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Conserved domains on  [gi|755506189|ref|XP_011248271|]
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acyl-coenzyme A amino acid N-acyltransferase 2 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
 15-144 1.56e-60

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: 187.83  E-value: 1.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506189   15 DEPVSIRATGLPPSQIVTIKATVKDENDNVFQSQAFYKTNEAGEVDLEKTPALGGDYVGVHPMGLFFSLKPKKAF-HRLM 93
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFrPRLY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755506189   94 KKDVMNSPLCICLDLYDSVnwleTVRIPSKASQRVQRWFVGPGVKREQIQE 144
Cdd:pfam04775  81 KRDVLPTPFVVTLSVYDGS----EESGKPLASVTVERWYMAPGVRRIEVRE 127
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 206-250 1.94e-19

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: 83.87  E-value: 1.94e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 755506189  206 VDLEYFEEAANFLLSHPKIQQPGIGVISTSKGAEIGLAMACYLKQ 250
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQ 45
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
145-246 2.89e-10

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


:

Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 58.82  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506189 145 GRVRGALFLPPGKGPFPGII---DLFGLiGGLVEFRASLLASHGFAVLALAYFAYEDLPEKPQEVD-----------LEY 210
Cdd:COG0412   14 VTLPGYLARPAGGGPRPGVVvlhEIFGL-NPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDPDEARalmgaldpellAAD 92

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755506189 211 FEEAANFLLSHPKIQQPGIGVISTSKGAEIGLAMAC 246
Cdd:COG0412   93 LRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAA 128
 
Name Accession Description Interval E-value
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
 15-144 1.56e-60

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: 187.83  E-value: 1.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506189   15 DEPVSIRATGLPPSQIVTIKATVKDENDNVFQSQAFYKTNEAGEVDLEKTPALGGDYVGVHPMGLFFSLKPKKAF-HRLM 93
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFrPRLY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755506189   94 KKDVMNSPLCICLDLYDSVnwleTVRIPSKASQRVQRWFVGPGVKREQIQE 144
Cdd:pfam04775  81 KRDVLPTPFVVTLSVYDGS----EESGKPLASVTVERWYMAPGVRRIEVRE 127
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
 206-250 1.94e-19

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: 83.87  E-value: 1.94e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 755506189  206 VDLEYFEEAANFLLSHPKIQQPGIGVISTSKGAEIGLAMACYLKQ 250
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQ 45
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
145-246 2.89e-10

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 58.82  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506189 145 GRVRGALFLPPGKGPFPGII---DLFGLiGGLVEFRASLLASHGFAVLALAYFAYEDLPEKPQEVD-----------LEY 210
Cdd:COG0412   14 VTLPGYLARPAGGGPRPGVVvlhEIFGL-NPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDPDEARalmgaldpellAAD 92

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755506189 211 FEEAANFLLSHPKIQQPGIGVISTSKGAEIGLAMAC 246
Cdd:COG0412   93 LRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAA 128
 
Name Accession Description Interval E-value
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
 15-144 1.56e-60

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: 187.83  E-value: 1.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506189   15 DEPVSIRATGLPPSQIVTIKATVKDENDNVFQSQAFYKTNEAGEVDLEKTPALGGDYVGVHPMGLFFSLKPKKAF-HRLM 93
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFrPRLY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755506189   94 KKDVMNSPLCICLDLYDSVnwleTVRIPSKASQRVQRWFVGPGVKREQIQE 144
Cdd:pfam04775  81 KRDVLPTPFVVTLSVYDGS----EESGKPLASVTVERWYMAPGVRRIEVRE 127
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
 206-250 1.94e-19

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: 83.87  E-value: 1.94e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 755506189  206 VDLEYFEEAANFLLSHPKIQQPGIGVISTSKGAEIGLAMACYLKQ 250
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQ 45
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
145-246 2.89e-10

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 58.82  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506189 145 GRVRGALFLPPGKGPFPGII---DLFGLiGGLVEFRASLLASHGFAVLALAYFAYEDLPEKPQEVD-----------LEY 210
Cdd:COG0412   14 VTLPGYLARPAGGGPRPGVVvlhEIFGL-NPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDPDEARalmgaldpellAAD 92

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755506189 211 FEEAANFLLSHPKIQQPGIGVISTSKGAEIGLAMAC 246
Cdd:COG0412   93 LRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAA 128
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
146-245 6.56e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 51.94  E-value: 6.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506189 146 RVRGALFLPPGKGPFPGIIDLFGLIGGLVEF---RASLLASHGFAVLALAYFAYEDLPEKPQEVDLEYFEEAANFLLSHP 222
Cdd:COG1506    9 TLPGWLYLPADGKKYPVVVYVHGGPGSRDDSflpLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARP 88

                         90       100
                 ....*....|....*....|...
gi 755506189 223 KIQQPGIGVISTSKGAEIGLAMA 245
Cdd:COG1506   89 YVDPDRIGIYGHSYGGYMALLAA 111
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 146-245 6.29e-05

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 43.36  E-value: 6.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506189 146 RVRGALFLPPG-KGPFPGIIdLFGLIGGLVEFR---ASLLASHGFAVLALAYFAYEDLPEKP-QEVDLEY--FEEAANFL 218
Cdd:COG1073   22 KLAGDLYLPAGaSKKYPAVV-VAHGNGGVKEQRalyAQRLAELGFNVLAFDYRGYGESEGEPrEEGSPERrdARAAVDYL 100

                         90       100
                 ....*....|....*....|....*..
gi 755506189 219 LSHPKIQQPGIGVISTSKGAEIGLAMA 245
Cdd:COG1073  101 RTLPGVDPERIGLLGISLGGGYALNAA 127
 
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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