BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
203-412
1.84e-116
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).
:
Pssm-ID: 430252 [Multi-domain] Cd Length: 211 Bit Score: 338.49 E-value: 1.84e-116
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
16-141
1.81e-58
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.
:
Pssm-ID: 461422 Cd Length: 127 Bit Score: 187.06 E-value: 1.81e-58
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
145-259
5.16e-03
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.
The actual alignment was detected with superfamily member pfam01738:
Pssm-ID: 473884 [Multi-domain] Cd Length: 213 Bit Score: 38.10 E-value: 5.16e-03
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
203-412
1.84e-116
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).
Pssm-ID: 430252 [Multi-domain] Cd Length: 211 Bit Score: 338.49 E-value: 1.84e-116
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
16-141
1.81e-58
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.
Pssm-ID: 461422 Cd Length: 127 Bit Score: 187.06 E-value: 1.81e-58
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
203-412
1.84e-116
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).
Pssm-ID: 430252 [Multi-domain] Cd Length: 211 Bit Score: 338.49 E-value: 1.84e-116
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
16-141
1.81e-58
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.
Pssm-ID: 461422 Cd Length: 127 Bit Score: 187.06 E-value: 1.81e-58
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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