NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|215766058|dbj|BAG98286|]
View 

unnamed protein product [Oryza sativa Japonica Group]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
43-153 1.20e-07

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: 47.55  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215766058  43 LAGARVSLAEAGRAVCSLRVTAELTDAEGNWHPGAIaaaaddvcaaaiMSV--------------EGIIKVSVHYDISYF 108
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAI------------ATLadtagglaalsalpPGALAVTVDLNVNYL 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 215766058 109 SPAKLhEEVELDGRVVEQKGKMTAVTVEIRKKDsGELVAIGRQWM 153
Cdd:cd03443   69 RPARG-GDLTARARVVKLGRRLAVVEVEVTDED-GKLVATARGTF 111
 
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 ...
43-153 1.20e-07

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: 47.55  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215766058  43 LAGARVSLAEAGRAVCSLRVTAELTDAEGNWHPGAIaaaaddvcaaaiMSV--------------EGIIKVSVHYDISYF 108
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAI------------ATLadtagglaalsalpPGALAVTVDLNVNYL 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 215766058 109 SPAKLhEEVELDGRVVEQKGKMTAVTVEIRKKDsGELVAIGRQWM 153
Cdd:cd03443   69 RPARG-GDLTARARVVKLGRRLAVVEVEVTDED-GKLVATARGTF 111
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
35-150 6.75e-06

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 43.39  E-value: 6.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215766058  35 RRAFNALPLA---GARVSLAEAGRAVCSLRVTAELTDAEGNWHPGAIAAAADDVCAAAIMSV--EGIIKVSVHYDISYFS 109
Cdd:COG2050    9 EGFLAANPFAellGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlpPGRRAVTIELNINFLR 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 215766058 110 PAKLHEEVELDGRVVEQKGKMTAVTVEIRKKDsGELVAIGR 150
Cdd:COG2050   89 PARLGDRLTAEARVVRRGRRLAVVEVEVTDED-GKLVATAT 128
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
99-146 5.03e-05

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: 39.93  E-value: 5.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 215766058   99 VSVHYDISYFSPAKLHEEVELDGRVVEQKGKMTAVTVEIRKKDSGELV 146
Cdd:pfam03061  32 VVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
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 ...
43-153 1.20e-07

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: 47.55  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215766058  43 LAGARVSLAEAGRAVCSLRVTAELTDAEGNWHPGAIaaaaddvcaaaiMSV--------------EGIIKVSVHYDISYF 108
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAI------------ATLadtagglaalsalpPGALAVTVDLNVNYL 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 215766058 109 SPAKLhEEVELDGRVVEQKGKMTAVTVEIRKKDsGELVAIGRQWM 153
Cdd:cd03443   69 RPARG-GDLTARARVVKLGRRLAVVEVEVTDED-GKLVATARGTF 111
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
35-150 6.75e-06

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 43.39  E-value: 6.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215766058  35 RRAFNALPLA---GARVSLAEAGRAVCSLRVTAELTDAEGNWHPGAIAAAADDVCAAAIMSV--EGIIKVSVHYDISYFS 109
Cdd:COG2050    9 EGFLAANPFAellGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlpPGRRAVTIELNINFLR 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 215766058 110 PAKLHEEVELDGRVVEQKGKMTAVTVEIRKKDsGELVAIGR 150
Cdd:COG2050   89 PARLGDRLTAEARVVRRGRRLAVVEVEVTDED-GKLVATAT 128
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
99-146 5.03e-05

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: 39.93  E-value: 5.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 215766058   99 VSVHYDISYFSPAKLHEEVELDGRVVEQKGKMTAVTVEIRKKDSGELV 146
Cdd:pfam03061  32 VVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
91-151 5.23e-05

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 41.04  E-value: 5.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215766058  91 MSVEGIIKVSVHYDISYFSPAKLHEEVELDGRVVEQKGKMTAVTVEIRKKDSGELVAIGRQ 151
Cdd:COG0824   50 LEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRADDGELLATGET 110
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
56-153 9.27e-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: 39.77  E-value: 9.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215766058  56 AVCSLRVTAELTDAEGNWHPGA--IAAAADDVCAAAIMSVEGIIKVSVHYDISYFSPAKLHEEVELDGRVVEQKGKMTAV 133
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLllALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80
                         90       100
                 ....*....|....*....|
gi 215766058 134 TVEIRKKDsGELVAIGRQWM 153
Cdd:cd03440   81 EVEVRNED-GKLVATATATF 99
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
91-151 1.80e-03

4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII).


Pssm-ID: 238329 [Multi-domain]  Cd Length: 110  Bit Score: 36.04  E-value: 1.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215766058  91 MSVEGIIKVSVHYDISYFSPAKLHEEVELDGRVVEQKGKMTAVTVEIRKKDsGELVAIGRQ 151
Cdd:cd00586   45 LEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGRKSFTFEQEIFRED-GELLATAET 104
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH