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Conserved domains on  [gi|950181763|ref|WP_057229197|]
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MULTISPECIES: DUF4442 domain-containing protein [unclassified Acidovorax]

Protein Classification

hotdog family protein( domain architecture ID 107)

hotdog family protein may have metabolic roles such as thioester hydrolysis in fatty acid metabolism and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 32-161 6.89e-30

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.


The actual alignment was detected with superfamily member pfam14539:

Pssm-ID: 469797  Cd Length: 131  Bit Score: 105.80  E-value: 6.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950181763   32 LRRAVPFTGTAGVKFVSLTPERVEVHLANEHRVQNHIGGVHASAMNLLAETATGMVVGMNVRDDCIPLAKELSMAFKKRA 111
Cdd:pfam14539   8 VCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMTVDYLAKA 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 950181763  112 TGGLKAVAMLTAEQRAAmlasdKGEVQVAVTVTDEAGVEPVECVFTWaWI 161
Cdd:pfam14539  88 TGDLTAVAELDPEDWGE-----KGDLPVPVEVRDDAGTEVVRATITL-WV 131
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 32-161 6.89e-30

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: 105.80  E-value: 6.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950181763   32 LRRAVPFTGTAGVKFVSLTPERVEVHLANEHRVQNHIGGVHASAMNLLAETATGMVVGMNVRDDCIPLAKELSMAFKKRA 111
Cdd:pfam14539   8 VCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMTVDYLAKA 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 950181763  112 TGGLKAVAMLTAEQRAAmlasdKGEVQVAVTVTDEAGVEPVECVFTWaWI 161
Cdd:pfam14539  88 TGDLTAVAELDPEDWGE-----KGDLPVPVEVRDDAGTEVVRATITL-WV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 34-165 7.42e-14

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 64.58  E-value: 7.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950181763  34 RAVPFTGTAGVKFVSLTPERVEVHLANEHRVQNHIGGVHASAMNLLAETATGMVVGMNVRDDCIPLAKELSMAFKKRATG 113
Cdd:COG2050   13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARL 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 950181763 114 GLKAVAmltaeqRAAMLASDKGEVQVAVTVTDEAGVEPVECVFTWAWIPSSR 165
Cdd:COG2050   93 GDRLTA------EARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 43-160 2.50e-10

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: 54.87  E-value: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950181763  43 GVKFVSLTPERVEVHLANEHRVQNHIGGVHASAMNLLAETATGMVVGMNVRDDCIPLAKELSMAFKKRATGG-LKAVAML 121
Cdd:cd03443    3 GIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGdLTARARV 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 950181763 122 TAEQRAAMLasdkgevqVAVTVTDEAGVEPVECVFTWAW 160
Cdd:cd03443   83 VKLGRRLAV--------VEVEVTDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 37-119 4.22e-03

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: 35.40  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950181763   37 PFTGTAGVKFVSLTPERVEVHLANEHRVQNHIGGVHASAMNLLAETATGMVVGMNVRDDCIPLAKELSMAFKKRATGG-L 115
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGkV 80


                  ....
gi 950181763  116 KAVA 119
Cdd:TIGR00369  81 RAIA 84
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 32-161 6.89e-30

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: 105.80  E-value: 6.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950181763   32 LRRAVPFTGTAGVKFVSLTPERVEVHLANEHRVQNHIGGVHASAMNLLAETATGMVVGMNVRDDCIPLAKELSMAFKKRA 111
Cdd:pfam14539   8 VCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMTVDYLAKA 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 950181763  112 TGGLKAVAMLTAEQRAAmlasdKGEVQVAVTVTDEAGVEPVECVFTWaWI 161
Cdd:pfam14539  88 TGDLTAVAELDPEDWGE-----KGDLPVPVEVRDDAGTEVVRATITL-WV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 34-165 7.42e-14

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 64.58  E-value: 7.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950181763  34 RAVPFTGTAGVKFVSLTPERVEVHLANEHRVQNHIGGVHASAMNLLAETATGMVVGMNVRDDCIPLAKELSMAFKKRATG 113
Cdd:COG2050   13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARL 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 950181763 114 GLKAVAmltaeqRAAMLASDKGEVQVAVTVTDEAGVEPVECVFTWAWIPSSR 165
Cdd:COG2050   93 GDRLTA------EARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 43-160 2.50e-10

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: 54.87  E-value: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950181763  43 GVKFVSLTPERVEVHLANEHRVQNHIGGVHASAMNLLAETATGMVVGMNVRDDCIPLAKELSMAFKKRATGG-LKAVAML 121
Cdd:cd03443    3 GIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGdLTARARV 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 950181763 122 TAEQRAAMLasdkgevqVAVTVTDEAGVEPVECVFTWAW 160
Cdd:cd03443   83 VKLGRRLAV--------VEVEVTDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 37-119 4.22e-03

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: 35.40  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950181763   37 PFTGTAGVKFVSLTPERVEVHLANEHRVQNHIGGVHASAMNLLAETATGMVVGMNVRDDCIPLAKELSMAFKKRATGG-L 115
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGkV 80


                  ....
gi 950181763  116 KAVA 119
Cdd:TIGR00369  81 RAIA 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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