hypothetical protein J604_0892 [Acinetobacter sp. 694762]
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
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 ... |
25-156 | 9.97e-32 | |||
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 pfam14539: Pssm-ID: 469797 Cd Length: 131 Bit Score: 110.42 E-value: 9.97e-32
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Name | Accession | Description | Interval | E-value | |||
DUF4442 | pfam14539 | Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ... |
25-156 | 9.97e-32 | |||
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important. Pssm-ID: 434027 Cd Length: 131 Bit Score: 110.42 E-value: 9.97e-32
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PaaI | COG2050 | Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ... |
28-163 | 7.55e-19 | |||
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 441653 [Multi-domain] Cd Length: 138 Bit Score: 77.68 E-value: 7.55e-19
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PaaI_thioesterase | cd03443 | PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ... |
42-136 | 2.80e-15 | |||
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: 67.58 E-value: 2.80e-15
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Name | Accession | Description | Interval | E-value | |||
DUF4442 | pfam14539 | Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ... |
25-156 | 9.97e-32 | |||
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important. Pssm-ID: 434027 Cd Length: 131 Bit Score: 110.42 E-value: 9.97e-32
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PaaI | COG2050 | Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ... |
28-163 | 7.55e-19 | |||
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 441653 [Multi-domain] Cd Length: 138 Bit Score: 77.68 E-value: 7.55e-19
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PaaI_thioesterase | cd03443 | PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ... |
42-136 | 2.80e-15 | |||
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: 67.58 E-value: 2.80e-15
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hot_dog | cd03440 | The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
52-136 | 7.25e-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. Pssm-ID: 239524 [Multi-domain] Cd Length: 100 Bit Score: 34.37 E-value: 7.25e-03
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Blast search parameters | ||||
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