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Conserved domains on  [gi|568925970|ref|XP_006537628|]
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bile acid-CoA:amino acid N-acyltransferase isoform X1 [Mus musculus]

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 ...
33-241 1.19e-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: 296.50  E-value: 1.19e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970   33 VDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRATVLINGPNFVSQSPHVYHGQVYPPVPSNEEFV 112
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970  113 VTNALGLVEFYRTFQETADK-DSKYCFPIEKAHGHFLFVVGEDDKNLNSKVHANQAIAQLMKNGKK-NWTLLSYPGAGHL 190
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKpDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568925970  191 IEPPYTPLCQASRMPILIPSLSWGGEVIPHAAAQEHSWKEIQKFLKQHLLP 241
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 ...
33-241 1.19e-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: 296.50  E-value: 1.19e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970   33 VDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRATVLINGPNFVSQSPHVYHGQVYPPVPSNEEFV 112
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970  113 VTNALGLVEFYRTFQETADK-DSKYCFPIEKAHGHFLFVVGEDDKNLNSKVHANQAIAQLMKNGKK-NWTLLSYPGAGHL 190
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKpDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568925970  191 IEPPYTPLCQASRMPILIPSLSWGGEVIPHAAAQEHSWKEIQKFLKQHLLP 241
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
1-236 5.78e-11

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 60.37  E-value: 5.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970   1 MEFRASLLASRGFATLAL-------AYWNYDDLPSRLEKVD----LEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGL 69
Cdd:COG0412   45 IRDVARRLAAAGYVVLAPdlygrggPGDDPDEARALMGALDpellAADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLAL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970  70 SMAINLKQIRATVlingpnfvsqsphVYHGQvyPPVPSNEEfvvtnalglvefyrtfqetadkdskycfPIEKAHGHFLF 149
Cdd:COG0412  125 LAAARGPDLAAAV-------------SFYGG--LPADDLLD----------------------------LAARIKAPVLL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970 150 VVGEDDKNLNskVHANQAIAQLMKNGKKNWTLLSYPGAGHLIEPPYTPLcqasrmpilipslswggeviPHAAAQEHSWK 229
Cdd:COG0412  162 LYGEKDPLVP--PEQVAALEAALAAAGVDVELHVYPGAGHGFTNPGRPR--------------------YDPAAAEDAWQ 219

                 ....*..
gi 568925970 230 EIQKFLK 236
Cdd:COG0412  220 RTLAFLA 226
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
33-241 1.19e-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: 296.50  E-value: 1.19e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970   33 VDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRATVLINGPNFVSQSPHVYHGQVYPPVPSNEEFV 112
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970  113 VTNALGLVEFYRTFQETADK-DSKYCFPIEKAHGHFLFVVGEDDKNLNSKVHANQAIAQLMKNGKK-NWTLLSYPGAGHL 190
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKpDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568925970  191 IEPPYTPLCQASRMPILIPSLSWGGEVIPHAAAQEHSWKEIQKFLKQHLLP 241
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
1-236 5.78e-11

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 60.37  E-value: 5.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970   1 MEFRASLLASRGFATLAL-------AYWNYDDLPSRLEKVD----LEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGL 69
Cdd:COG0412   45 IRDVARRLAAAGYVVLAPdlygrggPGDDPDEARALMGALDpellAADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLAL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970  70 SMAINLKQIRATVlingpnfvsqsphVYHGQvyPPVPSNEEfvvtnalglvefyrtfqetadkdskycfPIEKAHGHFLF 149
Cdd:COG0412  125 LAAARGPDLAAAV-------------SFYGG--LPADDLLD----------------------------LAARIKAPVLL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970 150 VVGEDDKNLNskVHANQAIAQLMKNGKKNWTLLSYPGAGHLIEPPYTPLcqasrmpilipslswggeviPHAAAQEHSWK 229
Cdd:COG0412  162 LYGEKDPLVP--PEQVAALEAALAAAGVDVELHVYPGAGHGFTNPGRPR--------------------YDPAAAEDAWQ 219

                 ....*..
gi 568925970 230 EIQKFLK 236
Cdd:COG0412  220 RTLAFLA 226
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
4-197 4.85e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 55.02  E-value: 4.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970   4 RASLLASRGFATLALAYWNYDDLPSRLEKVDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGL-SMAINLKQIRATV 82
Cdd:COG1506   43 LAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARPYVDPDRIGIYGHSYGGYMALlAAARHPDRFKAAV 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970  83 LINGP-NFVSQSPHVYH-GQVYPPVPSNEEfvvtnalglvEFYRTFQetadkdskycfPIEKAH---GHFLFVVGEDDKN 157
Cdd:COG1506  123 ALAGVsDLRSYYGTTREyTERLMGGPWEDP----------EAYAARS-----------PLAYADklkTPLLLIHGEADDR 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568925970 158 lnskVHANQA--IAQLMKNGKKNWTLLSYPGAGHLIEPPYTP 197
Cdd:COG1506  182 ----VPPEQAerLYEALKKAGKPVELLVYPGEGHGFSGAGAP 219
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
5-189 4.77e-07

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 49.53  E-value: 4.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970   5 ASLLASRGFATLALAYWNYDD---LPSRLEKVDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRAT 81
Cdd:COG1073   57 AQRLAELGFNVLAFDYRGYGEsegEPREEGSPERRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRVKAV 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925970  82 VLINGPN----FVSQSPHVYHGQVYPPVPsneefvVTNALGLVEFYRTFQETADKdskycfpIEKAHGHFLFVVGEDDkn 157
Cdd:COG1073  137 ILDSPFTsledLAAQRAKEARGAYLPGVP------YLPNVRLASLLNDEFDPLAK-------IEKISRPLLFIHGEKD-- 201
                        170       180       190
                 ....*....|....*....|....*....|..
gi 568925970 158 lnsKVHANQAIAQLMKNGKKNWTLLSYPGAGH 189
Cdd:COG1073  202 ---EAVPFYMSEDLYEAAAEPKELLIVPGAGH 230
 
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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