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Conserved domains on  [gi|685308701|ref|XP_009145011|]
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1,4-dihydroxy-2-naphthoyl-CoA thioesterase 1-like isoform X1 [Brassica rapa]

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 ...
 3-155 9.90e-83

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 PLN02322:

Pssm-ID: 469797  Cd Length: 154  Bit Score: 240.35  E-value: 9.90e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685308701   3 SASSKTKALALPLHILGFEIDELSTTRVTGRLPVSQICCQPFKVLHGGVSALIAESLASIGAYMATDLKRVAGIQLSINH 82
Cdd:PLN02322   1 SASSNTKAIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSINH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685308701  83 LKSADLGDIVFAQASPVSSGKTIQVWEVKLWK-SRKESHNKTLISSSRVTLLCNLPTPGHAKNVSDPLKMISKL 155
Cdd:PLN02322  81 LKSADLGDLVFAEATPVSTGKTIQVWEVKLWKtTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLRMQAKL 154
 
Name Accession Description Interval E-value
PLN02322 PLN02322
acyl-CoA thioesterase
 3-155 9.90e-83

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 240.35  E-value: 9.90e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685308701   3 SASSKTKALALPLHILGFEIDELSTTRVTGRLPVSQICCQPFKVLHGGVSALIAESLASIGAYMATDLKRVAGIQLSINH 82
Cdd:PLN02322   1 SASSNTKAIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSINH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685308701  83 LKSADLGDIVFAQASPVSSGKTIQVWEVKLWK-SRKESHNKTLISSSRVTLLCNLPTPGHAKNVSDPLKMISKL 155
Cdd:PLN02322  81 LKSADLGDLVFAEATPVSTGKTIQVWEVKLWKtTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLRMQAKL 154
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 18-134 4.44e-25

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 93.47  E-value: 4.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685308701  18 LGFEIDELSTTRVTGRLPVSQICCQPFKVLHGGVSALIAESLASIGAYMATDLKRVA-GIQLSINHLKSADLGDIVFAQA 96
Cdd:COG2050   21 LGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAvTIELNINFLRPARLGDRLTAEA 100

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 685308701  97 SPVSSGKTIQVWEVKLWksrkeSHNKTLISSSRVTLLC 134
Cdd:COG2050  101 RVVRRGRRLAVVEVEVT-----DEDGKLVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 18-131 5.17e-25

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: 92.24  E-value: 5.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685308701  18 LGFEIDELSTTRVTGRLPVSQICCQPFKVLHGGVSALIAESLASIGAYMATDL-KRVAGIQLSINHLKSADLGDIVfAQA 96
Cdd:cd03443    2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPgALAVTVDLNVNYLRPARGGDLT-ARA 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 685308701  97 SPVSSGKTIQVWEVKLWKSrkeshNKTLISSSRVT 131
Cdd:cd03443   81 RVVKLGRRLAVVEVEVTDE-----DGKLVATARGT 110
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 18-133 1.93e-15

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: 67.76  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685308701   18 LGFEIDELSTTRVTGRLPVSQICCQPFKVLHGGVSALIAESLASIGAYMAT-DLKRVAGIQLSINHLKSADLGDIVfAQA 96
Cdd:TIGR00369   6 LGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNsGGQAVVGLELNANHLRPAREGKVR-AIA 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 685308701   97 SPVSSGKTIQVWEVKLwksrKESHNKtLISSSRVTLL 133
Cdd:TIGR00369  85 QVVHLGRQTGVAEIEI----VDEQGR-LCALSRGTTA 116
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 44-114 1.99e-13

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: 61.50  E-value: 1.99e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685308701   44 FKVLHGGVSALIAESLASIGAY-MATDLKRVAGIQLSINHLKSADLGDIVFAQASPVSSGKTIQVWEVKLWK 114
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARrLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72
 
Name Accession Description Interval E-value
PLN02322 PLN02322
acyl-CoA thioesterase
 3-155 9.90e-83

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 240.35  E-value: 9.90e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685308701   3 SASSKTKALALPLHILGFEIDELSTTRVTGRLPVSQICCQPFKVLHGGVSALIAESLASIGAYMATDLKRVAGIQLSINH 82
Cdd:PLN02322   1 SASSNTKAIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSINH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685308701  83 LKSADLGDIVFAQASPVSSGKTIQVWEVKLWK-SRKESHNKTLISSSRVTLLCNLPTPGHAKNVSDPLKMISKL 155
Cdd:PLN02322  81 LKSADLGDLVFAEATPVSTGKTIQVWEVKLWKtTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLRMQAKL 154
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 18-134 4.44e-25

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 93.47  E-value: 4.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685308701  18 LGFEIDELSTTRVTGRLPVSQICCQPFKVLHGGVSALIAESLASIGAYMATDLKRVA-GIQLSINHLKSADLGDIVFAQA 96
Cdd:COG2050   21 LGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAvTIELNINFLRPARLGDRLTAEA 100

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 685308701  97 SPVSSGKTIQVWEVKLWksrkeSHNKTLISSSRVTLLC 134
Cdd:COG2050  101 RVVRRGRRLAVVEVEVT-----DEDGKLVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 18-131 5.17e-25

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: 92.24  E-value: 5.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685308701  18 LGFEIDELSTTRVTGRLPVSQICCQPFKVLHGGVSALIAESLASIGAYMATDL-KRVAGIQLSINHLKSADLGDIVfAQA 96
Cdd:cd03443    2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPgALAVTVDLNVNYLRPARGGDLT-ARA 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 685308701  97 SPVSSGKTIQVWEVKLWKSrkeshNKTLISSSRVT 131
Cdd:cd03443   81 RVVKLGRRLAVVEVEVTDE-----DGKLVATARGT 110
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 18-133 1.93e-15

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: 67.76  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685308701   18 LGFEIDELSTTRVTGRLPVSQICCQPFKVLHGGVSALIAESLASIGAYMAT-DLKRVAGIQLSINHLKSADLGDIVfAQA 96
Cdd:TIGR00369   6 LGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNsGGQAVVGLELNANHLRPAREGKVR-AIA 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 685308701   97 SPVSSGKTIQVWEVKLwksrKESHNKtLISSSRVTLL 133
Cdd:TIGR00369  85 QVVHLGRQTGVAEIEI----VDEQGR-LCALSRGTTA 116
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 44-114 1.99e-13

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: 61.50  E-value: 1.99e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685308701   44 FKVLHGGVSALIAESLASIGAY-MATDLKRVAGIQLSINHLKSADLGDIVFAQASPVSSGKTIQVWEVKLWK 114
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARrLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
17-131 9.07e-12

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 58.87  E-value: 9.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685308701  17 ILGFEIDELSTTRVTGRLPVSQICCQPFKVLHGGVSALIAESLASIGAYMATD-LKRVAGIQLSINHLKSADLGDiVFAQ 95
Cdd:PRK10293  23 LLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEgEQKVVGLEINANHVRSAREGR-VRGV 101

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 685308701  96 ASPVSSGKTIQVWEVKLWKSRKEshnktLISSSRVT 131
Cdd:PRK10293 102 CKPLHLGSRHQVWQIEIFDEKGR-----LCCSSRLT 132
PRK10254 PRK10254
proofreading thioesterase EntH;
18-110 3.91e-10

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 54.61  E-value: 3.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685308701  18 LGFEIDELSTTRVTGRLPVSQICCQPFKVLHGGVSALIAESLASIGAYMAT-DLKRVAGIQLSINHLKSADLGDiVFAQA 96
Cdd:PRK10254  24 LGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTrDGQCVVGTELNATHHRPVSEGK-VRGVC 102

                         90
                 ....*....|....
gi 685308701  97 SPVSSGKTIQVWEV 110
Cdd:PRK10254 103 QPLHLGRQNQSWEI 116
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 30-133 4.79e-08

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: 48.24  E-value: 4.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685308701  30 VTGRLPVSQICCQPFKVLHGGVSALIAESLASIGAYMATDLKR-VAGIQLSINHLKSADLGDIVFAQASPVSSGKTIQVW 108
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLgAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                         90       100
                 ....*....|....*....|....*
gi 685308701 109 EVKLWKSRKEshnktLISSSRVTLL 133
Cdd:cd03440   81 EVEVRNEDGK-----LVATATATFV 100
PRK11688 PRK11688
thioesterase family protein;
16-134 3.20e-03

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 35.98  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685308701  16 HILGFEIDELSTTRVTGRLPVSQ--ICCQPFKVLHGGVSA--------LIAesLASIGAYMATD--------LKRVAGIQ 77
Cdd:PRK11688  25 RLLGLELERLEPDFVELSFKMQPelVGNIAQSILHGGVIAsvldvaggLVC--VGGILARHEDIseeelrqrLSRLGTID 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 685308701  78 LSINHLKSAdLGDIVFAQASPVSSGKTIQVwevklwkSRKESHNK--TLISSSRVTLLC 134
Cdd:PRK11688 103 LRVDYLRPG-RGERFTATSSVLRAGNKVAV-------ARMELHNEqgVHIASGTATYLV 153
 
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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