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Conserved domains on  [gi|1063705551|ref|NP_001324287|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

dienelactone hydrolase family protein( domain architecture ID 11123939)

dienelactone hydrolase family protein such as carboxymethylenebutenolidase, which catalyzes the reaction between 4-carboxymethylenebut-2-en-4-olide and water to produce 4-oxohex-2-enedioate

CATH:  3.40.50.1820
EC:  3.-.-.-|3.1.-.-
Gene Ontology:  GO:0005829|GO:0016787
PubMed:  2380986|19508187|12369917

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
DLH pfam01738
Dienelactone hydrolase family;
57-274 2.45e-76

Dienelactone hydrolase family;


:

Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 231.09  E-value: 2.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551  57 DAYVVGKDDA--PGIVVIQEWWGVDfeiKNHA-IKISQLEPGFKALIPDLYRGKVG-LDTAEAQHLMDGLDWPGAIK--- 129
Cdd:pfam01738   1 DAYLATPKNPpwPVVVVFQEIFGVN---DNIReIADRLADEGYVALAPDLYFRQGDpNDEADAARAMFELVSKRVMEkvl 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 130 -DIRASVNWLKSN---GSKKVGVTGMCMGGALAIASSVLVPEVDAVVGFYG-TPSSELADPAQAKAPIQAHFGELDNFVG 204
Cdd:pfam01738  78 dDLEAAVNYLKSQpevSPKKVGVVGYCMGGALAVLLAAKGPLVDAAVGFYGvGPEPPLIEAPDIKAPILFHFGEEDHFVP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 205 FSDVtaaKNLEEKLKASGVAHEVHIYPGNGHAFLNRSPEGvsrrksmglsdEDEAAVELAWSRFTSWMKQ 274
Cdd:pfam01738 158 ADSR---ELIEEALKAANVDHQIHSYPGAGHAFANDSRPS-----------YNAAAAEDAWERTLEFFKQ 213
 
Name Accession Description Interval E-value
DLH pfam01738
Dienelactone hydrolase family;
57-274 2.45e-76

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 231.09  E-value: 2.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551  57 DAYVVGKDDA--PGIVVIQEWWGVDfeiKNHA-IKISQLEPGFKALIPDLYRGKVG-LDTAEAQHLMDGLDWPGAIK--- 129
Cdd:pfam01738   1 DAYLATPKNPpwPVVVVFQEIFGVN---DNIReIADRLADEGYVALAPDLYFRQGDpNDEADAARAMFELVSKRVMEkvl 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 130 -DIRASVNWLKSN---GSKKVGVTGMCMGGALAIASSVLVPEVDAVVGFYG-TPSSELADPAQAKAPIQAHFGELDNFVG 204
Cdd:pfam01738  78 dDLEAAVNYLKSQpevSPKKVGVVGYCMGGALAVLLAAKGPLVDAAVGFYGvGPEPPLIEAPDIKAPILFHFGEEDHFVP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 205 FSDVtaaKNLEEKLKASGVAHEVHIYPGNGHAFLNRSPEGvsrrksmglsdEDEAAVELAWSRFTSWMKQ 274
Cdd:pfam01738 158 ADSR---ELIEEALKAANVDHQIHSYPGAGHAFANDSRPS-----------YNAAAAEDAWERTLEFFKQ 213
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
45-273 3.05e-54

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 175.15  E-value: 3.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551  45 RKIQIQ-RDDTTFDAYVV---GKDDAPGIVVIQEWWGVDFEIKNHAIKISQLepGFKALIPDLY-RGKVGLDTAEAQHLM 119
Cdd:COG0412     4 ETVTIPtPDGVTLPGYLArpaGGGPRPGVVVLHEIFGLNPHIRDVARRLAAA--GYVVLAPDLYgRGGPGDDPDEARALM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 120 DGLDWPGAIKDIRASVNWLKSNG---SKKVGVTGMCMGGALAIASSVLVPEVDAVVGFYGTPSSE--LADPAQAKAPIQA 194
Cdd:COG0412    82 GALDPELLAADLRAALDWLKAQPevdAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPADdlLDLAARIKAPVLL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705551 195 HFGELDNFVGFSDVTAaknLEEKLKASGVAHEVHIYPGNGHAFLNRspegvsrrksmGLSDEDEAAVELAWSRFTSWMK 273
Cdd:COG0412   162 LYGEKDPLVPPEQVAA---LEAALAAAGVDVELHVYPGAGHGFTNP-----------GRPRYDPAAAEDAWQRTLAFLA 226
 
Name Accession Description Interval E-value
DLH pfam01738
Dienelactone hydrolase family;
57-274 2.45e-76

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 231.09  E-value: 2.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551  57 DAYVVGKDDA--PGIVVIQEWWGVDfeiKNHA-IKISQLEPGFKALIPDLYRGKVG-LDTAEAQHLMDGLDWPGAIK--- 129
Cdd:pfam01738   1 DAYLATPKNPpwPVVVVFQEIFGVN---DNIReIADRLADEGYVALAPDLYFRQGDpNDEADAARAMFELVSKRVMEkvl 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 130 -DIRASVNWLKSN---GSKKVGVTGMCMGGALAIASSVLVPEVDAVVGFYG-TPSSELADPAQAKAPIQAHFGELDNFVG 204
Cdd:pfam01738  78 dDLEAAVNYLKSQpevSPKKVGVVGYCMGGALAVLLAAKGPLVDAAVGFYGvGPEPPLIEAPDIKAPILFHFGEEDHFVP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 205 FSDVtaaKNLEEKLKASGVAHEVHIYPGNGHAFLNRSPEGvsrrksmglsdEDEAAVELAWSRFTSWMKQ 274
Cdd:pfam01738 158 ADSR---ELIEEALKAANVDHQIHSYPGAGHAFANDSRPS-----------YNAAAAEDAWERTLEFFKQ 213
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
45-273 3.05e-54

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 175.15  E-value: 3.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551  45 RKIQIQ-RDDTTFDAYVV---GKDDAPGIVVIQEWWGVDFEIKNHAIKISQLepGFKALIPDLY-RGKVGLDTAEAQHLM 119
Cdd:COG0412     4 ETVTIPtPDGVTLPGYLArpaGGGPRPGVVVLHEIFGLNPHIRDVARRLAAA--GYVVLAPDLYgRGGPGDDPDEARALM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 120 DGLDWPGAIKDIRASVNWLKSNG---SKKVGVTGMCMGGALAIASSVLVPEVDAVVGFYGTPSSE--LADPAQAKAPIQA 194
Cdd:COG0412    82 GALDPELLAADLRAALDWLKAQPevdAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPADdlLDLAARIKAPVLL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705551 195 HFGELDNFVGFSDVTAaknLEEKLKASGVAHEVHIYPGNGHAFLNRspegvsrrksmGLSDEDEAAVELAWSRFTSWMK 273
Cdd:COG0412   162 LYGEKDPLVPPEQVAA---LEAALAAAGVDVELHVYPGAGHGFTNP-----------GRPRYDPAAAEDAWQRTLAFLA 226
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
124-277 4.97e-14

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 69.13  E-value: 4.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 124 WPGAIKDIRASVNWLKSNGSK------KVGVTGMCMGGALAIASSVL-----VPEVDAVVGFYGtPSSELADPAQAK--- 189
Cdd:COG0657    60 FPAALEDAYAALRWLRANAAElgidpdRIAVAGDSAGGHLAAALALRardrgGPRPAAQVLIYP-VLDLTASPLRADlag 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 190 -APIQAHFGELDNFVGFSdvtaaKNLEEKLKASGVAHEVHIYPGNGHAFLNRSPEGVSRRksmglsdedeaavelAWSRF 268
Cdd:COG0657   139 lPPTLIVTGEADPLVDES-----EALAAALRAAGVPVELHVYPGGGHGFGLLAGLPEARA---------------ALAEI 198


                  ....*....
gi 1063705551 269 TSWMKQYLA 277
Cdd:COG0657   199 AAFLRRALA 207
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
51-248 1.01e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 57.33  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551  51 RDDTTFDAYVV---GKDDAPGIVVIQEWWGVDFEIKNHAIKisQL-EPGFKALIPDlYRGkvgldtaeaqHLMDGLDWPG 126
Cdd:COG1506     5 ADGTTLPGWLYlpaDGKKYPVVVYVHGGPGSRDDSFLPLAQ--ALaSRGYAVLAPD-YRG----------YGESAGDWGG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 127 A-IKDIRASVNWLKSNG---SKKVGVTGMCMGGALAIASSVLVPE-VDAVV--------------------GFYGTPSSE 181
Cdd:COG1506    72 DeVDDVLAAIDYLAARPyvdPDRIGIYGHSYGGYMALLAAARHPDrFKAAValagvsdlrsyygttreyteRLMGGPWED 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705551 182 LADPAQA---------KAPIQAHFGELDNFVGFSDvtaAKNLEEKLKASGVAHEVHIYPGNGHAFLNRSPEGVSRR 248
Cdd:COG1506   152 PEAYAARsplayadklKTPLLLIHGEADDRVPPEQ---AERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLER 224
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
92-239 1.20e-05

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 45.38  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551  92 LEPGFKALIPDLyRGkVGLDTAEAQHLmdgLDWPGAIKDIRASVNWLKSNGSKKVGVTGMCMGGALA----------IAS 161
Cdd:COG2267    52 AAAGYAVLAFDL-RG-HGRSDGPRGHV---DSFDDYVDDLRAALDALRARPGLPVVLLGHSMGGLIAllyaarypdrVAG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 162 SVLV-------PEVDAVVGFYGtpSSELADPAQA-KAPIQAHFGELDNFVgfsDVTAAKNLEEKLKASGvahEVHIYPGN 233
Cdd:COG2267   127 LVLLapayradPLLGPSARWLR--ALRLAEALARiDVPVLVLHGGADRVV---PPEAARRLAARLSPDV---ELVLLPGA 198


                  ....*.
gi 1063705551 234 GHAFLN 239
Cdd:COG2267   199 RHELLN 204
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 124-176 7.20e-05

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 42.94  E-value: 7.20e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705551 124 WPGAIKDIRASVNWLKSNGSK------KVGVTGMCMGGALA--------------------IASSVLVPEVDAVVGFYG 176
Cdd:pfam20434  63 FPAQIQDVKAAIRFLRANAAKygidtnKIALMGFSAGGHLAllaglsnnnkefegnvgdytPESSKESFKVNAVVDFYG 141
YpfH COG0400
Predicted esterase [General function prediction only];
154-236 2.31e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 41.05  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 154 GGALAIASSVLVPE-VDAVVGFYGT----PSSELADPAQAKAPI-QAHfGELDNFVgfsDVTAAKNLEEKLKASGVAHEV 227
Cdd:COG0400    99 GAAMALSLALRRPElLAGVVALSGYlpgeEALPAPEAALAGTPVfLAH-GTQDPVI---PVERAREAAEALEAAGADVTY 174


                  ....*....
gi 1063705551 228 HIYPGnGHA 236
Cdd:COG0400   175 REYPG-GHE 182
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 95-172 3.03e-04

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 41.44  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551  95 GFKALIPDlYRGkvgldTAEAQHLMDGLDWPgAIKDIRASVNWLKS---NGSKKVGVTGMCMGGALAIASSVLVPEVDAV 171
Cdd:COG1073    64 GFNVLAFD-YRG-----YGESEGEPREEGSP-ERRDARAAVDYLRTlpgVDPERIGLLGISLGGGYALNAAATDPRVKAV 136


                  .
gi 1063705551 172 V 172
Cdd:COG1073   137 I 137
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 142-241 4.84e-04

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 40.44  E-value: 4.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705551 142 GSKKVGVTGMCMGGALAIASSVLVP-EVDAVVGFYGT--PSSELADPAQA---KAPI-QAHfGELDNFVgfsDVTAAKNL 214
Cdd:pfam02230 103 PSSRIIIGGFSQGAMLALYSALTLPlPLGGIVAFSGFlpLPTKFPSHPNLvtkKTPIfLIH-GEEDPVV---PLALGKLA 178

                          90       100
                  ....*....|....*....|....*..
gi 1063705551 215 EEKLKASGVAHEVHIYPGNGHAFLNRS 241
Cdd:pfam02230 179 KEYLKTSLNKVELKIYEGLAHSICGRE 205
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
123-198 7.47e-04

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 39.92  E-value: 7.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705551 123 DWpgaIKDIRASVNWLKSNGsKKVGVTGMCMGGALAIASSVLVPEVDAVVgFYGtPSSELADPAQAKAPIQAHFGE 198
Cdd:COG1647    67 DW---LEDVEEAYEILKAGY-DKVIVIGLSMGGLLALLLAARYPDVAGLV-LLS-PALKIDDPSAPLLPLLKYLAR 136
 
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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