acetyl-coenzyme A thioesterase isoform X4 [Homo sapiens]
BFIT_BACH and SRPBCC domain-containing protein( domain architecture ID 10130858)
BFIT_BACH and SRPBCC domain-containing protein
List of domain hits
Name | Accession | Description | Interval | E-value | |||
SRPBCC super family | cl14643 | START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ... |
311-377 | 5.76e-39 | |||
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins. The actual alignment was detected with superfamily member cd08914: Pssm-ID: 472699 Cd Length: 236 Bit Score: 139.26 E-value: 5.76e-39
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YciA | COG1607 | Acyl-CoA hydrolase [Lipid transport and metabolism]; |
3-148 | 3.07e-36 | |||
Acyl-CoA hydrolase [Lipid transport and metabolism]; : Pssm-ID: 441215 [Multi-domain] Cd Length: 146 Bit Score: 128.76 E-value: 3.07e-36
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YciA | COG1607 | Acyl-CoA hydrolase [Lipid transport and metabolism]; |
187-325 | 1.90e-30 | |||
Acyl-CoA hydrolase [Lipid transport and metabolism]; : Pssm-ID: 441215 [Multi-domain] Cd Length: 146 Bit Score: 113.74 E-value: 1.90e-30
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Name | Accession | Description | Interval | E-value | |||||
START_STARD15-like | cd08914 | Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ... |
311-377 | 5.76e-39 | |||||
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114) and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD15/ACOT12 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. Human STARD15/ACOT12 may have roles in cholesterol metabolism and in beta-oxidation. Pssm-ID: 176922 Cd Length: 236 Bit Score: 139.26 E-value: 5.76e-39
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YciA | COG1607 | Acyl-CoA hydrolase [Lipid transport and metabolism]; |
3-148 | 3.07e-36 | |||||
Acyl-CoA hydrolase [Lipid transport and metabolism]; Pssm-ID: 441215 [Multi-domain] Cd Length: 146 Bit Score: 128.76 E-value: 3.07e-36
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BFIT_BACH | cd03442 | Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ... |
3-115 | 9.23e-36 | |||||
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy. Pssm-ID: 239526 [Multi-domain] Cd Length: 123 Bit Score: 126.91 E-value: 9.23e-36
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YciA | COG1607 | Acyl-CoA hydrolase [Lipid transport and metabolism]; |
187-325 | 1.90e-30 | |||||
Acyl-CoA hydrolase [Lipid transport and metabolism]; Pssm-ID: 441215 [Multi-domain] Cd Length: 146 Bit Score: 113.74 E-value: 1.90e-30
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BFIT_BACH | cd03442 | Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ... |
181-305 | 2.24e-29 | |||||
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy. Pssm-ID: 239526 [Multi-domain] Cd Length: 123 Bit Score: 109.97 E-value: 2.24e-29
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PLN02647 | PLN02647 | acyl-CoA thioesterase |
25-251 | 1.95e-11 | |||||
acyl-CoA thioesterase Pssm-ID: 215349 [Multi-domain] Cd Length: 437 Bit Score: 65.20 E-value: 1.95e-11
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4HBT | pfam03061 | Thioesterase superfamily; This family contains a wide variety of enzymes, principally ... |
197-274 | 4.71e-10 | |||||
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: 55.34 E-value: 4.71e-10
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4HBT | pfam03061 | Thioesterase superfamily; This family contains a wide variety of enzymes, principally ... |
24-100 | 1.80e-08 | |||||
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: 51.10 E-value: 1.80e-08
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Name | Accession | Description | Interval | E-value | |||||
START_STARD15-like | cd08914 | Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ... |
311-377 | 5.76e-39 | |||||
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114) and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD15/ACOT12 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. Human STARD15/ACOT12 may have roles in cholesterol metabolism and in beta-oxidation. Pssm-ID: 176922 Cd Length: 236 Bit Score: 139.26 E-value: 5.76e-39
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YciA | COG1607 | Acyl-CoA hydrolase [Lipid transport and metabolism]; |
3-148 | 3.07e-36 | |||||
Acyl-CoA hydrolase [Lipid transport and metabolism]; Pssm-ID: 441215 [Multi-domain] Cd Length: 146 Bit Score: 128.76 E-value: 3.07e-36
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START_STARD14_15-like | cd08873 | Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ... |
312-377 | 9.13e-36 | |||||
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974), STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD14/ACOT11 and STARD15/ACOT12 are type II acetyl-CoA thioesterases; they catalyze the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, STARD14 and STARD15 each have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice. Human STARD15 may have roles in cholesterol metabolism and in beta-oxidation. Pssm-ID: 176882 Cd Length: 235 Bit Score: 130.41 E-value: 9.13e-36
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BFIT_BACH | cd03442 | Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ... |
3-115 | 9.23e-36 | |||||
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy. Pssm-ID: 239526 [Multi-domain] Cd Length: 123 Bit Score: 126.91 E-value: 9.23e-36
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YciA | COG1607 | Acyl-CoA hydrolase [Lipid transport and metabolism]; |
187-325 | 1.90e-30 | |||||
Acyl-CoA hydrolase [Lipid transport and metabolism]; Pssm-ID: 441215 [Multi-domain] Cd Length: 146 Bit Score: 113.74 E-value: 1.90e-30
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BFIT_BACH | cd03442 | Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ... |
181-305 | 2.24e-29 | |||||
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy. Pssm-ID: 239526 [Multi-domain] Cd Length: 123 Bit Score: 109.97 E-value: 2.24e-29
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START_STARD14-like | cd08913 | Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ... |
309-377 | 9.51e-20 | |||||
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD14/ACOT11 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice. Pssm-ID: 176921 Cd Length: 240 Bit Score: 87.23 E-value: 9.51e-20
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PLN02647 | PLN02647 | acyl-CoA thioesterase |
25-251 | 1.95e-11 | |||||
acyl-CoA thioesterase Pssm-ID: 215349 [Multi-domain] Cd Length: 437 Bit Score: 65.20 E-value: 1.95e-11
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4HBT | pfam03061 | Thioesterase superfamily; This family contains a wide variety of enzymes, principally ... |
197-274 | 4.71e-10 | |||||
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: 55.34 E-value: 4.71e-10
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4HBT | pfam03061 | Thioesterase superfamily; This family contains a wide variety of enzymes, principally ... |
24-100 | 1.80e-08 | |||||
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: 51.10 E-value: 1.80e-08
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hot_dog | cd03440 | The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
9-112 | 3.99e-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: 50.55 E-value: 3.99e-08
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hot_dog | cd03440 | The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
189-281 | 9.69e-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: 49.78 E-value: 9.69e-08
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PRK10694 | PRK10694 | acyl-CoA thioester hydrolase YciA; |
2-94 | 4.40e-06 | |||||
acyl-CoA thioester hydrolase YciA; Pssm-ID: 236736 [Multi-domain] Cd Length: 133 Bit Score: 45.62 E-value: 4.40e-06
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PaaI | COG2050 | Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ... |
5-115 | 2.90e-05 | |||||
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: 2.90e-05
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PaaI | COG2050 | Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ... |
185-269 | 2.66e-04 | |||||
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 441653 [Multi-domain] Cd Length: 138 Bit Score: 40.70 E-value: 2.66e-04
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PaaI_thioesterase | cd03443 | PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ... |
1-112 | 2.35e-03 | |||||
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: 37.54 E-value: 2.35e-03
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PaaI_thioesterase | cd03443 | PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ... |
186-269 | 8.69e-03 | |||||
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: 35.61 E-value: 8.69e-03
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Blast search parameters | ||||
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