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Conserved domains on  [gi|15228336|ref|NP_190391|]
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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 ...
 398-616 2.60e-56

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: 189.52  E-value: 2.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336   398 EVYKPKCQAHKNGYYDSFKDSNEENDFKANVKRVELAGIFDEVLGLVKKGQLPDGFEGSRGWINLATQYRRLIEPLDISN 477
Cdd:pfam18117   4 EWYKKTCELQGIGYYDSFKQKSSRRDFKANVSRLKLANYWDEVVEMAEKYPLPDGFELRKKWLYAGTNYRRLVEPLDIAE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336   478 YHGQLKNEDTGPYMLHGRPSRYKYAQRGYEHDILKPTGMIAKDVFwskvnglnLGLQQDiqeilknsgsecgSCFWAEVE 557
Cdd:pfam18117  84 YYRNGKNDDTGDYMSKGRSKRYKLLEKWLEARKKGDKSSKERSKP--------ASLTQD-------------SCFWAHVE 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336   558 ELK---------GKPYEEVQVRFKTLEGLLEGWIKDGEVdEKEIFLEGSTFRKWWN--TLPDSHKIHAPL 616
Cdd:pfam18117 143 EARilckllessGGEREDLKEKLLKFERYVMGLIKNKEV-SPDIFLEGSSFMQWWKeyKLPLGHSYQSPL 211
Lipase_3 pfam01764
Lipase (class 3);
40-196 1.59e-24

Lipase (class 3);


:

Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 99.26  E-value: 1.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336    40 FFAFRASFSSEDLFatentspfgeikmkrNQFPCMRSIGNDV---DTTVNEAFLKSLEvliGPRTSFHASVQSAVDRKQ- 115
Cdd:pfam01764   1 VVAFRGTNSILDWL---------------TDFDFSLTPFKDFflgGGKVHSGFLSAYT---SVREQVLAELKRLLEKYPd 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336   116 -QVVFTGHSFGGATAILATVWYLETYFIRdayaAPEPRCVTFGAPLVGDYIFKHALGrENWSRFFVNFVTRFDIVPRIML 194
Cdd:pfam01764  63 ySIVVTGHSLGGALASLAALDLVENGLRL----SSRVTVVTFGQPRVGNLEFAKLHD-SQGPKFSYRVVHQRDIVPRLPP 137


                  ..
gi 15228336   195 AR 196
Cdd:pfam01764 138 IV 139
 
Name Accession Description Interval E-value
EDS1_EP pfam18117
Enhanced disease susceptibility 1 protein EP domain; The plant specific protein family, which ...
 398-616 2.60e-56

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: 189.52  E-value: 2.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336   398 EVYKPKCQAHKNGYYDSFKDSNEENDFKANVKRVELAGIFDEVLGLVKKGQLPDGFEGSRGWINLATQYRRLIEPLDISN 477
Cdd:pfam18117   4 EWYKKTCELQGIGYYDSFKQKSSRRDFKANVSRLKLANYWDEVVEMAEKYPLPDGFELRKKWLYAGTNYRRLVEPLDIAE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336   478 YHGQLKNEDTGPYMLHGRPSRYKYAQRGYEHDILKPTGMIAKDVFwskvnglnLGLQQDiqeilknsgsecgSCFWAEVE 557
Cdd:pfam18117  84 YYRNGKNDDTGDYMSKGRSKRYKLLEKWLEARKKGDKSSKERSKP--------ASLTQD-------------SCFWAHVE 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336   558 ELK---------GKPYEEVQVRFKTLEGLLEGWIKDGEVdEKEIFLEGSTFRKWWN--TLPDSHKIHAPL 616
Cdd:pfam18117 143 EARilckllessGGEREDLKEKLLKFERYVMGLIKNKEV-SPDIFLEGSSFMQWWKeyKLPLGHSYQSPL 211
Lipase_3 pfam01764
Lipase (class 3);
40-196 1.59e-24

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 99.26  E-value: 1.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336    40 FFAFRASFSSEDLFatentspfgeikmkrNQFPCMRSIGNDV---DTTVNEAFLKSLEvliGPRTSFHASVQSAVDRKQ- 115
Cdd:pfam01764   1 VVAFRGTNSILDWL---------------TDFDFSLTPFKDFflgGGKVHSGFLSAYT---SVREQVLAELKRLLEKYPd 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336   116 -QVVFTGHSFGGATAILATVWYLETYFIRdayaAPEPRCVTFGAPLVGDYIFKHALGrENWSRFFVNFVTRFDIVPRIML 194
Cdd:pfam01764  63 ySIVVTGHSLGGALASLAALDLVENGLRL----SSRVTVVTFGQPRVGNLEFAKLHD-SQGPKFSYRVVHQRDIVPRLPP 137


                  ..
gi 15228336   195 AR 196
Cdd:pfam01764 138 IV 139
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 38-192 4.03e-14

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: 72.12  E-value: 4.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336  38 TVFFAFRASFSSEDLFaTENTSpfgeikmkrNQFPCMRSIGNDVdtTVNEAFLKSLEVLigpRTSFHASVQSAVDR--KQ 115
Cdd:cd00519  64 TIVIAFRGTVSLADWL-TDLDF---------SPVPLDPPLCSGG--KVHSGFYSAYKSL---YNQVLPELKSALKQypDY 128

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228336 116 QVVFTGHSFGGATAILATVWyletyfIRDAYAAPEPRCVTFGAPLVGDYIFKHALGRENwsRFFVNFVTRFDIVPRI 192
Cdd:cd00519 129 KIIVTGHSLGGALASLLALD------LRLRGPGSDVTVYTFGQPRVGNAAFAEYLESTK--GRVYRVVHGNDIVPRL 197
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
115-192 1.00e-10

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 62.85  E-value: 1.00e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228336 115 QQVVFTGHSFGGATAILATVWyletyfIRDAYAAPEPRCVTFGAPLVGDYIFKHALGREnwSRFFVNFVTRFDIVPRI 192
Cdd:COG3675  88 KRLYVTGHSLGGALATLAAAD------LERNYIFPVRGLYTFGQPRVGDRSFAKYYNLH--VPNSYRIVNNNDIVPLL 157
PLN02310 PLN02310
triacylglycerol lipase
 113-222 1.21e-03

triacylglycerol lipase


Pssm-ID: 215176  Cd Length: 405  Bit Score: 41.51  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336  113 RKQQVVFT--GHSFGGATAILATvwYLETYFIRDAYAApeprCVTFGAPLVGDYIFKHALGRENWSRFFVnfVTRFDIVP 190
Cdd:PLN02310 205 KGEEVSLTvtGHSLGGALALLNA--YEAATTIPDLFVS----VISFGAPRVGNIAFKEKLNELGVKTLRV--VVKQDKVP 276

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15228336  191 RI------MLARKTTIEQTLSYVLG------KLDSTRAPI--HESD 222
Cdd:PLN02310 277 KLpgllnkMLNKFHGLTGKLNWVYRhvgtqlKLDAFSSPYlkRESD 322
 
Name Accession Description Interval E-value
EDS1_EP pfam18117
Enhanced disease susceptibility 1 protein EP domain; The plant specific protein family, which ...
 398-616 2.60e-56

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: 189.52  E-value: 2.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336   398 EVYKPKCQAHKNGYYDSFKDSNEENDFKANVKRVELAGIFDEVLGLVKKGQLPDGFEGSRGWINLATQYRRLIEPLDISN 477
Cdd:pfam18117   4 EWYKKTCELQGIGYYDSFKQKSSRRDFKANVSRLKLANYWDEVVEMAEKYPLPDGFELRKKWLYAGTNYRRLVEPLDIAE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336   478 YHGQLKNEDTGPYMLHGRPSRYKYAQRGYEHDILKPTGMIAKDVFwskvnglnLGLQQDiqeilknsgsecgSCFWAEVE 557
Cdd:pfam18117  84 YYRNGKNDDTGDYMSKGRSKRYKLLEKWLEARKKGDKSSKERSKP--------ASLTQD-------------SCFWAHVE 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336   558 ELK---------GKPYEEVQVRFKTLEGLLEGWIKDGEVdEKEIFLEGSTFRKWWN--TLPDSHKIHAPL 616
Cdd:pfam18117 143 EARilckllessGGEREDLKEKLLKFERYVMGLIKNKEV-SPDIFLEGSSFMQWWKeyKLPLGHSYQSPL 211
Lipase_3 pfam01764
Lipase (class 3);
40-196 1.59e-24

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 99.26  E-value: 1.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336    40 FFAFRASFSSEDLFatentspfgeikmkrNQFPCMRSIGNDV---DTTVNEAFLKSLEvliGPRTSFHASVQSAVDRKQ- 115
Cdd:pfam01764   1 VVAFRGTNSILDWL---------------TDFDFSLTPFKDFflgGGKVHSGFLSAYT---SVREQVLAELKRLLEKYPd 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336   116 -QVVFTGHSFGGATAILATVWYLETYFIRdayaAPEPRCVTFGAPLVGDYIFKHALGrENWSRFFVNFVTRFDIVPRIML 194
Cdd:pfam01764  63 ySIVVTGHSLGGALASLAALDLVENGLRL----SSRVTVVTFGQPRVGNLEFAKLHD-SQGPKFSYRVVHQRDIVPRLPP 137


                  ..
gi 15228336   195 AR 196
Cdd:pfam01764 138 IV 139
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 38-192 4.03e-14

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: 72.12  E-value: 4.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336  38 TVFFAFRASFSSEDLFaTENTSpfgeikmkrNQFPCMRSIGNDVdtTVNEAFLKSLEVLigpRTSFHASVQSAVDR--KQ 115
Cdd:cd00519  64 TIVIAFRGTVSLADWL-TDLDF---------SPVPLDPPLCSGG--KVHSGFYSAYKSL---YNQVLPELKSALKQypDY 128

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228336 116 QVVFTGHSFGGATAILATVWyletyfIRDAYAAPEPRCVTFGAPLVGDYIFKHALGRENwsRFFVNFVTRFDIVPRI 192
Cdd:cd00519 129 KIIVTGHSLGGALASLLALD------LRLRGPGSDVTVYTFGQPRVGNAAFAEYLESTK--GRVYRVVHGNDIVPRL 197
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 116-192 1.37e-13

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: 68.68  E-value: 1.37e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228336 116 QVVFTGHSFGGATAILATVWYLETYFIRDayaapePRCVTFGAPLVGDYIFKHALGRENWSRFFVNFVTRFDIVPRI 192
Cdd:cd00741  29 KIHVTGHSLGGALAGLAGLDLRGRGLGRL------VRVYTFGPPRVGNAAFAEDRLDPSDALFVDRIVNDNDIVPRL 99
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
115-192 1.00e-10

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 62.85  E-value: 1.00e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228336 115 QQVVFTGHSFGGATAILATVWyletyfIRDAYAAPEPRCVTFGAPLVGDYIFKHALGREnwSRFFVNFVTRFDIVPRI 192
Cdd:COG3675  88 KRLYVTGHSLGGALATLAAAD------LERNYIFPVRGLYTFGQPRVGDRSFAKYYNLH--VPNSYRIVNNNDIVPLL 157
PLN02310 PLN02310
triacylglycerol lipase
 113-222 1.21e-03

triacylglycerol lipase


Pssm-ID: 215176  Cd Length: 405  Bit Score: 41.51  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228336  113 RKQQVVFT--GHSFGGATAILATvwYLETYFIRDAYAApeprCVTFGAPLVGDYIFKHALGRENWSRFFVnfVTRFDIVP 190
Cdd:PLN02310 205 KGEEVSLTvtGHSLGGALALLNA--YEAATTIPDLFVS----VISFGAPRVGNIAFKEKLNELGVKTLRV--VVKQDKVP 276

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15228336  191 RI------MLARKTTIEQTLSYVLG------KLDSTRAPI--HESD 222
Cdd:PLN02310 277 KLpgllnkMLNKFHGLTGKLNWVYRhvgtqlKLDAFSSPYlkRESD 322
 
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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