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Conserved domains on  [gi|1002271514|ref|XP_015640091|]
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endo-1,3;1,4-beta-D-glucanase isoform X2 [Oryza sativa Japonica Group]

Protein Classification

dienelactone hydrolase family protein( domain architecture ID 10785456)

dienelactone hydrolase family protein plays a crucial role in chlorocatechol degradation via the modified ortho cleavage pathway

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917
SCOP:  3000102

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
30-198 1.28e-19

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


:

Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 83.48  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271514  30 KAYVA--GSAGSKAAVVLISDAFGFEaPNLRKIADKVALFGYFVVVPDFLHGDPYqPDNPNNPGIWLQSHNPKEAFEEAK 107
Cdd:COG0412    17 PGYLArpAGGGPRPGVVVLHEIFGLN-PHIRDVARRLAAAGYVVLAPDLYGRGGP-GDDPDEARALMGALDPELLAADLR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271514 108 PVIAALK---EKGASFIGAAGYCWGAKVVVELG-KVHEIQAAVLLHPSLLA---VDDIKEVKCPISILGAEIDKTSPPEL 180
Cdd:COG0412    95 AALDWLKaqpEVDAGRVGVVGFCFGGGLALLAAaRGPDLAAAVSFYGGLPAddlLDLAARIKAPVLLLYGEKDPLVPPEQ 174

                         170
                  ....*....|....*....
gi 1002271514 181 LKQFEQIL-SPNPEFRLKI 198
Cdd:COG0412   175 VAALEAALaAAGVDVELHV 193
 
Name Accession Description Interval E-value
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
30-198 1.28e-19

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 83.48  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271514  30 KAYVA--GSAGSKAAVVLISDAFGFEaPNLRKIADKVALFGYFVVVPDFLHGDPYqPDNPNNPGIWLQSHNPKEAFEEAK 107
Cdd:COG0412    17 PGYLArpAGGGPRPGVVVLHEIFGLN-PHIRDVARRLAAAGYVVLAPDLYGRGGP-GDDPDEARALMGALDPELLAADLR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271514 108 PVIAALK---EKGASFIGAAGYCWGAKVVVELG-KVHEIQAAVLLHPSLLA---VDDIKEVKCPISILGAEIDKTSPPEL 180
Cdd:COG0412    95 AALDWLKaqpEVDAGRVGVVGFCFGGGLALLAAaRGPDLAAAVSFYGGLPAddlLDLAARIKAPVLLLYGEKDPLVPPEQ 174

                         170
                  ....*....|....*....
gi 1002271514 181 LKQFEQIL-SPNPEFRLKI 198
Cdd:COG0412   175 VAALEAALaAAGVDVELHV 193
DLH pfam01738
Dienelactone hydrolase family;
31-198 1.80e-18

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 80.09  E-value: 1.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271514  31 AYVAGSAGSKA-AVVLISDAFGFEaPNLRKIADKVALFGYFVVVPDFLHGDPYQPDNPNNPGIWLQSHNpKEAFEEAKP- 108
Cdd:pfam01738   2 AYLATPKNPPWpVVVVFQEIFGVN-DNIREIADRLADEGYVALAPDLYFRQGDPNDEADAARAMFELVS-KRVMEKVLDd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271514 109 ---VIAALK---EKGASFIGAAGYCWGAKVVVEL-GKVHEIQAAVLLHPSLLA--VDDIKEVKCPISILGAEIDKTSPPE 179
Cdd:pfam01738  80 leaAVNYLKsqpEVSPKKVGVVGYCMGGALAVLLaAKGPLVDAAVGFYGVGPEppLIEAPDIKAPILFHFGEEDHFVPAD 159

                         170       180
                  ....*....|....*....|
gi 1002271514 180 LLKQFEQILSP-NPEFRLKI 198
Cdd:pfam01738 160 SRELIEEALKAaNVDHQIHS 179
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
 16-70 8.25e-04

Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This group includes proteins identified as the Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. The Arabidopsis enzyme, a member of the medium chain dehydrogenase/reductase family, catalyzes the reduction of 7-8-double bond of phenylpropanal substrates as a plant defense mechanism. Prostaglandins and related eicosanoids (lipid mediators involved in host defense and inflamation) are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. Leukotriene B4 (LTB4) can be metabolized by LTB4 20-hydroxylase in inflamatory cells, and in other cells by bifunctional LTB4 12-HD/PGR. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176255 [Multi-domain]  Cd Length: 338  Bit Score: 39.61  E-value: 8.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002271514  16 AGGGGEVVGDFGGQKA-YVAGSAGSKAAVVLISDAFGF-EAPNLRKIAD-KVALFGYF 70
Cdd:cd08295   161 SGAVGQLVGQLAKLKGcYVVGSAGSDEKVDLLKNKLGFdDAFNYKEEPDlDAALKRYF 218
 
Name Accession Description Interval E-value
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
30-198 1.28e-19

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 83.48  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271514  30 KAYVA--GSAGSKAAVVLISDAFGFEaPNLRKIADKVALFGYFVVVPDFLHGDPYqPDNPNNPGIWLQSHNPKEAFEEAK 107
Cdd:COG0412    17 PGYLArpAGGGPRPGVVVLHEIFGLN-PHIRDVARRLAAAGYVVLAPDLYGRGGP-GDDPDEARALMGALDPELLAADLR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271514 108 PVIAALK---EKGASFIGAAGYCWGAKVVVELG-KVHEIQAAVLLHPSLLA---VDDIKEVKCPISILGAEIDKTSPPEL 180
Cdd:COG0412    95 AALDWLKaqpEVDAGRVGVVGFCFGGGLALLAAaRGPDLAAAVSFYGGLPAddlLDLAARIKAPVLLLYGEKDPLVPPEQ 174

                         170
                  ....*....|....*....
gi 1002271514 181 LKQFEQIL-SPNPEFRLKI 198
Cdd:COG0412   175 VAALEAALaAAGVDVELHV 193
DLH pfam01738
Dienelactone hydrolase family;
31-198 1.80e-18

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 80.09  E-value: 1.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271514  31 AYVAGSAGSKA-AVVLISDAFGFEaPNLRKIADKVALFGYFVVVPDFLHGDPYQPDNPNNPGIWLQSHNpKEAFEEAKP- 108
Cdd:pfam01738   2 AYLATPKNPPWpVVVVFQEIFGVN-DNIREIADRLADEGYVALAPDLYFRQGDPNDEADAARAMFELVS-KRVMEKVLDd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271514 109 ---VIAALK---EKGASFIGAAGYCWGAKVVVEL-GKVHEIQAAVLLHPSLLA--VDDIKEVKCPISILGAEIDKTSPPE 179
Cdd:pfam01738  80 leaAVNYLKsqpEVSPKKVGVVGYCMGGALAVLLaAKGPLVDAAVGFYGVGPEppLIEAPDIKAPILFHFGEEDHFVPAD 159

                         170       180
                  ....*....|....*....|
gi 1002271514 180 LLKQFEQILSP-NPEFRLKI 198
Cdd:pfam01738 160 SRELIEEALKAaNVDHQIHS 179
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
 16-70 8.25e-04

Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This group includes proteins identified as the Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. The Arabidopsis enzyme, a member of the medium chain dehydrogenase/reductase family, catalyzes the reduction of 7-8-double bond of phenylpropanal substrates as a plant defense mechanism. Prostaglandins and related eicosanoids (lipid mediators involved in host defense and inflamation) are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. Leukotriene B4 (LTB4) can be metabolized by LTB4 20-hydroxylase in inflamatory cells, and in other cells by bifunctional LTB4 12-HD/PGR. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176255 [Multi-domain]  Cd Length: 338  Bit Score: 39.61  E-value: 8.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002271514  16 AGGGGEVVGDFGGQKA-YVAGSAGSKAAVVLISDAFGF-EAPNLRKIAD-KVALFGYF 70
Cdd:cd08295   161 SGAVGQLVGQLAKLKGcYVVGSAGSDEKVDLLKNKLGFdDAFNYKEEPDlDAALKRYF 218
 
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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