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Conserved domains on  [gi|296848656|gb|ADH70674|]
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conserved hypothetical protein [Nocardiopsis dassonvillei subsp. dassonvillei DSM 43111]

Protein Classification

hotdog fold domain-containing protein( domain architecture ID 10629414)

hotdog fold domain-containing protein belonging to the hotdog fold superfamily of thioesterases and dehydratases, similar to PaaI family thioesterases

CATH:  3.10.129.10
PubMed:  15307895
SCOP:  3000149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 9-150 8.73e-43

Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important.


:

Pssm-ID: 434027  Cd Length: 131  Bit Score: 138.16  E-value: 8.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296848656    9 AEAVKAGFLAAVPFVRTLGLTFTELDHGRAVMRLPDNADHHNHVGGPHAGAMFTLAESASGAIIIGTFGdqlDRAVPLPT 88
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLP---DTHRWIPK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296848656   89 TSTIDFLKIATGDLTAEAVLGRPreeiiaelDEGRRPEFPIDVELRTEDGTVTGRMSITWTL 150
Cdd:pfam14539  78 GMTVDYLAKATGDLTAVAELDPE--------DWGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 9-150 8.73e-43

Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important.


Pssm-ID: 434027  Cd Length: 131  Bit Score: 138.16  E-value: 8.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296848656    9 AEAVKAGFLAAVPFVRTLGLTFTELDHGRAVMRLPDNADHHNHVGGPHAGAMFTLAESASGAIIIGTFGdqlDRAVPLPT 88
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLP---DTHRWIPK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296848656   89 TSTIDFLKIATGDLTAEAVLGRPreeiiaelDEGRRPEFPIDVELRTEDGTVTGRMSITWTL 150
Cdd:pfam14539  78 GMTVDYLAKATGDLTAVAELDPE--------DWGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 4-155 9.54e-23

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 87.31  E-value: 9.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296848656   4 MNPETAEAvkAGFLAAVPFVRTLGLTFTELDHGRAVMRLPDNADHHNHVGGPHAGAMFTLAESASGAIIIGTFGdqlDRA 83
Cdd:COG2050    1 MSDPLERL--EGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALP---PGR 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296848656  84 VPLPTTSTIDFLKIAT--GDLTAEAVlgrpreeiiaELDEGRRPEFpIDVELRTEDGTVTGRMSITWTLRPNRK 155
Cdd:COG2050   76 RAVTIELNINFLRPARlgDRLTAEAR----------VVRRGRRLAV-VEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 25-148 6.64e-17

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 71.43  E-value: 6.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296848656  25 TLGLTFTELDHGRAVMRLPDNADHHNHVGGPHAGAMFTLAESASGAIIIGTfgdqLDRAVPLPTTS-TIDFLKIAT-GDL 102
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSA----LPPGALAVTVDlNVNYLRPARgGDL 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 296848656 103 TAEAVLgrpreeiiaeLDEGRRpEFPIDVELRTEDGTVTGRMSITW 148
Cdd:cd03443   77 TARARV----------VKLGRR-LAVVEVEVTDEDGKLVATARGTF 111
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 21-106 2.74e-06

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 43.87  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296848656   21 PFVRTLGLTFTELDHGRAVMRLPDNADHHNHVGGPHAGAMFTLAESA-SGAIIIGTFGDQLDRAVPLpttsTIDFLKIAT 99
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAgSAAGYLCNSGGQAVVGLEL----NANHLRPAR 76


                  ....*...
gi 296848656  100 -GDLTAEA 106
Cdd:TIGR00369  77 eGKVRAIA 84
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 9-150 8.73e-43

Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important.


Pssm-ID: 434027  Cd Length: 131  Bit Score: 138.16  E-value: 8.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296848656    9 AEAVKAGFLAAVPFVRTLGLTFTELDHGRAVMRLPDNADHHNHVGGPHAGAMFTLAESASGAIIIGTFGdqlDRAVPLPT 88
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLP---DTHRWIPK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296848656   89 TSTIDFLKIATGDLTAEAVLGRPreeiiaelDEGRRPEFPIDVELRTEDGTVTGRMSITWTL 150
Cdd:pfam14539  78 GMTVDYLAKATGDLTAVAELDPE--------DWGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 4-155 9.54e-23

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 87.31  E-value: 9.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296848656   4 MNPETAEAvkAGFLAAVPFVRTLGLTFTELDHGRAVMRLPDNADHHNHVGGPHAGAMFTLAESASGAIIIGTFGdqlDRA 83
Cdd:COG2050    1 MSDPLERL--EGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALP---PGR 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296848656  84 VPLPTTSTIDFLKIAT--GDLTAEAVlgrpreeiiaELDEGRRPEFpIDVELRTEDGTVTGRMSITWTLRPNRK 155
Cdd:COG2050   76 RAVTIELNINFLRPARlgDRLTAEAR----------VVRRGRRLAV-VEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 25-148 6.64e-17

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 71.43  E-value: 6.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296848656  25 TLGLTFTELDHGRAVMRLPDNADHHNHVGGPHAGAMFTLAESASGAIIIGTfgdqLDRAVPLPTTS-TIDFLKIAT-GDL 102
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSA----LPPGALAVTVDlNVNYLRPARgGDL 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 296848656 103 TAEAVLgrpreeiiaeLDEGRRpEFPIDVELRTEDGTVTGRMSITW 148
Cdd:cd03443   77 TARARV----------VKLGRR-LAVVEVEVTDEDGKLVATARGTF 111
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 21-106 2.74e-06

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 43.87  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296848656   21 PFVRTLGLTFTELDHGRAVMRLPDNADHHNHVGGPHAGAMFTLAESA-SGAIIIGTFGDQLDRAVPLpttsTIDFLKIAT 99
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAgSAAGYLCNSGGQAVVGLEL----NANHLRPAR 76


                  ....*...
gi 296848656  100 -GDLTAEA 106
Cdd:TIGR00369  77 eGKVRAIA 84
 
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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