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Conserved domains on  [gi|489513457|ref|WP_003418298|]
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MULTISPECIES: dienelactone hydrolase family protein [Mycobacterium]

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];
29-175 4.85e-15

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


:

Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 72.31  E-value: 4.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513457  29 LPGVVYTPEAGLHLPGVAFGHDWLTGTSRYSGLLEHLASWGIVAAAPDSERGLAPSV-------LNLAFDLGVAL-DIVA 100
Cdd:COG0412   16 LPGYLARPAGGGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDdpdearaLMGALDPELLAaDLRA 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489513457 101 GVRLGPGKISVHPAKLGLVGHGFGGSAAVFAAAglTGTHVKSVAAIFPTVTNPAAEQPAATLDVPGLILTAPGDP 175
Cdd:COG0412   96 ALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAA--RGPDLAAAVSFYGGLPADDLLDLAARIKAPVLLLYGEKDP 168
 
Name Accession Description Interval E-value
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
29-175 4.85e-15

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 72.31  E-value: 4.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513457  29 LPGVVYTPEAGLHLPGVAFGHDWLTGTSRYSGLLEHLASWGIVAAAPDSERGLAPSV-------LNLAFDLGVAL-DIVA 100
Cdd:COG0412   16 LPGYLARPAGGGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDdpdearaLMGALDPELLAaDLRA 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489513457 101 GVRLGPGKISVHPAKLGLVGHGFGGSAAVFAAAglTGTHVKSVAAIFPTVTNPAAEQPAATLDVPGLILTAPGDP 175
Cdd:COG0412   96 ALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAA--RGPDLAAAVSFYGGLPADDLLDLAARIKAPVLLLYGEKDP 168
Chlorophyllase2 pfam12740
Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC: ...
29-147 1.60e-05

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: 45.00  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513457   29 LPGVVYTP-EAGLHlPGVAFGHDWLTGTSRYSGLLEHLASWGIVAAAPDSERGLAPSVLNLAFDLGVALDIVAGV--RLG 105
Cdd:pfam12740   4 KPLLVFTPtEAGTY-PVLLFLHGYLLYNSFYSQLLQHIASHGFIVVAPQLYLVAGPDGDEIKSAAKVANWLSNGLqhVLP 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489513457  106 PGkisVHPA--KLGLVGHGFGGSAAVFAAAGLTGTHVKSVAAIF 147
Cdd:pfam12740  83 EG---VEPDlsKLALSGHSRGGKTAFALALGHAKTSLKFSALIG 123
PLN00021 PLN00021
chlorophyllase
29-133 6.70e-04

chlorophyllase


Pssm-ID: 177659  Cd Length: 313  Bit Score: 40.42  E-value: 6.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513457  29 LPGVVYTP-EAGLHlPGVAFGHDWLTGTSRYSGLLEHLASWGIVAAAPD----------SERGLAPSVLN-LAFDLGVAL 96
Cdd:PLN00021  39 KPLLVATPsEAGTY-PVLLFLHGYLLYNSFYSQLLQHIASHGFIVVAPQlytlagpdgtDEIKDAAAVINwLSSGLAAVL 117
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489513457  97 divagvrlgPGKISVHPAKLGLVGHGFGGSAAvFAAA 133
Cdd:PLN00021 118 ---------PEGVRPDLSKLALAGHSRGGKTA-FALA 144
 
Name Accession Description Interval E-value
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
29-175 4.85e-15

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 72.31  E-value: 4.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513457  29 LPGVVYTPEAGLHLPGVAFGHDWLTGTSRYSGLLEHLASWGIVAAAPDSERGLAPSV-------LNLAFDLGVAL-DIVA 100
Cdd:COG0412   16 LPGYLARPAGGGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDdpdearaLMGALDPELLAaDLRA 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489513457 101 GVRLGPGKISVHPAKLGLVGHGFGGSAAVFAAAglTGTHVKSVAAIFPTVTNPAAEQPAATLDVPGLILTAPGDP 175
Cdd:COG0412   96 ALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAA--RGPDLAAAVSFYGGLPADDLLDLAARIKAPVLLLYGEKDP 168
Chlorophyllase2 pfam12740
Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC: ...
29-147 1.60e-05

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: 45.00  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513457   29 LPGVVYTP-EAGLHlPGVAFGHDWLTGTSRYSGLLEHLASWGIVAAAPDSERGLAPSVLNLAFDLGVALDIVAGV--RLG 105
Cdd:pfam12740   4 KPLLVFTPtEAGTY-PVLLFLHGYLLYNSFYSQLLQHIASHGFIVVAPQLYLVAGPDGDEIKSAAKVANWLSNGLqhVLP 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489513457  106 PGkisVHPA--KLGLVGHGFGGSAAVFAAAGLTGTHVKSVAAIF 147
Cdd:pfam12740  83 EG---VEPDlsKLALSGHSRGGKTAFALALGHAKTSLKFSALIG 123
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
29-155 2.83e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 44.24  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513457  29 LPGVVYTPEAGLHLPGVAFGHDWLTGTSR-YSGLLEHLASWGIVAAAPDSeRGLAPSVLNLAFDLgvALDIVAGVRLGPG 107
Cdd:COG1506   10 LPGWLYLPADGKKYPVVVYVHGGPGSRDDsFLPLAQALASRGYAVLAPDY-RGYGESAGDWGGDE--VDDVLAAIDYLAA 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489513457 108 KISVHPAKLGLVGHGFGGsAAVFAAAGLTGTHVKSVAAIFPtVTNPAA 155
Cdd:COG1506   87 RPYVDPDRIGIYGHSYGG-YMALLAAARHPDRFKAAVALAG-VSDLRS 132
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
29-201 4.05e-04

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 40.76  E-value: 4.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513457  29 LPGVVYTPEAGlHLPGVAFGHDWLTGTSRYSGLLEHLASWGIVAAAPD--------SERGLAPSVLNLAFDLGVALDIVA 100
Cdd:COG2267   16 LRGRRWRPAGS-PRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDlrghgrsdGPRGHVDSFDDYVDDLRAALDALR 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513457 101 gvrlgpgkiSVHPAKLGLVGHGFGGSAAVFAAAGLtGTHVKSVAAI-------------FPTVTNPAAEQPAATLDVPGL 167
Cdd:COG2267   95 ---------ARPGLPVVLLGHSMGGLIALLYAARY-PDRVAGLVLLapayradpllgpsARWLRALRLAEALARIDVPVL 164
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489513457 168 ILTAPGDPKTLTSNALGLSRAW-DKATLRIVSKAR 201
Cdd:COG2267  165 VLHGGADRVVPPEAARRLAARLsPDVELVLLPGAR 199
PLN00021 PLN00021
chlorophyllase
29-133 6.70e-04

chlorophyllase


Pssm-ID: 177659  Cd Length: 313  Bit Score: 40.42  E-value: 6.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513457  29 LPGVVYTP-EAGLHlPGVAFGHDWLTGTSRYSGLLEHLASWGIVAAAPD----------SERGLAPSVLN-LAFDLGVAL 96
Cdd:PLN00021  39 KPLLVATPsEAGTY-PVLLFLHGYLLYNSFYSQLLQHIASHGFIVVAPQlytlagpdgtDEIKDAAAVINwLSSGLAAVL 117
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489513457  97 divagvrlgPGKISVHPAKLGLVGHGFGGSAAvFAAA 133
Cdd:PLN00021 118 ---------PEGVRPDLSKLALAGHSRGGKTA-FALA 144
 
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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