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Conserved domains on  [gi|495541637|ref|WP_008266216|]
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DAPG hydrolase family protein [Stenotrophomonas sp. SKA14]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAPG_hydrolase super family cl39484
DAPG hydrolase PhiG domain; This domain is found in 2,4-diacetylphloroglucinol hydrolase PhiG ...
 10-218 6.26e-50

DAPG hydrolase PhiG domain; This domain is found in 2,4-diacetylphloroglucinol hydrolase PhiG present in Pseudomonas fluorescens. 2,4-diacetylphloroglucinol hydrolase is the gene product of PhiG that is responsible for cleaving toxic 2,4-diacetylphloroglucinol (DAPG). The small N-terminal region of the domain is involved in dimerization through hydrogen bonding of the dimer interface. The C-terminal catalytic region resembles the tetracenomycin aromatase/cyclase and has a Bet v1-like fold. DAPG PhiG is the first discovered hydrolase whose catalytic domain belongs to the Bet v1-like fold, rather than the classical alpha/beta-fold hydrolases.


The actual alignment was detected with superfamily member pfam18089:

Pssm-ID: 465645  Cd Length: 224  Bit Score: 162.56  E-value: 6.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495541637   10 WLDHHDLLDPAPMRLETGIQRREDGTLRVAVRIDLHGCKGRMLDWWFTFFET-TQHIRWWHPLDHVEHRGWDAAWQRGRS 88
Cdd:pfam18089   4 IEDINRLLEPGYLPVENGYCILPDGTGYVASLTFMPGVTAEMIDWWFAWHPLeSLRYKIWFPEAHYGISVLDPDRLLDPS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495541637   89 ------YHGASIHAVESLADIpPVAARLKFHDPRTL-LVPERLQvaqdAGDVSAVIAARIGFGDHVRLDAhgdpcdGQML 161
Cdd:pfam18089  84 lsmkerYWGNTHYVVEDVGNG-PQDLHISFVSPEEFgFDPELLK----EKKIAAIVCAVVGDGGEPNLKA------TVMV 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495541637  162 HVARDTPFGCVLRSRFVLG---------------LDSAEPQRDASDAVGLGLLKHCYTEFSFLSRLLPSLYY 218
Cdd:pfam18089 153 HFVRETEGGVELRSRFWLGyqvvrvppldragklVKTLPDGVAIPEELAQGLARHCVKEFTNLASILPELYA 224
 
Name Accession Description Interval E-value
DAPG_hydrolase pfam18089
DAPG hydrolase PhiG domain; This domain is found in 2,4-diacetylphloroglucinol hydrolase PhiG ...
 10-218 6.26e-50

DAPG hydrolase PhiG domain; This domain is found in 2,4-diacetylphloroglucinol hydrolase PhiG present in Pseudomonas fluorescens. 2,4-diacetylphloroglucinol hydrolase is the gene product of PhiG that is responsible for cleaving toxic 2,4-diacetylphloroglucinol (DAPG). The small N-terminal region of the domain is involved in dimerization through hydrogen bonding of the dimer interface. The C-terminal catalytic region resembles the tetracenomycin aromatase/cyclase and has a Bet v1-like fold. DAPG PhiG is the first discovered hydrolase whose catalytic domain belongs to the Bet v1-like fold, rather than the classical alpha/beta-fold hydrolases.


Pssm-ID: 465645  Cd Length: 224  Bit Score: 162.56  E-value: 6.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495541637   10 WLDHHDLLDPAPMRLETGIQRREDGTLRVAVRIDLHGCKGRMLDWWFTFFET-TQHIRWWHPLDHVEHRGWDAAWQRGRS 88
Cdd:pfam18089   4 IEDINRLLEPGYLPVENGYCILPDGTGYVASLTFMPGVTAEMIDWWFAWHPLeSLRYKIWFPEAHYGISVLDPDRLLDPS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495541637   89 ------YHGASIHAVESLADIpPVAARLKFHDPRTL-LVPERLQvaqdAGDVSAVIAARIGFGDHVRLDAhgdpcdGQML 161
Cdd:pfam18089  84 lsmkerYWGNTHYVVEDVGNG-PQDLHISFVSPEEFgFDPELLK----EKKIAAIVCAVVGDGGEPNLKA------TVMV 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495541637  162 HVARDTPFGCVLRSRFVLG---------------LDSAEPQRDASDAVGLGLLKHCYTEFSFLSRLLPSLYY 218
Cdd:pfam18089 153 HFVRETEGGVELRSRFWLGyqvvrvppldragklVKTLPDGVAIPEELAQGLARHCVKEFTNLASILPELYA 224
 
Name Accession Description Interval E-value
DAPG_hydrolase pfam18089
DAPG hydrolase PhiG domain; This domain is found in 2,4-diacetylphloroglucinol hydrolase PhiG ...
 10-218 6.26e-50

DAPG hydrolase PhiG domain; This domain is found in 2,4-diacetylphloroglucinol hydrolase PhiG present in Pseudomonas fluorescens. 2,4-diacetylphloroglucinol hydrolase is the gene product of PhiG that is responsible for cleaving toxic 2,4-diacetylphloroglucinol (DAPG). The small N-terminal region of the domain is involved in dimerization through hydrogen bonding of the dimer interface. The C-terminal catalytic region resembles the tetracenomycin aromatase/cyclase and has a Bet v1-like fold. DAPG PhiG is the first discovered hydrolase whose catalytic domain belongs to the Bet v1-like fold, rather than the classical alpha/beta-fold hydrolases.


Pssm-ID: 465645  Cd Length: 224  Bit Score: 162.56  E-value: 6.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495541637   10 WLDHHDLLDPAPMRLETGIQRREDGTLRVAVRIDLHGCKGRMLDWWFTFFET-TQHIRWWHPLDHVEHRGWDAAWQRGRS 88
Cdd:pfam18089   4 IEDINRLLEPGYLPVENGYCILPDGTGYVASLTFMPGVTAEMIDWWFAWHPLeSLRYKIWFPEAHYGISVLDPDRLLDPS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495541637   89 ------YHGASIHAVESLADIpPVAARLKFHDPRTL-LVPERLQvaqdAGDVSAVIAARIGFGDHVRLDAhgdpcdGQML 161
Cdd:pfam18089  84 lsmkerYWGNTHYVVEDVGNG-PQDLHISFVSPEEFgFDPELLK----EKKIAAIVCAVVGDGGEPNLKA------TVMV 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495541637  162 HVARDTPFGCVLRSRFVLG---------------LDSAEPQRDASDAVGLGLLKHCYTEFSFLSRLLPSLYY 218
Cdd:pfam18089 153 HFVRETEGGVELRSRFWLGyqvvrvppldragklVKTLPDGVAIPEELAQGLARHCVKEFTNLASILPELYA 224
 
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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