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Conserved domains on  [gi|212632910|ref|NP_001129757|]
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BAAT/Acyl-CoA thioester hydrolase C-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
124-332 1.53e-58

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 pfam08840:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 211  Bit Score: 188.64  E-value: 1.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910  124 VDVEYFLKPIEFVLGLSYTT-NMLGIQGVSFGATIVDLLSTRYPQIKAVVSINGPHAQCSYSLLKEHGKQMIVPELDDSK 202
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKgPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910  203 LYFLNTILVTAPCFKTLTPILTEENSIPWHWIpkETAFRLIGSVDDLCAPSIHSNLHIQKKLQETGHYVELELV---NGG 279
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERA--KGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEVEVQLVcypGAG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 212632910  280 HIMEPPYFPHHDIVYAKFQGFYCGYGGEIVLHAKSQERTWANTINFFKRKLGS 332
Cdd:pfam08840 159 HLIEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
1-61 1.20e-14

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: 69.95  E-value: 1.20e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212632910    1 MGLFLSMTPSEDFAYGGYLRCTPPIPFFYLLQLSD---DSGTKLDEMYIKKHWMHPLLTRTEIE 61
Cdd:pfam04775  63 MGLFWSMKPEPGFRPRLYKRDVLPTPFVVTLSVYDgseESGKPLASVTVERWYMAPGVRRIEVR 126
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
55-176 2.41e-12

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 65.76  E-value: 2.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910  55 LTRTEIEY---DG--FCGTLFKPPGDGPFPCVMDISGtGGGLHEH---KGAMLASEGFVVICVAFFQFKDlPYKLEDVDV 126
Cdd:COG0412    1 MTTETVTIptpDGvtLPGYLARPAGGGPRPGVVVLHE-IFGLNPHirdVARRLAAAGYVVLAPDLYGRGG-PGDDPDEAR 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212632910 127 EYFLKP------------IEFVLGLSYT-TNMLGIQGVSFGATIVDLLSTRYPQIKAVVSING 176
Cdd:COG0412   79 ALMGALdpellaadlraaLDWLKAQPEVdAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYG 141
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
124-332 1.53e-58

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: 188.64  E-value: 1.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910  124 VDVEYFLKPIEFVLGLSYTT-NMLGIQGVSFGATIVDLLSTRYPQIKAVVSINGPHAQCSYSLLKEHGKQMIVPELDDSK 202
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKgPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910  203 LYFLNTILVTAPCFKTLTPILTEENSIPWHWIpkETAFRLIGSVDDLCAPSIHSNLHIQKKLQETGHYVELELV---NGG 279
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERA--KGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEVEVQLVcypGAG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 212632910  280 HIMEPPYFPHHDIVYAKFQGFYCGYGGEIVLHAKSQERTWANTINFFKRKLGS 332
Cdd:pfam08840 159 HLIEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
1-61 1.20e-14

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: 69.95  E-value: 1.20e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212632910    1 MGLFLSMTPSEDFAYGGYLRCTPPIPFFYLLQLSD---DSGTKLDEMYIKKHWMHPLLTRTEIE 61
Cdd:pfam04775  63 MGLFWSMKPEPGFRPRLYKRDVLPTPFVVTLSVYDgseESGKPLASVTVERWYMAPGVRRIEVR 126
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
55-176 2.41e-12

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 65.76  E-value: 2.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910  55 LTRTEIEY---DG--FCGTLFKPPGDGPFPCVMDISGtGGGLHEH---KGAMLASEGFVVICVAFFQFKDlPYKLEDVDV 126
Cdd:COG0412    1 MTTETVTIptpDGvtLPGYLARPAGGGPRPGVVVLHE-IFGLNPHirdVARRLAAAGYVVLAPDLYGRGG-PGDDPDEAR 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212632910 127 EYFLKP------------IEFVLGLSYT-TNMLGIQGVSFGATIVDLLSTRYPQIKAVVSING 176
Cdd:COG0412   79 ALMGALdpellaadlraaLDWLKAQPEVdAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYG 141
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
67-301 4.03e-09

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 56.18  E-value: 4.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910  67 GTLFKPPGDGPFPCVMDISGTGGGLHE---HKGAMLASEGFVVICVAFFQFKDLPYKLEDVDVEYFLKPIEFVLGLSYT- 142
Cdd:COG1506   12 GWLYLPADGKKYPVVVYVHGGPGSRDDsflPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARPYVd 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910 143 TNMLGIQGVSFGATIVDLLSTRYPQ-IKAVVSINGPHAQCSY-SLLKEHGKQMIVPELDDSKLYFLNTILVTAPCFKtlT 220
Cdd:COG1506   92 PDRIGIYGHSYGGYMALLAAARHPDrFKAAVALAGVSDLRSYyGTTREYTERLMGGPWEDPEAYAARSPLAYADKLK--T 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910 221 PILteensipwhwipketafrLIGSVDDLCAPSIHSnLHIQKKLQETGHYVELELV-NGGHIMEPPYFPHhdiVYAKFQG 299
Cdd:COG1506  170 PLL------------------LIHGEADDRVPPEQA-ERLYEALKKAGKPVELLVYpGEGHGFSGAGAPD---YLERILD 227

                 ..
gi 212632910 300 FY 301
Cdd:COG1506  228 FL 229
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
124-332 1.53e-58

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: 188.64  E-value: 1.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910  124 VDVEYFLKPIEFVLGLSYTT-NMLGIQGVSFGATIVDLLSTRYPQIKAVVSINGPHAQCSYSLLKEHGKQMIVPELDDSK 202
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKgPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910  203 LYFLNTILVTAPCFKTLTPILTEENSIPWHWIpkETAFRLIGSVDDLCAPSIHSNLHIQKKLQETGHYVELELV---NGG 279
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERA--KGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEVEVQLVcypGAG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 212632910  280 HIMEPPYFPHHDIVYAKFQGFYCGYGGEIVLHAKSQERTWANTINFFKRKLGS 332
Cdd:pfam08840 159 HLIEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
1-61 1.20e-14

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: 69.95  E-value: 1.20e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212632910    1 MGLFLSMTPSEDFAYGGYLRCTPPIPFFYLLQLSD---DSGTKLDEMYIKKHWMHPLLTRTEIE 61
Cdd:pfam04775  63 MGLFWSMKPEPGFRPRLYKRDVLPTPFVVTLSVYDgseESGKPLASVTVERWYMAPGVRRIEVR 126
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
55-176 2.41e-12

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 65.76  E-value: 2.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910  55 LTRTEIEY---DG--FCGTLFKPPGDGPFPCVMDISGtGGGLHEH---KGAMLASEGFVVICVAFFQFKDlPYKLEDVDV 126
Cdd:COG0412    1 MTTETVTIptpDGvtLPGYLARPAGGGPRPGVVVLHE-IFGLNPHirdVARRLAAAGYVVLAPDLYGRGG-PGDDPDEAR 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212632910 127 EYFLKP------------IEFVLGLSYT-TNMLGIQGVSFGATIVDLLSTRYPQIKAVVSING 176
Cdd:COG0412   79 ALMGALdpellaadlraaLDWLKAQPEVdAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYG 141
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
67-301 4.03e-09

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 56.18  E-value: 4.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910  67 GTLFKPPGDGPFPCVMDISGTGGGLHE---HKGAMLASEGFVVICVAFFQFKDLPYKLEDVDVEYFLKPIEFVLGLSYT- 142
Cdd:COG1506   12 GWLYLPADGKKYPVVVYVHGGPGSRDDsflPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARPYVd 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910 143 TNMLGIQGVSFGATIVDLLSTRYPQ-IKAVVSINGPHAQCSY-SLLKEHGKQMIVPELDDSKLYFLNTILVTAPCFKtlT 220
Cdd:COG1506   92 PDRIGIYGHSYGGYMALLAAARHPDrFKAAVALAGVSDLRSYyGTTREYTERLMGGPWEDPEAYAARSPLAYADKLK--T 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212632910 221 PILteensipwhwipketafrLIGSVDDLCAPSIHSnLHIQKKLQETGHYVELELV-NGGHIMEPPYFPHhdiVYAKFQG 299
Cdd:COG1506  170 PLL------------------LIHGEADDRVPPEQA-ERLYEALKKAGKPVELLVYpGEGHGFSGAGAPD---YLERILD 227

                 ..
gi 212632910 300 FY 301
Cdd:COG1506  228 FL 229
 
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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