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Conserved domains on  [gi|48675862|ref|NP_620262|]
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acyl-coenzyme A thioesterase 2, mitochondrial [Rattus norvegicus]

Protein Classification

similar to acyl-coenzyme A thioesterase( domain architecture ID 10521458)

protein similar to acyl-coenzyme A thioesterase

Graphical summary

 Zoom to residue level

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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 ...
244-451 3.30e-113

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: 331.55  E-value: 3.30e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862   244 MRIEYFEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTVCYKDETIPPVSLLRDKV 323
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862   324 KMTKDGLLDVVEALQSPLV--DKKSFIPVERSDTTFLFLVGQDDHNWKSEFYAREASKRLQAHGKE-KPQIICYPEAGHY 400
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSkpDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 48675862   401 IEPPYFPLCSAGMHLLVGANITFGGEPKPHSVAQLDAWQQLQTFFHKQLSG 451
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
57-182 3.26e-59

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: 190.14  E-value: 3.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862    57 DEPLSITVRGLAPEQPVTLRAALRDEKGALFRAHARYRADAGGELDLARAPALGGSFTGLEPMGLIWAMEPERPLW-RLV 135
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 48675862   136 KRDVQ-KPYVVELEVLDGHEPDgGQRLAQAVHERHFMAPGVRRVPVRD 182
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVRE 127
Axe1 super family cl34617
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
180-294 9.70e-08

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3458:

Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 53.66  E-value: 9.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 180 VRDGRVRATLFLPPEPGPFPGIIDLFGVGGG-LLEYRASLLAGKGFAVMAL---------------AYYNYDDLPKTMeT 243
Cdd:COG3458  64 FGGARIYGWLLRPKGEGPLPAVVEFHGYGGGrGLPHEDLDWAAAGYAVLVMdtrgqgsswgdtpdpGGYSGGALPGYM-T 142
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48675862 244 MRIE-----YFEE-------AVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVV 294
Cdd:COG3458 143 RGIDdpdtyYYRRvyldavrAVDALRSLPEVDGKRIGVTGGSQGGGLALAAAALDPRVKAAAA 205
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
244-451 3.30e-113

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: 331.55  E-value: 3.30e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862   244 MRIEYFEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTVCYKDETIPPVSLLRDKV 323
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862   324 KMTKDGLLDVVEALQSPLV--DKKSFIPVERSDTTFLFLVGQDDHNWKSEFYAREASKRLQAHGKE-KPQIICYPEAGHY 400
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSkpDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 48675862   401 IEPPYFPLCSAGMHLLVGANITFGGEPKPHSVAQLDAWQQLQTFFHKQLSG 451
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
57-182 3.26e-59

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: 190.14  E-value: 3.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862    57 DEPLSITVRGLAPEQPVTLRAALRDEKGALFRAHARYRADAGGELDLARAPALGGSFTGLEPMGLIWAMEPERPLW-RLV 135
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 48675862   136 KRDVQ-KPYVVELEVLDGHEPDgGQRLAQAVHERHFMAPGVRRVPVRD 182
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVRE 127
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
177-445 9.64e-18

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 81.94  E-value: 9.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 177 RVPVRDG-RVRATLFLPPEPGPFPGII---DLFGVGGGLlEYRASLLAGKGFAVMALAYYNYDDLPKTMETMR------- 245
Cdd:COG0412   7 TIPTPDGvTLPGYLARPAGGGPRPGVVvlhEIFGLNPHI-RDVARRLAAAGYVVLAPDLYGRGGPGDDPDEARalmgald 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 246 ----IEYFEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAvgntvcykdetippvsllrd 321
Cdd:COG0412  86 pellAADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPA-------------------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 322 kvkmtkDGLLDVVEALQSPLvdkksfipversdttfLFLVGQDDHNWKSEfYAREASKRLQAHGKEKpQIICYPEAGHyi 401
Cdd:COG0412 146 ------DDLLDLAARIKAPV----------------LLLYGEKDPLVPPE-QVAALEAALAAAGVDV-ELHVYPGAGH-- 199
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 48675862 402 eppyfplcsaGMHllvganitFGGEPKPHSVAQLDAWQQLQTFF 445
Cdd:COG0412 200 ----------GFT--------NPGRPRYDPAAAEDAWQRTLAFL 225
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
180-294 9.70e-08

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 53.66  E-value: 9.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 180 VRDGRVRATLFLPPEPGPFPGIIDLFGVGGG-LLEYRASLLAGKGFAVMAL---------------AYYNYDDLPKTMeT 243
Cdd:COG3458  64 FGGARIYGWLLRPKGEGPLPAVVEFHGYGGGrGLPHEDLDWAAAGYAVLVMdtrgqgsswgdtpdpGGYSGGALPGYM-T 142
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48675862 244 MRIE-----YFEE-------AVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVV 294
Cdd:COG3458 143 RGIDdpdtyYYRRvyldavrAVDALRSLPEVDGKRIGVTGGSQGGGLALAAAALDPRVKAAAA 205
DLH pfam01738
Dienelactone hydrolase family;
186-298 2.13e-04

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 42.34  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862   186 RATLFLPPEPgPFPGII---DLFGVGGGLLEYRASLlAGKGFAVMALAYY-------NYDDLPKTMETMRIEY------- 248
Cdd:pfam01738   1 DAYLATPKNP-PWPVVVvfqEIFGVNDNIREIADRL-ADEGYVALAPDLYfrqgdpnDEADAARAMFELVSKRvmekvld 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 48675862   249 -FEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGS 298
Cdd:pfam01738  79 dLEAAVNYLKSQPEVSPKKVGVVGYCMGGALAVLLAAKGPLVDAAVGFYGV 129
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
244-451 3.30e-113

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: 331.55  E-value: 3.30e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862   244 MRIEYFEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTVCYKDETIPPVSLLRDKV 323
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862   324 KMTKDGLLDVVEALQSPLV--DKKSFIPVERSDTTFLFLVGQDDHNWKSEFYAREASKRLQAHGKE-KPQIICYPEAGHY 400
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSkpDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 48675862   401 IEPPYFPLCSAGMHLLVGANITFGGEPKPHSVAQLDAWQQLQTFFHKQLSG 451
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
57-182 3.26e-59

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: 190.14  E-value: 3.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862    57 DEPLSITVRGLAPEQPVTLRAALRDEKGALFRAHARYRADAGGELDLARAPALGGSFTGLEPMGLIWAMEPERPLW-RLV 135
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 48675862   136 KRDVQ-KPYVVELEVLDGHEPDgGQRLAQAVHERHFMAPGVRRVPVRD 182
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVRE 127
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
177-445 9.64e-18

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 81.94  E-value: 9.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 177 RVPVRDG-RVRATLFLPPEPGPFPGII---DLFGVGGGLlEYRASLLAGKGFAVMALAYYNYDDLPKTMETMR------- 245
Cdd:COG0412   7 TIPTPDGvTLPGYLARPAGGGPRPGVVvlhEIFGLNPHI-RDVARRLAAAGYVVLAPDLYGRGGPGDDPDEARalmgald 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 246 ----IEYFEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAvgntvcykdetippvsllrd 321
Cdd:COG0412  86 pellAADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPA-------------------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 322 kvkmtkDGLLDVVEALQSPLvdkksfipversdttfLFLVGQDDHNWKSEfYAREASKRLQAHGKEKpQIICYPEAGHyi 401
Cdd:COG0412 146 ------DDLLDLAARIKAPV----------------LLLYGEKDPLVPPE-QVAALEAALAAAGVDV-ELHVYPGAGH-- 199
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 48675862 402 eppyfplcsaGMHllvganitFGGEPKPHSVAQLDAWQQLQTFF 445
Cdd:COG0412 200 ----------GFT--------NPGRPRYDPAAAEDAWQRTLAFL 225
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
177-407 2.52e-17

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 80.83  E-value: 2.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 177 RVPVRDG-RVRATLFLPPEPGPFPGIIDLFGVGGGLLE---YRASLLAGKGFAVMALAYYNYDDLPKTMETMRIEYFEEA 252
Cdd:COG1506   1 TFKSADGtTLPGWLYLPADGKKYPVVVYVHGGPGSRDDsflPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 253 VNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVingSVAAVGNTVCYKDETIPPVSLLRDKVKMTKDGL-- 330
Cdd:COG1506  81 IDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAV---ALAGVSDLRSYYGTTREYTERLMGGPWEDPEAYaa 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 331 ---LDVVEALQSPLvdkksfipversdttfLFLVGQDDHNWKSEfYAREASKRLQAHGKEKpQIICYPEAGHYIEPPYFP 407
Cdd:COG1506 158 rspLAYADKLKTPL----------------LLIHGEADDRVPPE-QAERLYEALKKAGKPV-ELLVYPGEGHGFSGAGAP 219
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
178-400 1.50e-12

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 67.25  E-value: 1.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 178 VPVRDG-RVRATLFLPP-EPGPFPGIIdLFGVGGGLLEYR---ASLLAGKGFAVMALAYYNYDD---LPKTMETMRIEYF 249
Cdd:COG1073  15 FKSRDGiKLAGDLYLPAgASKKYPAVV-VAHGNGGVKEQRalyAQRLAELGFNVLAFDYRGYGEsegEPREEGSPERRDA 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 250 EEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVING--SVAAVGN--TVCYKDETIPPVSLLrdkvkm 325
Cdd:COG1073  94 RAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDSPftSLEDLAAqrAKEARGAYLPGVPYL------ 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48675862 326 TKDGLLDVVEALQSPLVDkksfipVERSDTTFLFLVGQDDHnwkseFYAREASKRLQAHGKEKPQIICYPEAGHY 400
Cdd:COG1073 168 PNVRLASLLNDEFDPLAK------IEKISRPLLFIHGEKDE-----AVPFYMSEDLYEAAAEPKELLIVPGAGHV 231
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
180-294 9.70e-08

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 53.66  E-value: 9.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862 180 VRDGRVRATLFLPPEPGPFPGIIDLFGVGGG-LLEYRASLLAGKGFAVMAL---------------AYYNYDDLPKTMeT 243
Cdd:COG3458  64 FGGARIYGWLLRPKGEGPLPAVVEFHGYGGGrGLPHEDLDWAAAGYAVLVMdtrgqgsswgdtpdpGGYSGGALPGYM-T 142
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48675862 244 MRIE-----YFEE-------AVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVV 294
Cdd:COG3458 143 RGIDdpdtyYYRRvyldavrAVDALRSLPEVDGKRIGVTGGSQGGGLALAAAALDPRVKAAAA 205
DLH pfam01738
Dienelactone hydrolase family;
186-298 2.13e-04

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 42.34  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675862   186 RATLFLPPEPgPFPGII---DLFGVGGGLLEYRASLlAGKGFAVMALAYY-------NYDDLPKTMETMRIEY------- 248
Cdd:pfam01738   1 DAYLATPKNP-PWPVVVvfqEIFGVNDNIREIADRL-ADEGYVALAPDLYfrqgdpnDEADAARAMFELVSKRvmekvld 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 48675862   249 -FEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGS 298
Cdd:pfam01738  79 dLEAAVNYLKSQPEVSPKKVGVVGYCMGGALAVLLAAKGPLVDAAVGFYGV 129
 
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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