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Conserved domains on  [gi|1755143142|gb|QES89324|]
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hotdog fold thioesterase [Rhizosphaericola mali]

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 ...
 4-140 5.30e-50

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 PRK10254:

Pssm-ID: 469797  Cd Length: 137  Bit Score: 156.30  E-value: 5.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142   4 IWfKKHINLAELNASSKNTMTEFLEIQFTEIGDDYLKATMPVTAKTHQPMGILHGGASAALAETVGSIAGWLVVDISHKI 83
Cdd:PRK10254    2 IW-KRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQCV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1755143142  84 cVGMELNCNHIRSKKSGIVTATARPWHIGKTTQVWDIQIHDEKEKLVCISRLTLAVI 140
Cdd:PRK10254   81 -VGTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
 
Name Accession Description Interval E-value
PRK10254 PRK10254
proofreading thioesterase EntH;
4-140 5.30e-50

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 156.30  E-value: 5.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142   4 IWfKKHINLAELNASSKNTMTEFLEIQFTEIGDDYLKATMPVTAKTHQPMGILHGGASAALAETVGSIAGWLVVDISHKI 83
Cdd:PRK10254    2 IW-KRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQCV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1755143142  84 cVGMELNCNHIRSKKSGIVTATARPWHIGKTTQVWDIQIHDEKEKLVCISRLTLAVI 140
Cdd:PRK10254   81 -VGTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 22-139 1.62e-41

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: 134.01  E-value: 1.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142  22 TMTEFLEIQFTEIGDDYLKATMPVTAKTHQPMGILHGGASAALAETVGSIAGWLVvDISHKICVGMELNCNHIRSKKSGI 101
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLC-NSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1755143142 102 VTATARPWHIGKTTQVWDIQIHDEKEKLVCISRLTLAV 139
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 12-144 4.44e-39

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 128.52  E-value: 4.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142  12 LAELNAS-SKNTMTEFLEIQFTEIGDDYLKATMPVTAKTHQPMGILHGGASAALAETVGSIAGWLVVDiSHKICVGMELN 90
Cdd:COG2050     5 LERLEGFlAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALP-PGRRAVTIELN 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1755143142  91 CNHIRSKKSGI-VTATARPWHIGKTTQVWDIQIHDEKEKLVCISRLTLAVINQPK 144
Cdd:COG2050    84 INFLRPARLGDrLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 26-139 5.57e-37

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: 122.28  E-value: 5.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142  26 FLEIQFTEIGDDYLKATMPVTAKTHQPMGILHGGASAALAETVGSIAGWLVVDiSHKICVGMELNCNHIRSKKSGIVTAT 105
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALP-PGALAVTVDLNVNYLRPARGGDLTAR 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1755143142 106 ARPWHIGKTTQVWDIQIHDEKEKLVCISRLTLAV 139
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 53-131 4.39e-18

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 73.44  E-value: 4.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142  53 MGILHGGASAALAETVGSIAGWLVVdISHKICVGMELNCNHIRSKKSG-IVTATARPWHIGKTTQVWDIQIHDEKEKLVC 131
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLG-GSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PRK10254 PRK10254
proofreading thioesterase EntH;
4-140 5.30e-50

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 156.30  E-value: 5.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142   4 IWfKKHINLAELNASSKNTMTEFLEIQFTEIGDDYLKATMPVTAKTHQPMGILHGGASAALAETVGSIAGWLVVDISHKI 83
Cdd:PRK10254    2 IW-KRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQCV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1755143142  84 cVGMELNCNHIRSKKSGIVTATARPWHIGKTTQVWDIQIHDEKEKLVCISRLTLAVI 140
Cdd:PRK10254   81 -VGTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
4-140 4.93e-42

1,4-dihydroxy-2-naphthoyl-CoA hydrolase;


Pssm-ID: 182360  Cd Length: 136  Bit Score: 136.29  E-value: 4.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142   4 IWfKKHINLAELNASSKNTMTEFLEIQFTEIGDDYLKATMPVTAKTHQPMGILHGGASAALAETVGSIAGWLVVDISHKI 83
Cdd:PRK10293    2 IW-KRKITLEALNAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1755143142  84 cVGMELNCNHIRSKKSGIVTATARPWHIGKTTQVWDIQIHDEKEKLVCISRLTLAVI 140
Cdd:PRK10293   81 -VGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 22-139 1.62e-41

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: 134.01  E-value: 1.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142  22 TMTEFLEIQFTEIGDDYLKATMPVTAKTHQPMGILHGGASAALAETVGSIAGWLVvDISHKICVGMELNCNHIRSKKSGI 101
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLC-NSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1755143142 102 VTATARPWHIGKTTQVWDIQIHDEKEKLVCISRLTLAV 139
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 12-144 4.44e-39

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 128.52  E-value: 4.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142  12 LAELNAS-SKNTMTEFLEIQFTEIGDDYLKATMPVTAKTHQPMGILHGGASAALAETVGSIAGWLVVDiSHKICVGMELN 90
Cdd:COG2050     5 LERLEGFlAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALP-PGRRAVTIELN 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1755143142  91 CNHIRSKKSGI-VTATARPWHIGKTTQVWDIQIHDEKEKLVCISRLTLAVINQPK 144
Cdd:COG2050    84 INFLRPARLGDrLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 26-139 5.57e-37

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: 122.28  E-value: 5.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142  26 FLEIQFTEIGDDYLKATMPVTAKTHQPMGILHGGASAALAETVGSIAGWLVVDiSHKICVGMELNCNHIRSKKSGIVTAT 105
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALP-PGALAVTVDLNVNYLRPARGGDLTAR 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1755143142 106 ARPWHIGKTTQVWDIQIHDEKEKLVCISRLTLAV 139
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 53-131 4.39e-18

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 73.44  E-value: 4.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142  53 MGILHGGASAALAETVGSIAGWLVVdISHKICVGMELNCNHIRSKKSG-IVTATARPWHIGKTTQVWDIQIHDEKEKLVC 131
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLG-GSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PLN02322 PLN02322
acyl-CoA thioesterase
 27-143 3.52e-16

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 70.48  E-value: 3.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142  27 LEIQFTEIGDDYLKATMPVTAKTHQPMGILHGGASAALAETVGSIAGWLVVDIshKICVGMELNCNHIRSKKSG-IVTAT 105
Cdd:PLN02322   16 LGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGF--KRVAGIQLSINHLKSADLGdLVFAE 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1755143142 106 ARPWHIGKTTQVWDIQI-----HDEKEK-LVCISRLTLaVINQP 143
Cdd:PLN02322   94 ATPVSTGKTIQVWEVKLwkttdKDKANKiLISSSRVTL-ICNLP 136
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 39-138 6.30e-11

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: 55.56  E-value: 6.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755143142  39 LKATMPVTAKTHQPMGILHGGASAALAETVGSIAgWLVVDISHKICVGMELNCNHIRSKKSG-IVTATARPWHIGKTTQV 117
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAA-AARLGGRGLGAVTLSLDVRFLRPVRPGdTLTVEAEVVRVGRSSVT 79

                          90       100
                  ....*....|....*....|.
gi 1755143142 118 WDIQIHDEKEKLVCISRLTLA 138
Cdd:cd03440    80 VEVEVRNEDGKLVATATATFV 100
 
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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