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Conserved domains on  [gi|1398331575|ref|NP_001351106|]
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acyl-coenzyme A thioesterase 2, mitochondrial 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 ...
68-277 2.01e-127

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: 360.83  E-value: 2.01e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575  68 LHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELCLSMASFLKGITAAVVINGSVANVGGTLHYKGETLPPVGVNRNRI 147
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575 148 KVTKDGYADIVDVLNSPLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRR-KPQIICYPETGHY 226
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1398331575 227 IEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGG 277
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 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 ...
68-277 2.01e-127

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: 360.83  E-value: 2.01e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575  68 LHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELCLSMASFLKGITAAVVINGSVANVGGTLHYKGETLPPVGVNRNRI 147
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575 148 KVTKDGYADIVDVLNSPLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRR-KPQIICYPETGHY 226
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1398331575 227 IEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGG 277
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
7-271 4.78e-10

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 58.44  E-value: 4.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575   7 GAVPGVSTAEAEPGPFPGIV---DMFGTGGGLlEYRASLLAGKGFAVMALAYYNYEDLPKTMET-----------LHLEY 72
Cdd:COG0412    14 VTLPGYLARPAGGGPRPGVVvlhEIFGLNPHI-RDVARRLAAAGYVVLAPDLYGRGGPGDDPDEaralmgaldpeLLAAD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575  73 FEEAMNYLLSHPEVKGPGVGLLGISKGGELCLSMASFLKGITAAVVINGSvanvggtlhykgetlppvgvnrnrikVTKD 152
Cdd:COG0412    93 LRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGG--------------------------LPAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575 153 GYADIVDVLNSPLegpdqksfipveraestfLFLVGQDDHNWKSEfYANEACKRLQAHGRRKpQIICYPETGHyieppyf 232
Cdd:COG0412   147 DLLDLAARIKAPV------------------LLLYGEKDPLVPPE-QVAALEAALAAAGVDV-ELHVYPGAGH------- 199
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1398331575 233 plcraSLHALvgspiiwgGEPRAHAMAQVDAWKQLQTFF 271
Cdd:COG0412   200 -----GFTNP--------GRPRYDPAAAEDAWQRTLAFL 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 ...
68-277 2.01e-127

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: 360.83  E-value: 2.01e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575  68 LHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELCLSMASFLKGITAAVVINGSVANVGGTLHYKGETLPPVGVNRNRI 147
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575 148 KVTKDGYADIVDVLNSPLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRR-KPQIICYPETGHY 226
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1398331575 227 IEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGG 277
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
7-271 4.78e-10

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 58.44  E-value: 4.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575   7 GAVPGVSTAEAEPGPFPGIV---DMFGTGGGLlEYRASLLAGKGFAVMALAYYNYEDLPKTMET-----------LHLEY 72
Cdd:COG0412    14 VTLPGYLARPAGGGPRPGVVvlhEIFGLNPHI-RDVARRLAAAGYVVLAPDLYGRGGPGDDPDEaralmgaldpeLLAAD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575  73 FEEAMNYLLSHPEVKGPGVGLLGISKGGELCLSMASFLKGITAAVVINGSvanvggtlhykgetlppvgvnrnrikVTKD 152
Cdd:COG0412    93 LRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGG--------------------------LPAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575 153 GYADIVDVLNSPLegpdqksfipveraestfLFLVGQDDHNWKSEfYANEACKRLQAHGRRKpQIICYPETGHyieppyf 232
Cdd:COG0412   147 DLLDLAARIKAPV------------------LLLYGEKDPLVPPE-QVAALEAALAAAGVDV-ELHVYPGAGH------- 199
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1398331575 233 plcraSLHALvgspiiwgGEPRAHAMAQVDAWKQLQTFF 271
Cdd:COG0412   200 -----GFTNP--------GRPRYDPAAAEDAWQRTLAFL 225
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
17-233 2.01e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 56.56  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575  17 AEPGPFPGIVDMFGTGGGLLE---YRASLLAGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGL 93
Cdd:COG1506    18 ADGKKYPVVVYVHGGPGSRDDsflPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARPYVDPDRIGI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331575  94 LGISKGGELCLSMASFLKGITAAVVINGSVANvggtlhykgetlppvgvNRNRIKVTKDGYADIVDVLNSPLEGPDQKSf 173
Cdd:COG1506    98 YGHSYGGYMALLAAARHPDRFKAAVALAGVSD-----------------LRSYYGTTREYTERLMGGPWEDPEAYAARS- 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398331575 174 iPVERAEST---FLFLVGQDDHNWKSEfYANEACKRLQAHGRRKpQIICYPETGHYIEPPYFP 233
Cdd:COG1506   160 -PLAYADKLktpLLLIHGEADDRVPPE-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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