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Conserved domains on  [gi|1887096806|ref|NP_001138836|]
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sn-1-specific diacylglycerol lipase ABHD11 isoform 8 [Homo sapiens]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 58-248 1.15e-38

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


:

Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 133.97  E-value: 1.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  58 PAVVFLHGLFGSKTNFNSIAKILAQqtGRRVLTVDARNHGDSPHSP-DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGK 136
Cdd:COG0596    24 PPVVLLHGLPGSSYEWRPLIPALAA--GYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 137 TAMLLALQRDMAVRQ-HLLTNLVEVDGRFVWR--VNLDALTQHLDKILAFPQRQ--ESYLGPTLFLLGGNSQFVHPSHHP 211
Cdd:COG0596   102 VALELAARHPERVAGlVLVDEVLAALAEPLRRpgLAPEALAALLRALARTDLRErlARITVPTLVIWGEKDPIVPPALAR 181

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1887096806 212 EIMRLFPRAQMQTVPNAGHWIHADRPQDFIAAIRGFL 248
Cdd:COG0596   182 RLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFL 218
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 58-248 1.15e-38

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 133.97  E-value: 1.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  58 PAVVFLHGLFGSKTNFNSIAKILAQqtGRRVLTVDARNHGDSPHSP-DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGK 136
Cdd:COG0596    24 PPVVLLHGLPGSSYEWRPLIPALAA--GYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 137 TAMLLALQRDMAVRQ-HLLTNLVEVDGRFVWR--VNLDALTQHLDKILAFPQRQ--ESYLGPTLFLLGGNSQFVHPSHHP 211
Cdd:COG0596   102 VALELAARHPERVAGlVLVDEVLAALAEPLRRpgLAPEALAALLRALARTDLRErlARITVPTLVIWGEKDPIVPPALAR 181

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1887096806 212 EIMRLFPRAQMQTVPNAGHWIHADRPQDFIAAIRGFL 248
Cdd:COG0596   182 RLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFL 218
PRK10673 PRK10673
esterase;
44-248 2.37e-37

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 131.78  E-value: 2.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  44 LPLSYRLLDGE---AALPaVVFLHGLFGSKTNFNSIAKILaqQTGRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQ 120
Cdd:PRK10673    1 MKLNIRAQTAQnphNNSP-IVLVHGLFGSLDNLGVLARDL--VNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 121 LGLVPCVVVGHSMGGKTAML---LALQR------------DMAVRQH------------------------LLTNLVE-- 159
Cdd:PRK10673   78 LQIEKATFIGHSMGGKAVMAltaLAPDRidklvaidiapvDYHVRRHdeifaainavseagattrqqaaaiMRQHLNEeg 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 160 ---------VDGRfvWRVNLDALTQHLDKILAFpQRQESYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGH 230
Cdd:PRK10673  158 viqfllksfVDGE--WRFNVPVLWDQYPHIVGW-EKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGH 234

                         250
                  ....*....|....*...
gi 1887096806 231 WIHADRPQDFIAAIRGFL 248
Cdd:PRK10673  235 WVHAEKPDAVLRAIRRYL 252
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 58-237 1.18e-18

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 82.17  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  58 PAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSP---DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMG 134
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARD-GFRVIALDLRGFGKSSRPKaqdDYRTDDLAEDLEYILEALGLEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 135 GKTAMLLALQRDMAVR-----------QHLLTNLVEVDGRFVWRVNLDAL------------------------------ 173
Cdd:pfam00561  80 GLIALAYAAKYPDRVKalvllgaldppHELDEADRFILALFPGFFDGFVAdfapnplgrlvakllallllrlrllkalpl 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 174 -----------------TQHLDKILAFPQRQE-----SYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGHW 231
Cdd:pfam00561 160 lnkrfpsgdyalakslvTGALLFIETWSTELRakflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHF 239


                  ....*.
gi 1887096806 232 IHADRP 237
Cdd:pfam00561 240 AFLEGP 245
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 46-248 9.08e-10

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 57.37  E-value: 9.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  46 LSYRLLDGEAALPAVVFLHGLfgsKTNFNSIAKILAQQTGR-RVLTVDARNHGDSPhSPDMSYEI--MSQDLQDLLPQLG 122
Cdd:TIGR02427   2 LHYRLDGAADGAPVLVFINSL---GTDLRMWDPVLPALTPDfRVLRYDKRGHGLSD-APEGPYSIedLADDVLALLDHLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 123 LVPCVVVGHSMGGKTAMLLAL-------------------------QRDMAVRQHLLTNLVE-VDGRFVWRVNLDALTQH 176
Cdd:TIGR02427  78 IERAVFCGLSLGGLIAQGLAArrpdrvralvlsntaakigtpeswnARIAAVRAEGLAALADaVLERWFTPGFREAHPAR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 177 LDKILAFPQRQ--ESYLG-------------------PTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGHWIHAD 235
Cdd:TIGR02427 158 LDLYRNMLVRQppDGYAGccaairdadfrdrlgaiavPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVE 237

                         250
                  ....*....|...
gi 1887096806 236 RPQDFIAAIRGFL 248
Cdd:TIGR02427 238 QPEAFNAALRDFL 250
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 58-248 1.15e-38

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 133.97  E-value: 1.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  58 PAVVFLHGLFGSKTNFNSIAKILAQqtGRRVLTVDARNHGDSPHSP-DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGK 136
Cdd:COG0596    24 PPVVLLHGLPGSSYEWRPLIPALAA--GYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 137 TAMLLALQRDMAVRQ-HLLTNLVEVDGRFVWR--VNLDALTQHLDKILAFPQRQ--ESYLGPTLFLLGGNSQFVHPSHHP 211
Cdd:COG0596   102 VALELAARHPERVAGlVLVDEVLAALAEPLRRpgLAPEALAALLRALARTDLRErlARITVPTLVIWGEKDPIVPPALAR 181

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1887096806 212 EIMRLFPRAQMQTVPNAGHWIHADRPQDFIAAIRGFL 248
Cdd:COG0596   182 RLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFL 218
PRK10673 PRK10673
esterase;
44-248 2.37e-37

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 131.78  E-value: 2.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  44 LPLSYRLLDGE---AALPaVVFLHGLFGSKTNFNSIAKILaqQTGRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQ 120
Cdd:PRK10673    1 MKLNIRAQTAQnphNNSP-IVLVHGLFGSLDNLGVLARDL--VNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 121 LGLVPCVVVGHSMGGKTAML---LALQR------------DMAVRQH------------------------LLTNLVE-- 159
Cdd:PRK10673   78 LQIEKATFIGHSMGGKAVMAltaLAPDRidklvaidiapvDYHVRRHdeifaainavseagattrqqaaaiMRQHLNEeg 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 160 ---------VDGRfvWRVNLDALTQHLDKILAFpQRQESYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGH 230
Cdd:PRK10673  158 viqfllksfVDGE--WRFNVPVLWDQYPHIVGW-EKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGH 234

                         250
                  ....*....|....*...
gi 1887096806 231 WIHADRPQDFIAAIRGFL 248
Cdd:PRK10673  235 WVHAEKPDAVLRAIRRYL 252
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
48-248 4.43e-21

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 88.14  E-value: 4.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  48 YRLLDGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSPDM--SYEIMSQDLQ---DLLPQLG 122
Cdd:COG2267    19 RRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPRGHvdSFDDYVDDLRaalDALRARP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 123 LVPCVVVGHSMGGKTAMLLALQRDMAVRQhlltnLVEVDGRFVWRVnLDALTQHLDKILAFPQRQESYLGPTLFLLGGNS 202
Cdd:COG2267    98 GLPVVLLGHSMGGLIALLYAARYPDRVAG-----LVLLAPAYRADP-LLGPSARWLRALRLAEALARIDVPVLVLHGGAD 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1887096806 203 QFVHPSHHPEIM-RLFPRAQMQTVPNAGHWIHADRPQD-FIAAIRGFL 248
Cdd:COG2267   172 RVVPPEAARRLAaRLSPDVELVLLPGARHELLNEPAREeVLAAILAWL 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 58-237 1.18e-18

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 82.17  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  58 PAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSP---DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMG 134
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARD-GFRVIALDLRGFGKSSRPKaqdDYRTDDLAEDLEYILEALGLEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 135 GKTAMLLALQRDMAVR-----------QHLLTNLVEVDGRFVWRVNLDAL------------------------------ 173
Cdd:pfam00561  80 GLIALAYAAKYPDRVKalvllgaldppHELDEADRFILALFPGFFDGFVAdfapnplgrlvakllallllrlrllkalpl 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 174 -----------------TQHLDKILAFPQRQE-----SYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGHW 231
Cdd:pfam00561 160 lnkrfpsgdyalakslvTGALLFIETWSTELRakflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHF 239


                  ....*.
gi 1887096806 232 IHADRP 237
Cdd:pfam00561 240 AFLEGP 245
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
52-248 2.49e-13

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 67.35  E-value: 2.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  52 DGEAALPAVVFLHGLFGSKTN-FNSIAKILAQQtGRRVLTVDARNHGDSPHSPdmsYEIMSQDLQ---DLLPQLGLVP-- 125
Cdd:COG1506    18 ADGKKYPVVVYVHGGPGSRDDsFLPLAQALASR-GYAVLAPDYRGYGESAGDW---GGDEVDDVLaaiDYLAARPYVDpd 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 126 -CVVVGHSMGGKTAMLLALQRD----MAVRQHLLTNLVEVDGRFVWRVNLDALTQHLDKILAFPQRQESYL----GPTLF 196
Cdd:COG1506    94 rIGIYGHSYGGYMALLAAARHPdrfkAAVALAGVSDLRSYYGTTREYTERLMGGPWEDPEAYAARSPLAYAdklkTPLLL 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1887096806 197 LLGGNSQFVHPSHhpeIMRLF-------PRAQMQTVPNAGHWIHADRPQDFIAAIRGFL 248
Cdd:COG1506   174 IHGEADDRVPPEQ---AERLYealkkagKPVELLVYPGEGHGFSGAGAPDYLERILDFL 229
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 52-248 4.63e-12

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 63.78  E-value: 4.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  52 DGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSP--DMSYEImsQDLQDLLPQLGLVPCV-- 127
Cdd:COG1073    32 GASKKYPAVVVAHGNGGVKEQRALYAQRLAEL-GFNVLAFDYRGYGESEGEPreEGSPER--RDARAAVDYLRTLPGVdp 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 128 ----VVGHSMGGKTAMLLA---------------LQRDMAVRQHLLTNLVEVDGRFVWRVNL---DALTQHLDkilAFpQ 185
Cdd:COG1073   109 erigLLGISLGGGYALNAAatdprvkavildspfTSLEDLAAQRAKEARGAYLPGVPYLPNVrlaSLLNDEFD---PL-A 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887096806 186 RQESYLGPTLFLLGGNSQFvHPSHHPEimRLFPRA----QMQTVPNAGHWIHADRPQD-FIAAIRGFL 248
Cdd:COG1073   185 KIEKISRPLLFIHGEKDEA-VPFYMSE--DLYEAAaepkELLIVPGAGHVDLYDRPEEeYFDKLAEFF 249
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 60-243 6.41e-11

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 60.18  E-value: 6.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  60 VVFLHGLFGSKTNFNSiakilAQQTGRRVLTVDARNHGDSPHSPDMSYEImsQDLQDLLPQLGLV-PCVVVGHSMGGKTA 138
Cdd:pfam12697   1 VVLVHGAGLSAAPLAA-----LLAAGVAVLAPDLPGHGSSSPPPLDLADL--ADLAALLDELGAArPVVLVGHSLGGAVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 139 MLLA-------------------LQRDMAVRQHLLTNLV----------------EVDGRFVWRVNLDALTQHLDKILAF 183
Cdd:pfam12697  74 LAAAaaalvvgvlvaplaappglLAALLALLARLGAALAapawlaaeslargfldDLPADAEWAAALARLAALLAALALL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 184 PQRQESYLGPTLFLLGGNSQFVHPsHHPEIMRLFPRAQMQTVPNAGHWIHaDRPQDFIAA 243
Cdd:pfam12697 154 PLAAWRDLPVPVLVLAEEDRLVPE-LAQRLLAALAGARLVVLPGAGHLPL-DDPEEVAEA 211
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 58-154 7.75e-11

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 60.24  E-value: 7.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  58 PAVVFLHGLFGSKTNFNSIAKILAQqtgRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGKT 137
Cdd:PRK11126    3 PWLVFLHGLLGSGQDWQPVGEALPD---YPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRI 79

                          90
                  ....*....|....*..
gi 1887096806 138 AMLLALQRDMAVRQHLL 154
Cdd:PRK11126   80 AMYYACQGLAGGLCGLI 96
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
52-235 2.14e-10

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 58.82  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  52 DGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSPDMSYEIMSQ--------DLQ---DLLPQ 120
Cdd:COG0412    24 AGGGPRPGVVVLHEIFGLNPHIRDVARRLAAA-GYVVLAPDLYGRGGPGDDPDEARALMGAldpellaaDLRaalDWLKA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 121 LGLV---PCVVVGHSMGGKTAMLLALQRDmavrqhlltnlvEVDGRFVW--RVNLDALTQHLDKILAfpqrqesylgPTL 195
Cdd:COG0412   103 QPEVdagRVGVVGFCFGGGLALLAAARGP------------DLAAAVSFygGLPADDLLDLAARIKA----------PVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1887096806 196 FLLGGNSQFVHPSHHPEIMRLFPRA----QMQTVPNAGHWIHAD 235
Cdd:COG0412   161 LLYGEKDPLVPPEQVAALEAALAAAgvdvELHVYPGAGHGFTNP 204
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 53-248 3.93e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 59.19  E-value: 3.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  53 GEAALPAVVFLHGLFGSKTN--FNsiakILAQQTGRRVLTVDARNHGDS-PHSPDMSYEIMSQDLQDLLPQLGLVPCVVV 129
Cdd:PRK14875  127 GEGDGTPVVLIHGFGGDLNNwlFN----HAALAAGRPVIALDLPGHGASsKAVGAGSLDELAAAVLAFLDALGIERAHLV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 130 GHSMGGKTAMLLAL----------------------------------QRDMA-VRQHLLTNLVEVDGRFVWRV----NL 170
Cdd:PRK14875  203 GHSMGGAVALRLAArapqrvasltliapaglgpeingdyidgfvaaesRRELKpVLELLFADPALVTRQMVEDLlkykRL 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 171 DALTQHLDKILA--FPQ-RQESYLG--------PTLFLLGGNSQFVhPSHHPEimRLFPRAQMQTVPNAGHWIHADRPQD 239
Cdd:PRK14875  283 DGVDDALRALADalFAGgRQRVDLRdrlaslaiPVLVIWGEQDRII-PAAHAQ--GLPDGVAVHVLPGAGHMPQMEAAAD 359


                  ....*....
gi 1887096806 240 FIAAIRGFL 248
Cdd:PRK14875  360 VNRLLAEFL 368
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 46-248 9.08e-10

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 57.37  E-value: 9.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  46 LSYRLLDGEAALPAVVFLHGLfgsKTNFNSIAKILAQQTGR-RVLTVDARNHGDSPhSPDMSYEI--MSQDLQDLLPQLG 122
Cdd:TIGR02427   2 LHYRLDGAADGAPVLVFINSL---GTDLRMWDPVLPALTPDfRVLRYDKRGHGLSD-APEGPYSIedLADDVLALLDHLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 123 LVPCVVVGHSMGGKTAMLLAL-------------------------QRDMAVRQHLLTNLVE-VDGRFVWRVNLDALTQH 176
Cdd:TIGR02427  78 IERAVFCGLSLGGLIAQGLAArrpdrvralvlsntaakigtpeswnARIAAVRAEGLAALADaVLERWFTPGFREAHPAR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 177 LDKILAFPQRQ--ESYLG-------------------PTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGHWIHAD 235
Cdd:TIGR02427 158 LDLYRNMLVRQppDGYAGccaairdadfrdrlgaiavPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVE 237

                         250
                  ....*....|...
gi 1887096806 236 RPQDFIAAIRGFL 248
Cdd:TIGR02427 238 QPEAFNAALRDFL 250
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
58-248 2.97e-09

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 55.72  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  58 PAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHS-PDMSYEIMSQDLQDLLPQL--GLVPCVVVGHSMG 134
Cdd:COG1647    16 KGVLLLHGFTGSPAEMRPLAEALAKA-GYTVYAPRLPGHGTSPEDlLKTTWEDWLEDVEEAYEILkaGYDKVIVIGLSMG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806 135 GKTAMLLALQRD-------------MAVRQHLLTNLVEVDGRFVWRVNLDALTQHLDKI--LAFPQRQ-----------E 188
Cdd:COG1647    95 GLLALLLAARYPdvaglvllspalkIDDPSAPLLPLLKYLARSLRGIGSDIEDPEVAEYayDRTPLRAlaelqrlirevR 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1887096806 189 SYLG----PTLFLLGGNSQFVHPSHHPEIMRLF--PRAQMQTVPNAGHWIHADRPQDFIA-AIRGFL 248
Cdd:COG1647   175 RDLPkitaPTLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDSGHVITLDKDREEVAeEILDFL 241
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 59-145 8.79e-09

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 54.14  E-value: 8.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  59 AVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSP----HSPdmSYEIMSQDLQDLLPQL----GLVPCVVVG 130
Cdd:pfam12146   6 VVVLVHGLGEHSGRYAHLADALAAQ-GFAVYAYDHRGHGRSDgkrgHVP--SFDDYVDDLDTFVDKIreehPGLPLFLLG 82

                          90
                  ....*....|....*
gi 1887096806 131 HSMGGKTAMLLALQR 145
Cdd:pfam12146  83 HSMGGLIAALYALRY 97
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 60-135 1.21e-07

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 48.67  E-value: 1.21e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887096806  60 VVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVdarNHGDSPHSPDMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGG 135
Cdd:COG1075     8 VVLVHGLGGSAASWAPLAPRLRAA-GYPVYAL---NYPSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSMGG 79
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
48-143 2.45e-06

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 46.79  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  48 YRLLDGEAALPAVVFLHG---LFGSKTNFNSIAKILAQQTGRRVLTVDARnhgdspHSPDMSYEIMSQDLQDLL------ 118
Cdd:COG0657     4 YRPAGAKGPLPVVVYFHGggwVSGSKDTHDPLARRLAARAGAAVVSVDYR------LAPEHPFPAALEDAYAALrwlran 77

                          90       100
                  ....*....|....*....|....*...
gi 1887096806 119 -PQLGLVP--CVVVGHSMGGKTAMLLAL 143
Cdd:COG0657    78 aAELGIDPdrIAVAGDSAGGHLAAALAL 105
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 60-141 1.07e-05

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


Pssm-ID: 369540  Cd Length: 233  Bit Score: 45.05  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  60 VVFLHGLFGSKTNFNSIAKILAQQtgRRVLTVDARNHGDSP---HSPDMSYEIMSQDLQDLLPQLGLV------------ 124
Cdd:pfam07819   7 VLFIPGNAGSYKQVRSIASVAANL--YQVLRKLLQNDNGFHldfFSVDFNEELSAFHGRTLLDQAEYLndairyilslya 84

                          90       100
                  ....*....|....*....|....
gi 1887096806 125 -------PCVVVGHSMGGKTAMLL 141
Cdd:pfam07819  85 sgrpgptSVILIGHSMGGIVARAA 108
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
41-142 1.65e-05

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 45.10  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  41 PRPLPLSYRL-------LDGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVD-----------ARNHGDSPHS 102
Cdd:COG4188    39 DRPLPVDVWYpatapadAPAGGPFPLVVLSHGLGGSREGYAYLAEHLASH-GYVVAAPDhpgsnaadlsaALDGLADALD 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1887096806 103 P--------DMSY-----EIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAMLLA 142
Cdd:COG4188   118 PeelwerplDLSFvldqlLALNKSDPPLAGRLDLDRIGVIGHSLGGYTALALA 170
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 60-150 2.17e-05

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 45.23  E-value: 2.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806   60 VVFLHGLFGSKTNFNSIAKILAQQTgrRVLTVDARNHGDSP---------HSPDMSYEIMSQDLQDLLPQLGLVPCVVVG 130
Cdd:PLN02980  1374 VLFLHGFLGTGEDWIPIMKAISGSA--RCISIDLPGHGGSKiqnhaketqTEPTLSVELVADLLYKLIEHITPGKVTLVG 1451

                           90       100
                   ....*....|....*....|
gi 1887096806  131 HSMGGKTAMLLALQRDMAVR 150
Cdd:PLN02980  1452 YSMGARIALYMALRFSDKIE 1471
PRK10566 PRK10566
esterase; Provisional
 56-139 1.62e-04

esterase; Provisional


Pssm-ID: 182555 [Multi-domain]  Cd Length: 249  Bit Score: 41.90  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  56 ALPAVVFLHGLFGSKTNFNSIAKILAqQTGRRVLTVDARNH-----GDSPHSPDMSYEIMSQDLQDL------LPQLGLV 124
Cdd:PRK10566   26 PLPTVFFYHGFTSSKLVYSYFAVALA-QAGFRVIMPDAPMHgarfsGDEARRLNHFWQILLQNMQEFptlraaIREEGWL 104

                          90
                  ....*....|....*...
gi 1887096806 125 P---CVVVGHSMGGKTAM 139
Cdd:PRK10566  105 LddrLAVGGASMGGMTAL 122
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
45-143 1.96e-04

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 41.79  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  45 PLSYRLLDGEAALPAVVFLHGLFGSKTNF-NSIAKILAQQtGRRVLTVDARNHGDS-PHSP---DMSY-EIMSQD----- 113
Cdd:COG4757    19 PLAARLFPPAGPPRAVVLINPATGVPQRFyRPFARYLAER-GFAVLTYDYRGIGLSrPGSLrgfDAGYrDWGELDlpavl 97

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1887096806 114 --LQDLLPQLglvPCVVVGHSMGGktaMLLAL 143
Cdd:COG4757    98 daLRARFPGL---PLLLVGHSLGG---QLLGL 123
Chlorophyllase pfam07224
Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1. ...
 39-163 2.50e-03

Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1.1.14). Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of ester bond to yield chlorophyllide and phytol.


Pssm-ID: 254111  Cd Length: 307  Bit Score: 38.28  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096806  39 AEPRPLPLSYRLLDGEaaLPAVVFLHGLFGSKTN----FNSIAK----ILAQQTGRRVLTVDARNHGDSPHSpdmSYEIM 110
Cdd:pfam07224  30 PPPKPLIIITPKEAGT--YPVVLFLHGTMLSNEFyslfFNHIAShgfiVVAPQLYRLFPPPSQQDEIDSAAE---VANWL 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887096806 111 SQDLQDLLP---QLGLVPCVVVGHSMGGKTAMLLALQRDMAVRQHLLTNLVEVDGR 163
Cdd:pfam07224 105 PLGLQVVLPtgvEANLSKLALSGHSRGGKTAFALALGYSLDVTFSALIGVDPVAGT 160
 
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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