NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1761000912|ref|NP_001361644|]
View 

bile acid-CoA:amino acid N-acyltransferase [Homo sapiens]

Protein Classification

acyl-CoA thioesterase/bile acid-CoA:amino acid N-acyltransferase family protein( domain architecture ID 10521460)

acyl-CoA thioesterase/bile acid-CoA:amino acid N-acyltransferase (BAAT) family protein may catalyze the hydrolysis of acyl-CoA or catalyze the amidation of bile acids with the amino acids taurine and glycine

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
206-412 4.26e-97

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: 289.18  E-value: 4.26e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 206 TDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQIGLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLI 285
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 286 STNALGLLELYRTFETTQVG-ASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKN-NWTLLSYPGAGHL 363
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKpDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1761000912 364 IEPPYSPLCCASTTHDL--RLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIP 412
Cdd:pfam08840 161 IEPPYFPHCGASFHALVgmPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
14-144 4.62e-62

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: 196.30  E-value: 4.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912  14 DEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDLNHASSLGGDYMGVHPMGLFWSLKPEKLLT-RLL 92
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1761000912  93 KRDVMNRPFQVQVKLYDlelivNNKVASAPKASLTLERWYVAPGVTRIKVRE 144
Cdd:pfam04775  81 KRDVLPTPFVVTLSVYD-----GSEESGKPLASVTVERWYMAPGVRRIEVRE 127
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
206-412 4.26e-97

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: 289.18  E-value: 4.26e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 206 TDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQIGLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLI 285
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 286 STNALGLLELYRTFETTQVG-ASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKN-NWTLLSYPGAGHL 363
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKpDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1761000912 364 IEPPYSPLCCASTTHDL--RLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIP 412
Cdd:pfam08840 161 IEPPYFPHCGASFHALVgmPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
14-144 4.62e-62

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: 196.30  E-value: 4.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912  14 DEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDLNHASSLGGDYMGVHPMGLFWSLKPEKLLT-RLL 92
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1761000912  93 KRDVMNRPFQVQVKLYDlelivNNKVASAPKASLTLERWYVAPGVTRIKVRE 144
Cdd:pfam04775  81 KRDVLPTPFVVTLSVYD-----GSEESGKPLASVTVERWYMAPGVRRIEVRE 127
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
139-410 1.24e-11

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 64.27  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 139 RIKVREG-RLRGALFLPPGEGLFPGVID---LFGGLGGLLEFRASLLASRGFASLALAYHNYEDLPRKPEVTDLEYFEEA 214
Cdd:COG1506     1 TFKSADGtTLPGWLYLPADGKKYPVVVYvhgGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 215 ANFLLRHPKVFGSGVGVVSVCQGVQIGL-SMAIYLKQVTATVLING-TNFPFGIPQVYH-GQIHQPLPHSAQlistnalg 291
Cdd:COG1506    81 IDYLAARPYVDPDRIGIYGHSYGGYMALlAAARHPDRFKAAVALAGvSDLRSYYGTTREyTERLMGGPWEDP-------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 292 llELYRTFETtqvgasqyLFPIEEAQGQFLFIVGEGDKTInSKAHAEQAIGQLKRHGKnNWTLLSYPGAGHLIEPPYSPl 371
Cdd:COG1506   153 --EAYAARSP--------LAYADKLKTPLLLIHGEADDRV-PPEQAERLYEALKKAGK-PVELLVYPGEGHGFSGAGAP- 219
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1761000912 372 ccastthdlrlhwggeviphaaaqeHAWKEIQRFLRKHL 410
Cdd:COG1506   220 -------------------------DYLERILDFLDRHL 233
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
206-412 4.26e-97

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: 289.18  E-value: 4.26e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 206 TDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQIGLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLI 285
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 286 STNALGLLELYRTFETTQVG-ASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKN-NWTLLSYPGAGHL 363
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKpDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1761000912 364 IEPPYSPLCCASTTHDL--RLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIP 412
Cdd:pfam08840 161 IEPPYFPHCGASFHALVgmPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
14-144 4.62e-62

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: 196.30  E-value: 4.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912  14 DEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDLNHASSLGGDYMGVHPMGLFWSLKPEKLLT-RLL 92
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1761000912  93 KRDVMNRPFQVQVKLYDlelivNNKVASAPKASLTLERWYVAPGVTRIKVRE 144
Cdd:pfam04775  81 KRDVLPTPFVVTLSVYD-----GSEESGKPLASVTVERWYMAPGVRRIEVRE 127
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
139-410 1.24e-11

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 64.27  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 139 RIKVREG-RLRGALFLPPGEGLFPGVID---LFGGLGGLLEFRASLLASRGFASLALAYHNYEDLPRKPEVTDLEYFEEA 214
Cdd:COG1506     1 TFKSADGtTLPGWLYLPADGKKYPVVVYvhgGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 215 ANFLLRHPKVFGSGVGVVSVCQGVQIGL-SMAIYLKQVTATVLING-TNFPFGIPQVYH-GQIHQPLPHSAQlistnalg 291
Cdd:COG1506    81 IDYLAARPYVDPDRIGIYGHSYGGYMALlAAARHPDRFKAAVALAGvSDLRSYYGTTREyTERLMGGPWEDP-------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 292 llELYRTFETtqvgasqyLFPIEEAQGQFLFIVGEGDKTInSKAHAEQAIGQLKRHGKnNWTLLSYPGAGHLIEPPYSPl 371
Cdd:COG1506   153 --EAYAARSP--------LAYADKLKTPLLLIHGEADDRV-PPEQAERLYEALKKAGK-PVELLVYPGEGHGFSGAGAP- 219
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1761000912 372 ccastthdlrlhwggeviphaaaqeHAWKEIQRFLRKHL 410
Cdd:COG1506   220 -------------------------DYLERILDFLDRHL 233
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
138-407 5.00e-10

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 59.21  E-value: 5.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 138 TRIKVREG-RLRGALFLPPGEGLFPGVI---------DLFgglggllEFRASLLASRGFASLAL-AYHNYEDLPRKPEVT 206
Cdd:COG0412     6 VTIPTPDGvTLPGYLARPAGGGPRPGVVvlheifglnPHI-------RDVARRLAAAGYVVLAPdLYGRGGPGDDPDEAR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 207 DL----------EYFEEAANFLLRHPKVFGSGVGVVSVCQGVQIGLSMAIYLKQVTATVLINGtnfpfgipqvyhGQIHQ 276
Cdd:COG0412    79 ALmgaldpellaADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYG------------GLPAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000912 277 PLPHSAQLISTnalgllelyrtfettqvgasqylfPIeeaqgqfLFIVGEGDKTINsKAHAEQAIGQLKRHGKnNWTLLS 356
Cdd:COG0412   147 DLLDLAARIKA------------------------PV-------LLLYGEKDPLVP-PEQVAALEAALAAAGV-DVELHV 193
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1761000912 357 YPGAGHLIEPPYSPLccastthdlrlhwggeviPHAAAQEHAWKEIQRFLR 407
Cdd:COG0412   194 YPGAGHGFTNPGRPR------------------YDPAAAEDAWQRTLAFLA 226
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH