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Conserved domains on  [gi|795469842|ref|XP_011767679|]
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LOW QUALITY PROTEIN: acyl-coenzyme A thioesterase THEM5 [Macaca nemestrina]

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 ...
 143-192 1.69e-05

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 cd03443:

Pssm-ID: 469797 [Multi-domain]  Cd Length: 113  Bit Score: 42.93  E-value: 1.69e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 795469842 143 VCLFQPGPYLEGPPGFTHSGSLAAMMDETFS---KTAFLAGEGVFTLSFNIRF 192
Cdd:cd03443   15 VLRLPVRPRHLNPGGIVHGGAIATLADTAGGlaaLSALPPGALAVTVDLNVNY 67
 
Name Accession Description Interval E-value
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 143-192 1.69e-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: 42.93  E-value: 1.69e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 795469842 143 VCLFQPGPYLEGPPGFTHSGSLAAMMDETFS---KTAFLAGEGVFTLSFNIRF 192
Cdd:cd03443   15 VLRLPVRPRHLNPGGIVHGGAIATLADTAGGlaaLSALPPGALAVTVDLNVNY 67
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 143-192 2.43e-05

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 43.01  E-value: 2.43e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 795469842 143 VCLFQPGPYLEGPPGFTHSGSLAAMMDETFSKTAFLA---GEGVFTLSFNIRF 192
Cdd:COG2050   34 VLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlppGRRAVTIELNINF 86
 
Name Accession Description Interval E-value
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 143-192 1.69e-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: 42.93  E-value: 1.69e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 795469842 143 VCLFQPGPYLEGPPGFTHSGSLAAMMDETFS---KTAFLAGEGVFTLSFNIRF 192
Cdd:cd03443   15 VLRLPVRPRHLNPGGIVHGGAIATLADTAGGlaaLSALPPGALAVTVDLNVNY 67
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 143-192 2.43e-05

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 43.01  E-value: 2.43e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 795469842 143 VCLFQPGPYLEGPPGFTHSGSLAAMMDETFSKTAFLA---GEGVFTLSFNIRF 192
Cdd:COG2050   34 VLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlppGRRAVTIELNINF 86
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 143-232 9.44e-05

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: 40.54  E-value: 9.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795469842 143 VCLFQPGPYLEGPPGFTHSGSLAAMMDETFSKTAFLAGE---GVFTLSFNIRFKNLIPMSSLVVMDIEVGKIEDQKLYMS 219
Cdd:cd03440    2 VLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGrglGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVE 81

                         90
                 ....*....|...
gi 795469842 220 CIAHSRDQQTVYT 232
Cdd:cd03440   82 VEVRNEDGKLVAT 94
 
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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