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Conserved domains on  [gi|1570010350|gb|RYP11507|]
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hypothetical protein DL764_000030 [Monosporascus ibericus]

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 ...
 59-174 2.08e-03

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 cd00586:

Pssm-ID: 469797 [Multi-domain]  Cd Length: 110  Bit Score: 36.82  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570010350  59 VEHGILWaEHQDPYGHVMHTQFMHFLGACFYRVMESYDEYlskeeyDGMIQARTVIPAVRKYELNIRRQVTYPDTVIAAF 138
Cdd:cd00586     3 LEIRVRF-GDTDAAGHVNNARYLRYFEEAREEFLRELGLG------YDELEEQGLGLVVVELEIDYLRPLRLGDRLTVET 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1570010350 139 RqdyIEPTRNNGTTVLFSLKQQD--IVAEVKGSTTYMD 174
Cdd:cd00586    76 R---VLRLGRKSFTFEQEIFREDgeLLATAETVLVCVD 110
 
Name Accession Description Interval E-value
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 59-174 2.08e-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: 36.82  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570010350  59 VEHGILWaEHQDPYGHVMHTQFMHFLGACFYRVMESYDEYlskeeyDGMIQARTVIPAVRKYELNIRRQVTYPDTVIAAF 138
Cdd:cd00586     3 LEIRVRF-GDTDAAGHVNNARYLRYFEEAREEFLRELGLG------YDELEEQGLGLVVVELEIDYLRPLRLGDRLTVET 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1570010350 139 RqdyIEPTRNNGTTVLFSLKQQD--IVAEVKGSTTYMD 174
Cdd:cd00586    76 R---VLRLGRKSFTFEQEIFREDgeLLATAETVLVCVD 110
 
Name Accession Description Interval E-value
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 59-174 2.08e-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: 36.82  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570010350  59 VEHGILWaEHQDPYGHVMHTQFMHFLGACFYRVMESYDEYlskeeyDGMIQARTVIPAVRKYELNIRRQVTYPDTVIAAF 138
Cdd:cd00586     3 LEIRVRF-GDTDAAGHVNNARYLRYFEEAREEFLRELGLG------YDELEEQGLGLVVVELEIDYLRPLRLGDRLTVET 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1570010350 139 RqdyIEPTRNNGTTVLFSLKQQD--IVAEVKGSTTYMD 174
Cdd:cd00586    76 R---VLRLGRKSFTFEQEIFREDgeLLATAETVLVCVD 110
 
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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