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Conserved domains on  [gi|490929796|ref|WP_004791649|]
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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 ...
 39-165 6.18e-55

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: 169.75  E-value: 6.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929796   39 LLSKVVSREAPYFQTVNPMIQKLDLNVCEASIKKNKSIENHIGTVHVIAICNGLEFVMGVLAEASVPQHLRWLPKGMNVN 118
Cdd:pfam14539   3 LFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMTVD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 490929796  119 YVAKADSDIKLVATIDDE-WKV-GDMQVKVNAYRADGQPVVQGYITLWV 165
Cdd:pfam14539  83 YLAKATGDLTAVAELDPEdWGEkGDLPVPVEVRDDAGTEVVRATITLWV 131
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 39-165 6.18e-55

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: 169.75  E-value: 6.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929796   39 LLSKVVSREAPYFQTVNPMIQKLDLNVCEASIKKNKSIENHIGTVHVIAICNGLEFVMGVLAEASVPQHLRWLPKGMNVN 118
Cdd:pfam14539   3 LFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMTVD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 490929796  119 YVAKADSDIKLVATIDDE-WKV-GDMQVKVNAYRADGQPVVQGYITLWV 165
Cdd:pfam14539  83 YLAKATGDLTAVAELDPEdWGEkGDLPVPVEVRDDAGTEVVRATITLWV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 46-169 2.27e-13

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 63.42  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929796  46 REAPYFQTVNPMIQKLDLNVCEASIKKNKSIENHIGTVHVIAICNGLEFVMGVLAEASVPQHLRWLPKGMNVNYVAKADS 125
Cdd:COG2050   13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARL 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490929796 126 DIKLVAT---IDDEWKVGDMQVKVnaYRADGQPVVQGYITLWVTEKK 169
Cdd:COG2050   93 GDRLTAEarvVRRGRRLAVVEVEV--TDEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 66-159 1.12e-05

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: 42.16  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929796  66 CEASIKKNKSIENHIGTVHVIAICNGLEFVMGVLAEASVPQHLRWLPKGMNVNYVAKA-DSDIKLVATIDdewKVGD--M 142
Cdd:cd03443   14 VVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPArGGDLTARARVV---KLGRrlA 90

                         90
                 ....*....|....*..
gi 490929796 143 QVKVNAYRADGQPVVQG 159
Cdd:cd03443   91 VVEVEVTDEDGKLVATA 107
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 39-165 6.18e-55

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: 169.75  E-value: 6.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929796   39 LLSKVVSREAPYFQTVNPMIQKLDLNVCEASIKKNKSIENHIGTVHVIAICNGLEFVMGVLAEASVPQHLRWLPKGMNVN 118
Cdd:pfam14539   3 LFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMTVD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 490929796  119 YVAKADSDIKLVATIDDE-WKV-GDMQVKVNAYRADGQPVVQGYITLWV 165
Cdd:pfam14539  83 YLAKATGDLTAVAELDPEdWGEkGDLPVPVEVRDDAGTEVVRATITLWV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 46-169 2.27e-13

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 63.42  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929796  46 REAPYFQTVNPMIQKLDLNVCEASIKKNKSIENHIGTVHVIAICNGLEFVMGVLAEASVPQHLRWLPKGMNVNYVAKADS 125
Cdd:COG2050   13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARL 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490929796 126 DIKLVAT---IDDEWKVGDMQVKVnaYRADGQPVVQGYITLWVTEKK 169
Cdd:COG2050   93 GDRLTAEarvVRRGRRLAVVEVEV--TDEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 66-159 1.12e-05

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: 42.16  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929796  66 CEASIKKNKSIENHIGTVHVIAICNGLEFVMGVLAEASVPQHLRWLPKGMNVNYVAKA-DSDIKLVATIDdewKVGD--M 142
Cdd:cd03443   14 VVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPArGGDLTARARVV---KLGRrlA 90

                         90
                 ....*....|....*..
gi 490929796 143 QVKVNAYRADGQPVVQG 159
Cdd:cd03443   91 VVEVEVTDEDGKLVATA 107
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 78-163 1.03e-04

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: 39.38  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929796  78 NHIGTVHVIAICNGLEFVMGVLAEASVPQHLRWLPKGMNVNYV--AKADSDIKLVATIDdewKVGD--MQVKVNAYRADG 153
Cdd:cd03440   13 DGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLrpVRPGDTLTVEAEVV---RVGRssVTVEVEVRNEDG 89

                         90
                 ....*....|
gi 490929796 154 QPVVQGYITL 163
Cdd:cd03440   90 KLVATATATF 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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