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Conserved domains on  [gi|81230487|ref|NP_001032239|]
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acyl-coenzyme A thioesterase 6 isoform 2 [Homo sapiens]

Protein Classification

alpha/beta hydrolase; tannase/feruloyl esterase family alpha/beta hydrolase( domain architecture ID 10556038)

uncharacterized alpha/beta hydrolase; may catalyze the cleavage and formation of ester bonds| tannase/feruloyl esterase family alpha/beta hydrolase similar to Aspergillus oryzae tannase and Aspergillus niger feruloyl esterase B

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
1-198 4.27e-102

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: 293.42  E-value: 4.27e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230487     1 MLQHPKVKGPSIALLGFSKGGDLCLSMASFLKGITATVLINACVANTVAPLHYKDMIIPKLVDDLGKVKITKSGFLTFMD 80
Cdd:pfam08840  13 LLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRIKVNKDGLLDIRD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230487    81 TWSNPLEEHNHQSLVPLEKAQVPFLFIVGMDDQSWKSEFYAQIASERLQAHGKE-RPQIICYPETGHCIDPPYFPPSRAS 159
Cdd:pfam08840  93 MFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHLIEPPYFPHCGAS 172
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 81230487   160 VHAVLGEAIFYGGEPKAHSKAQVDAWQQIQTFFHKHLNG 198
Cdd:pfam08840 173 FHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
1-198 4.27e-102

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: 293.42  E-value: 4.27e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230487     1 MLQHPKVKGPSIALLGFSKGGDLCLSMASFLKGITATVLINACVANTVAPLHYKDMIIPKLVDDLGKVKITKSGFLTFMD 80
Cdd:pfam08840  13 LLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRIKVNKDGLLDIRD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230487    81 TWSNPLEEHNHQSLVPLEKAQVPFLFIVGMDDQSWKSEFYAQIASERLQAHGKE-RPQIICYPETGHCIDPPYFPPSRAS 159
Cdd:pfam08840  93 MFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHLIEPPYFPHCGAS 172
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 81230487   160 VHAVLGEAIFYGGEPKAHSKAQVDAWQQIQTFFHKHLNG 198
Cdd:pfam08840 173 FHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
3-192 4.81e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 42.65  E-value: 4.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230487   3 QHPKVKGPSIALLGFSKGGDLCLSMASFLKGITATVLINACVANtvaplhykdmiiPKLVDDLGKVKitksgfltfmdtw 82
Cdd:COG0412 102 AQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPA------------DDLLDLAARIK------------- 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230487  83 snpleehnhqslvplekaqVPFLFIVGMDDQSWKSEFYAQIAsERLQAHGKERpQIICYPETGHCidppYFPPSRASVHA 162
Cdd:COG0412 157 -------------------APVLLLYGEKDPLVPPEQVAALE-AALAAAGVDV-ELHVYPGAGHG----FTNPGRPRYDP 211
                       170       180       190
                ....*....|....*....|....*....|
gi 81230487 163 vlgeaifyggepkahsKAQVDAWQQIQTFF 192
Cdd:COG0412 212 ----------------AAAEDAWQRTLAFL 225
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
1-198 4.27e-102

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: 293.42  E-value: 4.27e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230487     1 MLQHPKVKGPSIALLGFSKGGDLCLSMASFLKGITATVLINACVANTVAPLHYKDMIIPKLVDDLGKVKITKSGFLTFMD 80
Cdd:pfam08840  13 LLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRIKVNKDGLLDIRD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230487    81 TWSNPLEEHNHQSLVPLEKAQVPFLFIVGMDDQSWKSEFYAQIASERLQAHGKE-RPQIICYPETGHCIDPPYFPPSRAS 159
Cdd:pfam08840  93 MFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHLIEPPYFPHCGAS 172
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 81230487   160 VHAVLGEAIFYGGEPKAHSKAQVDAWQQIQTFFHKHLNG 198
Cdd:pfam08840 173 FHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
3-192 4.81e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 42.65  E-value: 4.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230487   3 QHPKVKGPSIALLGFSKGGDLCLSMASFLKGITATVLINACVANtvaplhykdmiiPKLVDDLGKVKitksgfltfmdtw 82
Cdd:COG0412 102 AQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPA------------DDLLDLAARIK------------- 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230487  83 snpleehnhqslvplekaqVPFLFIVGMDDQSWKSEFYAQIAsERLQAHGKERpQIICYPETGHCidppYFPPSRASVHA 162
Cdd:COG0412 157 -------------------APVLLLYGEKDPLVPPEQVAALE-AALAAAGVDV-ELHVYPGAGHG----FTNPGRPRYDP 211
                       170       180       190
                ....*....|....*....|....*....|
gi 81230487 163 vlgeaifyggepkahsKAQVDAWQQIQTFF 192
Cdd:COG0412 212 ----------------AAAEDAWQRTLAFL 225
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
1-154 8.74e-03

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 36.15  E-value: 8.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230487   1 MLQHPKVKGPSIALLGFSKGGDLCLSMASFLKGitatvLINACVAntVAPLHykdmiipklvdDLGKVKITKSGFL-TFM 79
Cdd:COG1506  84 LAARPYVDPDRIGIYGHSYGGYMALLAAARHPD-----RFKAAVA--LAGVS-----------DLRSYYGTTREYTeRLM 145
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81230487  80 DTWSNPLEEHNHQSLVP-LEKAQVPFLFIVGMDDQSWKSEfYAQIASERLQAHGKERpQIICYPETGHCIDPPYFP 154
Cdd:COG1506 146 GGPWEDPEAYAARSPLAyADKLKTPLLLIHGEADDRVPPE-QAERLYEALKKAGKPV-ELLVYPGEGHGFSGAGAP 219
 
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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