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Conserved domains on  [gi|1098752262|ref|XP_018840237|]
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1,4-dihydroxy-2-naphthoyl-CoA thioesterase 1 [Juglans regia]

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 ...
 7-160 3.38e-78

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: 229.18  E-value: 3.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098752262   7 AESSKTGFLDAPLNAIGFQIGDLTPQKVTGRLQVTETCCQPFKVLHGGVSALIAEGVASIGAHMASGFQRVAGIHLSINH 86
Cdd:PLN02322    1 SASSNTKAIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSINH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098752262  87 LKRADLGDLVLVEAAPVNAGKTIQVWEVQFWKVDPSNSQNKSLVASSRVTLLCNMPVPENAKNASDALRKYARL 160
Cdd:PLN02322   81 LKSADLGDLVFAEATPVSTGKTIQVWEVKLWKTTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLRMQAKL 154
 
Name Accession Description Interval E-value
PLN02322 PLN02322
acyl-CoA thioesterase
 7-160 3.38e-78

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 229.18  E-value: 3.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098752262   7 AESSKTGFLDAPLNAIGFQIGDLTPQKVTGRLQVTETCCQPFKVLHGGVSALIAEGVASIGAHMASGFQRVAGIHLSINH 86
Cdd:PLN02322    1 SASSNTKAIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSINH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098752262  87 LKRADLGDLVLVEAAPVNAGKTIQVWEVQFWKVDPSNSQNKSLVASSRVTLLCNMPVPENAKNASDALRKYARL 160
Cdd:PLN02322   81 LKSADLGDLVFAEATPVSTGKTIQVWEVKLWKTTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLRMQAKL 154
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 13-139 2.22e-22

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 86.54  E-value: 2.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098752262  13 GFLDAP--LNAIGFQIGDLTPQKVTGRLQVTETCCQPFKVLHGGVSALIAEGVASIGAHMASGF-QRVAGIHLSINHLKR 89
Cdd:COG2050    10 GFLAANpfAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPgRRAVTIELNINFLRP 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1098752262  90 ADLGDLVLVEAAPVNAGKTIQVWEVQFWkvdpsNSQNKsLVASSRVTLLC 139
Cdd:COG2050    90 ARLGDRLTAEARVVRRGRRLAVVEVEVT-----DEDGK-LVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 21-136 1.14e-21

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: 84.15  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098752262  21 AIGFQIGDLTPQKVTGRLQVTETCCQPFKVLHGGVSALIAEGVASIGAHMASG-FQRVAGIHLSINHLKRADLGDLVlVE 99
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPpGALAVTVDLNVNYLRPARGGDLT-AR 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1098752262 100 AAPVNAGKTIQVWEVQFWkvdpsNSQNKsLVASSRVT 136
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVT-----DEDGK-LVATARGT 110
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 48-121 8.96e-15

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: 65.35  E-value: 8.96e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1098752262  48 FKVLHGGVSALIAEGVASIGAHMASGFQR-VAGIHLSINHLKRADLGDLVLVEAAPVNAGKTIQVWEVQFWKVDP 121
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDG 75
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 19-138 6.52e-13

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: 61.59  E-value: 6.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098752262  19 LNAIGFQIGDLTPQKVTGRLQVTETCCQPFKVLHGGVSALIAE-GVASIGAHMASGFQRVAGIHLSINHLKRADLGDLVl 97
Cdd:TIGR00369   3 VSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADtAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKVR- 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1098752262  98 VEAAPVNAGKTIQVWEVQFWkvdpsNSQNKsLVASSRVTLL 138
Cdd:TIGR00369  82 AIAQVVHLGRQTGVAEIEIV-----DEQGR-LCALSRGTTA 116
 
Name Accession Description Interval E-value
PLN02322 PLN02322
acyl-CoA thioesterase
 7-160 3.38e-78

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 229.18  E-value: 3.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098752262   7 AESSKTGFLDAPLNAIGFQIGDLTPQKVTGRLQVTETCCQPFKVLHGGVSALIAEGVASIGAHMASGFQRVAGIHLSINH 86
Cdd:PLN02322    1 SASSNTKAIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSINH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098752262  87 LKRADLGDLVLVEAAPVNAGKTIQVWEVQFWKVDPSNSQNKSLVASSRVTLLCNMPVPENAKNASDALRKYARL 160
Cdd:PLN02322   81 LKSADLGDLVFAEATPVSTGKTIQVWEVKLWKTTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLRMQAKL 154
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 13-139 2.22e-22

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 86.54  E-value: 2.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098752262  13 GFLDAP--LNAIGFQIGDLTPQKVTGRLQVTETCCQPFKVLHGGVSALIAEGVASIGAHMASGF-QRVAGIHLSINHLKR 89
Cdd:COG2050    10 GFLAANpfAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPgRRAVTIELNINFLRP 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1098752262  90 ADLGDLVLVEAAPVNAGKTIQVWEVQFWkvdpsNSQNKsLVASSRVTLLC 139
Cdd:COG2050    90 ARLGDRLTAEARVVRRGRRLAVVEVEVT-----DEDGK-LVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 21-136 1.14e-21

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: 84.15  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098752262  21 AIGFQIGDLTPQKVTGRLQVTETCCQPFKVLHGGVSALIAEGVASIGAHMASG-FQRVAGIHLSINHLKRADLGDLVlVE 99
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPpGALAVTVDLNVNYLRPARGGDLT-AR 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1098752262 100 AAPVNAGKTIQVWEVQFWkvdpsNSQNKsLVASSRVT 136
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVT-----DEDGK-LVATARGT 110
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 48-121 8.96e-15

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: 65.35  E-value: 8.96e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1098752262  48 FKVLHGGVSALIAEGVASIGAHMASGFQR-VAGIHLSINHLKRADLGDLVLVEAAPVNAGKTIQVWEVQFWKVDP 121
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDG 75
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 19-138 6.52e-13

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: 61.59  E-value: 6.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098752262  19 LNAIGFQIGDLTPQKVTGRLQVTETCCQPFKVLHGGVSALIAE-GVASIGAHMASGFQRVAGIHLSINHLKRADLGDLVl 97
Cdd:TIGR00369   3 VSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADtAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKVR- 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1098752262  98 VEAAPVNAGKTIQVWEVQFWkvdpsNSQNKsLVASSRVTLL 138
Cdd:TIGR00369  82 AIAQVVHLGRQTGVAEIEIV-----DEQGR-LCALSRGTTA 116
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 34-138 2.42e-10

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: 54.40  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098752262  34 VTGRLQVTETCCQPFKVLHGGVSALIAEGVASIGAHMASGFQR-VAGIHLSINHLKRADLGDLVLVEAAPVNAGKTIQVW 112
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLgAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                          90       100
                  ....*....|....*....|....*.
gi 1098752262 113 EVQFWkvdpsnSQNKSLVASSRVTLL 138
Cdd:cd03440    81 EVEVR------NEDGKLVATATATFV 100
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
7-136 9.23e-10

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 53.86  E-value: 9.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098752262   7 AESSKTGFLDAPLNaigfQIGDLTpqkVTGRLQVTETCCQPFKVLHGGVSALIAEGVASIGAHMAS-GFQRVAGIHLSIN 85
Cdd:PRK10293   16 GEGNMVGLLDIRFE----HIGDDT---LEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTeGEQKVVGLEINAN 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1098752262  86 HLKRADLGDLVLVeAAPVNAGKTIQVWEVQFWkvdpsnSQNKSLVASSRVT 136
Cdd:PRK10293   89 HVRSAREGRVRGV-CKPLHLGSRHQVWQIEIF------DEKGRLCCSSRLT 132
PRK10254 PRK10254
proofreading thioesterase EntH;
46-114 1.85e-06

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 44.98  E-value: 1.85e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098752262  46 QPFKVLHGGVSALIAEGVASI-GAHMASGFQRVAGIHLSINHLKRADLGDlVLVEAAPVNAGKTIQVWEV 114
Cdd:PRK10254   48 QPFGLLHGGASAALAETLGSMaGFLMTRDGQCVVGTELNATHHRPVSEGK-VRGVCQPLHLGRQNQSWEI 116
 
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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