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Conserved domains on  [gi|491232874|ref|WP_005091106|]
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MULTISPECIES: hotdog fold domain-containing protein [Acinetobacter]

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 ...
 18-150 1.27e-66

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: 198.64  E-value: 1.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491232874   18 KWTFTRMLCLKAPYFSSIAPLFEELKPNYCKISIKKKRSVLNHIGTVHAIAMCNMAELAGGTMTEVTVPSSHRWIPKGMT 97
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 491232874   98 VEYLKKAETDLIAIATPVEEnyDWDKAGEYLVNVDVFDKANEKVFHAKITMWI 150
Cdd:pfam14539  81 VDYLAKATGDLTAVAELDPE--DWGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 18-150 1.27e-66

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: 198.64  E-value: 1.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491232874   18 KWTFTRMLCLKAPYFSSIAPLFEELKPNYCKISIKKKRSVLNHIGTVHAIAMCNMAELAGGTMTEVTVPSSHRWIPKGMT 97
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 491232874   98 VEYLKKAETDLIAIATPVEEnyDWDKAGEYLVNVDVFDKANEKVFHAKITMWI 150
Cdd:pfam14539  81 VDYLAKATGDLTAVAELDPE--DWGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 28-155 1.24e-18

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 76.91  E-value: 1.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491232874  28 KAPYFSSIAPLFEELKPNYCKISIKKKRSVLNHIGTVHAIAMCNMAELAGGTMTEVTVPSSHRWIPKGMTVEYLKKAE-- 105
Cdd:COG2050   14 ANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARlg 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491232874 106 TDLIAIATPVeenydwdKAGE--YLVNVDVFDKANEKVFHAKITMWISKKKK 155
Cdd:COG2050   94 DRLTAEARVV-------RRGRrlAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 39-148 7.54e-14

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: 63.73  E-value: 7.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491232874  39 FEELKPNYCKISIKKKRSVLNHIGTVHAIAMCNMAELAGGTMTEVTVPSSHRWIPKGMTVEYLKKA-ETDLIAIATPVee 117
Cdd:cd03443    6 VVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPArGGDLTARARVV-- 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491232874 118 nydwdKAGEYLVNVD--VFDKANEKVFHAKITM 148
Cdd:cd03443   84 -----KLGRRLAVVEveVTDEDGKLVATARGTF 111
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 18-150 1.27e-66

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: 198.64  E-value: 1.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491232874   18 KWTFTRMLCLKAPYFSSIAPLFEELKPNYCKISIKKKRSVLNHIGTVHAIAMCNMAELAGGTMTEVTVPSSHRWIPKGMT 97
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 491232874   98 VEYLKKAETDLIAIATPVEEnyDWDKAGEYLVNVDVFDKANEKVFHAKITMWI 150
Cdd:pfam14539  81 VDYLAKATGDLTAVAELDPE--DWGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 28-155 1.24e-18

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 76.91  E-value: 1.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491232874  28 KAPYFSSIAPLFEELKPNYCKISIKKKRSVLNHIGTVHAIAMCNMAELAGGTMTEVTVPSSHRWIPKGMTVEYLKKAE-- 105
Cdd:COG2050   14 ANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARlg 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491232874 106 TDLIAIATPVeenydwdKAGE--YLVNVDVFDKANEKVFHAKITMWISKKKK 155
Cdd:COG2050   94 DRLTAEARVV-------RRGRrlAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 39-148 7.54e-14

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: 63.73  E-value: 7.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491232874  39 FEELKPNYCKISIKKKRSVLNHIGTVHAIAMCNMAELAGGTMTEVTVPSSHRWIPKGMTVEYLKKA-ETDLIAIATPVee 117
Cdd:cd03443    6 VVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPArGGDLTARARVV-- 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491232874 118 nydwdKAGEYLVNVD--VFDKANEKVFHAKITM 148
Cdd:cd03443   84 -----KLGRRLAVVEveVTDEDGKLVATARGTF 111
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 58-148 8.95e-03

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 33.99  E-value: 8.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491232874  58 LNHIGTVHAIAMCNMAELAGGTMTEVTVPSSHRWIPKGMTVEYLK--KAETDLIAIATPVeenydWDKAGEYLVNVDVFD 135
Cdd:cd03440   12 IDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRpvRPGDTLTVEAEVV-----RVGRSSVTVEVEVRN 86

                         90
                 ....*....|...
gi 491232874 136 KANEKVFHAKITM 148
Cdd:cd03440   87 EDGKLVATATATF 99
 
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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