSYRIVNN-NDIVPL 156
PLN02934 PLN02934
triacylglycerol lipase
 113-205 2.88e-06

triacylglycerol lipase


Pssm-ID: 215504  Cd Length: 515  Bit Score: 49.78  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231218  113 VITGHSTGGALAA-FTALWLLSQSSPPSFRVFCI-TFGSPLLGNQSLSTSIsRSRLAH---NFCHVVSIHDLVPRSsneq 187
Cdd:PLN02934 324 VVTGHSLGGALAIlFPTVLVLQEETEVMKRLLGVyTFGQPRIGNRQLGKFM-EAQLNYpvpRYFRVVYCNDLVPRL---- 398

                         90
                 ....*....|....*...
gi 15231218  188 fwPFGTYLFCSDKGGVCL 205
Cdd:PLN02934 399 --PYDDKTFLYKHFGVCL 414
 
Name Accession Description Interval E-value
EDS1_EP pfam18117
Enhanced disease susceptibility 1 protein EP domain; The plant specific protein family, which ...
 316-524 2.55e-75

Enhanced disease susceptibility 1 protein EP domain; The plant specific protein family, which comprises EDS1 (Enhanced disease susceptibility 1), PAD4 (Phytoalexin deficient4) and SAG101 (Senescence-associated gene 101), is involved in innate immunity. Signaling by intracellular immune receptors with NB-ARC domain (pfam00931) relies on this protein family. C-terminus of Arabidopsis EDS1 and PAD4 proteins did not have recognizable sequence homology to other domains and therefore named EP domain (EDS1-PAD4). A combination of an N-terminal lipase_3 domain (pfam01764) and the C-terminal EP-domain is the defining feature of this family. Structurally, EP domain comprises exclusively of alpha-helices (PDB:4NFU). Structure-function analysis of Arabidopsis proteins showed that EDS1 forms heterodimers with PAD4 or SAG101, chiefly through the N-terminal lipase_3 domain. These heterodimers are essential for plant defense signaling. The EP domain is not stable without the lipase_3 domain, but is required for immunity. Mutations of conserved residues in the EP domain of EDS1 strongly affect its immune signaling function.


Pssm-ID: 407951  Cd Length: 214  Bit Score: 237.29  E-value: 2.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231218   316 EIQWYKDRCDasEEQLGYYDFFKRYSLKRDFKVNMSRIRLAKFWDTVIKMVETNELPFDFHLGKKWIYASQFYQLLAEPL 395
Cdd:pfam18117   2 QLEWYKKTCE--LQGIGYYDSFKQKSSRRDFKANVSRLKLANYWDEVVEMAEKYPLPDGFELRKKWLYAGTNYRRLVEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231218   396 DIANFYKNRDIKTGGHYLEGNRPKRYEVIDKWQKGVKVP--EECVRSRYASTTQDTCFWAKLEQAKEWLDEArkeSSDPQ 473
Cdd:pfam18117  80 DIAEYYRNGKNDDTGDYMSKGRSKRYKLLEKWLEARKKGdkSSKERSKPASLTQDSCFWAHVEEARILCKLL---ESSGG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15231218   474 RRSLLREKIVPFESYANTLVTKKEVSLDVKAKNSSYSVWeanLKEFKCKMG 524
Cdd:pfam18117 157 EREDLKEKLLKFERYVMGLIKNKEVSPDIFLEGSSFMQW---WKEYKLPLG 204
Lipase_3 pfam01764
Lipase (class 3);
112-186 9.61e-22

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 91.17  E-value: 9.61e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231218   112 VVITGHSTGGALAAFTALWLLSQSSPPSFRVFCITFGSPLLGNQSLSTSISrSRLAHNFCHVVSIHDLVPRSSNE 186
Cdd:pfam01764  65 IVVTGHSLGGALASLAALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHD-SQGPKFSYRVVHQRDIVPRLPPI 138
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 112-232 1.30e-14

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 71.38  E-value: 1.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231218 112 VVITGHSTGGALAAFTALWLlsQSSPPSFRVFCITFGSPLLGNQSLSTSISRSRLAHNFCHVVSIHDLVPRSS--NEQFW 189
Cdd:cd00741  30 IHVTGHSLGGALAGLAGLDL--RGRGLGRLVRVYTFGPPRVGNAAFAEDRLDPSDALFVDRIVNDNDIVPRLPpgGEGYP 107

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15231218 190 PFGT--YLFCSDKGGVCLDNAGSVRLMFNILNTTATQNTEEHQRY 232
Cdd:cd00741 108 HGGAefYINGGKSQPGCCKNVLEAVDIDFGNIGLSGNGLCDHLRY 152
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 112-193 1.07e-12

Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 67.50  E-value: 1.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231218 112 VVITGHSTGGALAAFTALWLlsQSSPPSFRVFCITFGSPLLGNQSLSTSISRSRlaHNFCHVVSIHDLVPR------SSN 185
Cdd:cd00519 130 IIVTGHSLGGALASLLALDL--RLRGPGSDVTVYTFGQPRVGNAAFAEYLESTK--GRVYRVVHGNDIVPRlppgslTPP 205


                ....*...
gi 15231218 186 EQFWPFGT 193
Cdd:cd00519 206 EGYTHVGT 213
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
112-182 1.94e-07

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 52.45  E-value: 1.94e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231218 112 VVITGHSTGGALAAFTALWLlsQSSPPSFRVFCITFGSPLLGNQSLSTSISRsRLAHNFCHVVSiHDLVPR 182
Cdd:COG3675  90 LYVTGHSLGGALATLAAADL--ERNYIFPVRGLYTFGQPRVGDRSFAKYYNL-HVPNSYRIVNN-NDIVPL 156
PLN02934 PLN02934
triacylglycerol lipase
 113-205 2.88e-06

triacylglycerol lipase


Pssm-ID: 215504  Cd Length: 515  Bit Score: 49.78  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231218  113 VITGHSTGGALAA-FTALWLLSQSSPPSFRVFCI-TFGSPLLGNQSLSTSIsRSRLAH---NFCHVVSIHDLVPRSsneq 187
Cdd:PLN02934 324 VVTGHSLGGALAIlFPTVLVLQEETEVMKRLLGVyTFGQPRIGNRQLGKFM-EAQLNYpvpRYFRVVYCNDLVPRL---- 398

                         90
                 ....*....|....*...
gi 15231218  188 fwPFGTYLFCSDKGGVCL 205
Cdd:PLN02934 399 --PYDDKTFLYKHFGVCL 414
PLN02753 PLN02753
triacylglycerol lipase
 112-183 1.68e-03

triacylglycerol lipase


Pssm-ID: 178354  Cd Length: 531  Bit Score: 41.24  E-value: 1.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231218  112 VVITGHSTGGALAAFTA-----LWLLSQSSPPSFRVFCITFGSPLLGNQSLSTSIsrSRLAHNFCHVVSIHDLVPRS 183
Cdd:PLN02753 314 ITVTGHSLGGALAILSAydiaeMGLNRSKKGKVIPVTVLTYGGPRVGNVRFKDRM--EELGVKVLRVVNVHDVVPKS 388
PLN02802 PLN02802
triacylglycerol lipase
 112-182 2.07e-03

triacylglycerol lipase


Pssm-ID: 215432  Cd Length: 509  Bit Score: 40.91  E-value: 2.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231218  112 VVITGHSTGGALAAFTALwLLSQSSPPSFRVFCITFGSPLLGNQSLSTSISRSRLahNFCHVVSIHDLVPR 182
Cdd:PLN02802 332 ITVTGHSLGAALALLVAD-ELATCVPAAPPVAVFSFGGPRVGNRAFADRLNARGV--KVLRVVNAQDVVTR 399
PLN03037 PLN03037
lipase class 3 family protein; Provisional
 114-182 6.31e-03

lipase class 3 family protein; Provisional


Pssm-ID: 215547  Cd Length: 525  Bit Score: 39.17  E-value: 6.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231218  114 ITGHSTGGALAAFTAlWLLSQSSPPSFRVFCITFGSPLLGNQSLSTSIsrSRLAHNFCHVVSIHDLVPR 182
Cdd:PLN03037 322 ITGHSLGGALALLNA-YEAARSVPALSNISVISFGAPRVGNLAFKEKL--NELGVKVLRVVNKQDIVPK 387
PLN02454 PLN02454
triacylglycerol lipase
 112-182 7.72e-03

triacylglycerol lipase


Pssm-ID: 215249  Cd Length: 414  Bit Score: 38.67  E-value: 7.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231218  112 VVITGHSTGGALAAFTALWLL-SQSSPPSFRVFCITFGSPLLGNQSLSTSISRSRLAHnFCHVVSIHDLVPR 182
Cdd:PLN02454 230 IVLTGHSLGASLATLAAFDIVeNGVSGADIPVTAIVFGSPQVGNKEFNDRFKEHPNLK-ILHVRNTIDLIPH 300
 
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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