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Conserved domains on  [gi|6323147|ref|NP_013219|]
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palmitoyl-(protein) hydrolase [Saccharomyces cerevisiae S288C]

Protein Classification

alpha/beta hydrolase( domain architecture ID 10491393)

alpha/beta hydrolase similar to acyl-protein thioesterase that hydrolyzes fatty acids from S-acylated cysteine residues in proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 1-225 3.42e-99

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


:

Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 287.35  E-value: 3.42e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147      1 MNGLRVAAKIQPARQTIIFLHGLGDTGSGWGFlaqylQQRDPAAFQHTNFVFPNAPELHVTANGGALMPAWFDILEWDPS 80
Cdd:pfam02230   1 NGCAEVVSPRDPAQATVIFLHGLGDSGHGWAD-----AAKTEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147     81 FsKVDSDGFMNSLNSIEKTVKQEIDKGIKPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSGFCSIPGILKQHKNGIN 160
Cdd:pfam02230  76 A-KEDEAGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNLVT 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323147    161 VKTPIFHGHGDMDPVVPIGLGIKAKQFYQDSCeiQNYEFKVYKGMAHSTVPDELEDLASFIKKSL 225
Cdd:pfam02230 155 KKTPIFLIHGEEDPVVPLALGKLAKEYLKTSL--NKVELKIYEGLAHSICGREMQDIKKFLSKHI 217
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 1-225 3.42e-99

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 287.35  E-value: 3.42e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147      1 MNGLRVAAKIQPARQTIIFLHGLGDTGSGWGFlaqylQQRDPAAFQHTNFVFPNAPELHVTANGGALMPAWFDILEWDPS 80
Cdd:pfam02230   1 NGCAEVVSPRDPAQATVIFLHGLGDSGHGWAD-----AAKTEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147     81 FsKVDSDGFMNSLNSIEKTVKQEIDKGIKPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSGFCSIPGILKQHKNGIN 160
Cdd:pfam02230  76 A-KEDEAGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNLVT 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323147    161 VKTPIFHGHGDMDPVVPIGLGIKAKQFYQDSCeiQNYEFKVYKGMAHSTVPDELEDLASFIKKSL 225
Cdd:pfam02230 155 KKTPIFLIHGEEDPVVPLALGKLAKEYLKTSL--NKVELKIYEGLAHSICGREMQDIKKFLSKHI 217
YpfH COG0400
Predicted esterase [General function prediction only];
11-226 8.09e-46

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 150.83  E-value: 8.09e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147   11 QPARQTIIFLHGLGDTGSGWGFLAQYLQQRDpaafqhTNFVFPNAPELHVTAnggalMPAWFDILEWDPSFskvDSDGFM 90
Cdd:COG0400   2 GPAAPLVVLLHGYGGDEEDLLPLAPELALPG------AAVLAPRAPVPEGPG-----GRAWFDLSFLEGRE---DEEGLA 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147   91 NSLNSIEKTVKQ-EIDKGIKPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSGFcSIPGILKQHKNGINVKTPIFHGH 169
Cdd:COG0400  68 AAAEALAAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGY-LPGEEALPAPEAALAGTPVFLAH 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6323147  170 GDMDPVVPIGLGIKAKQFYQDsceiQNY--EFKVYKgMAHSTVPDELEDLASFIKKSLS 226
Cdd:COG0400 147 GTQDPVIPVERAREAAEALEA----AGAdvTYREYP-GGHEISPEELADARAWLAERLA 200
PRK11460 PRK11460
putative hydrolase; Provisional
 11-179 2.32e-08

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 52.73  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147    11 QPARQTIIFLHGLGDTGSGWGFLAQYLQQrdpaAFQHTNFVFPNAPElhVTANGGALMpaWFdilewdpSFSKVDSDgfm 90
Cdd:PRK11460  13 KPAQQLLLLFHGVGDNPVAMGEIGSWFAP----AFPDALVVSVGGPE--PSGNGAGRQ--WF-------SVQGITED--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147    91 NSLNSIEKTVKQEID--------KGIKPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSG-FCSIPgilkQHKNGinv 161
Cdd:PRK11460  75 NRQARVAAIMPTFIEtvrywqqqSGVGASATALIGFSQGAIMALEAVKAEPGLAGRVIAFSGrYASLP----ETAPT--- 147

                        170
                 ....*....|....*...
gi 6323147   162 KTPIFHGHGDMDPVVPIG 179
Cdd:PRK11460 148 ATTIHLIHGGEDPVIDVA 165
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 67-132 2.48e-03

Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 37.84  E-value: 2.48e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323147   67 LMPAWFDILEWDPSFSKVDSdGFMNSLNSIEKTVKQEIDKGIK--PE-QIIIGGFSQGAALALATSVTL 132
Cdd:cd00519  82 LDFSPVPLDPPLCSGGKVHS-GFYSAYKSLYNQVLPELKSALKqyPDyKIIVTGHSLGGALASLLALDL 149
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 1-225 3.42e-99

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 287.35  E-value: 3.42e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147      1 MNGLRVAAKIQPARQTIIFLHGLGDTGSGWGFlaqylQQRDPAAFQHTNFVFPNAPELHVTANGGALMPAWFDILEWDPS 80
Cdd:pfam02230   1 NGCAEVVSPRDPAQATVIFLHGLGDSGHGWAD-----AAKTEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147     81 FsKVDSDGFMNSLNSIEKTVKQEIDKGIKPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSGFCSIPGILKQHKNGIN 160
Cdd:pfam02230  76 A-KEDEAGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNLVT 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323147    161 VKTPIFHGHGDMDPVVPIGLGIKAKQFYQDSCeiQNYEFKVYKGMAHSTVPDELEDLASFIKKSL 225
Cdd:pfam02230 155 KKTPIFLIHGEEDPVVPLALGKLAKEYLKTSL--NKVELKIYEGLAHSICGREMQDIKKFLSKHI 217
YpfH COG0400
Predicted esterase [General function prediction only];
11-226 8.09e-46

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 150.83  E-value: 8.09e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147   11 QPARQTIIFLHGLGDTGSGWGFLAQYLQQRDpaafqhTNFVFPNAPELHVTAnggalMPAWFDILEWDPSFskvDSDGFM 90
Cdd:COG0400   2 GPAAPLVVLLHGYGGDEEDLLPLAPELALPG------AAVLAPRAPVPEGPG-----GRAWFDLSFLEGRE---DEEGLA 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147   91 NSLNSIEKTVKQ-EIDKGIKPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSGFcSIPGILKQHKNGINVKTPIFHGH 169
Cdd:COG0400  68 AAAEALAAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGY-LPGEEALPAPEAALAGTPVFLAH 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6323147  170 GDMDPVVPIGLGIKAKQFYQDsceiQNY--EFKVYKgMAHSTVPDELEDLASFIKKSLS 226
Cdd:COG0400 147 GTQDPVIPVERAREAAEALEA----AGAdvTYREYP-GGHEISPEELADARAWLAERLA 200
FSH1 pfam03959
Serine hydrolase (FSH1); This is a family of serine hydrolases.
 17-177 2.51e-09

Serine hydrolase (FSH1); This is a family of serine hydrolases.


Pssm-ID: 461110  Cd Length: 208  Bit Score: 54.98  E-value: 2.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147     17 IIFLHGLGDTGSGW----GFLAQYLQQRDPaafqhtNFVFPNAP-ELHVTANGGALMPAWFDILEWDPSFSKVDSDGFMN 91
Cdd:pfam03959   6 VLCLHGFGQSGEIFraktGALRKLLKKLGV------EFVYLDAPfELAEPADLPGSESEKDEGEDDEPYRAWFFGDDDTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147     92 SLNSIEKTVKqEIDKGIK---PEQIIIGgFSQGAALAlATSVTLPWKIGG--------IVALSGFCSIPGILKQHKNGIN 160
Cdd:pfam03959  80 EYLGLDESLD-YVRDYIKengPFDGILG-FSQGAALA-AILASLLEEGLPlshpplkfAILFSGFRPRPPIYQEYYSEDP 156

                         170
                  ....*....|....*..
gi 6323147    161 VKTPIFHGHGDMDPVVP 177
Cdd:pfam03959 157 IQTPSLHVIGELDTVVP 173
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 4-225 5.30e-09

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 54.92  E-value: 5.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147    4 LRVAAKIQPARQTIIFLHGLGDTGSGWGFLAQYLQQR-------DPAAF-----QHTNFVFPNAPELHvtanggalmpAW 71
Cdd:COG1073  27 LYLPAGASKKYPAVVVAHGNGGVKEQRALYAQRLAELgfnvlafDYRGYgesegEPREEGSPERRDAR----------AA 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147   72 FDILEWDPsfskvdsdgfmnslnsiektvkqeidkGIKPEQIIIGGFSQGAALALATSVTLPwKIGGIVALSGFCSIPGI 151
Cdd:COG1073  97 VDYLRTLP---------------------------GVDPERIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDL 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147  152 LKQHKNGI-------------------------------NVKTPIFHGHGDMDPVVPIGLGIKAkqfYQDSCEiqNYEFK 200
Cdd:COG1073 149 AAQRAKEArgaylpgvpylpnvrlasllndefdplakieKISRPLLFIHGEKDEAVPFYMSEDL---YEAAAE--PKELL 223

                       250       260       270
                ....*....|....*....|....*....|
gi 6323147  201 VYKGMAHSTVPDELED-----LASFIKKSL 225
Cdd:COG1073 224 IVPGAGHVDLYDRPEEeyfdkLAEFFKKNL 253
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
106-225 1.29e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 53.48  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147  106 KGIKPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSGFCSIPGILKQHKNGI------------------------NV 161
Cdd:COG1506  88 PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTerlmggpwedpeayaarsplayadKL 167

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323147  162 KTPIFHGHGDMDPVVPIGlgiKAKQFYQDSCEI-QNYEFKVYKGMAH----STVPDELEDLASFIKKSL 225
Cdd:COG1506 168 KTPLLLIHGEADDRVPPE---QAERLYEALKKAgKPVELLVYPGEGHgfsgAGAPDYLERILDFLDRHL 233
PRK11460 PRK11460
putative hydrolase; Provisional
 11-179 2.32e-08

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 52.73  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147    11 QPARQTIIFLHGLGDTGSGWGFLAQYLQQrdpaAFQHTNFVFPNAPElhVTANGGALMpaWFdilewdpSFSKVDSDgfm 90
Cdd:PRK11460  13 KPAQQLLLLFHGVGDNPVAMGEIGSWFAP----AFPDALVVSVGGPE--PSGNGAGRQ--WF-------SVQGITED--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147    91 NSLNSIEKTVKQEID--------KGIKPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSG-FCSIPgilkQHKNGinv 161
Cdd:PRK11460  75 NRQARVAAIMPTFIEtvrywqqqSGVGASATALIGFSQGAIMALEAVKAEPGLAGRVIAFSGrYASLP----ETAPT--- 147

                        170
                 ....*....|....*...
gi 6323147   162 KTPIFHGHGDMDPVVPIG 179
Cdd:PRK11460 148 ATTIHLIHGGEDPVIDVA 165
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
11-223 5.36e-08

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 51.54  E-value: 5.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147   11 QPARQTIIFLHGLGDTGSGWGFLAQYLQQRDPAAFqhtnfvfpnAPEL--HvtanGGALMPawfdiLEWDPSFSKVDSDg 88
Cdd:COG2267  25 GSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVL---------AFDLrgH----GRSDGP-----RGHVDSFDDYVDD- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147   89 fmnsLNSIEKTVKQEidkgiKPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSGF------CSIP-GILKQ---HKNG 158
Cdd:COG2267  86 ----LRAALDALRAR-----PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAyradplLGPSaRWLRAlrlAEAL 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147  159 INVKTPIFHGHGDMDPVVPIGLgikAKQFYQDSCEiqNYEFKVYKGMAHSTVPDE-----LEDLASFIKK 223
Cdd:COG2267 157 ARIDVPVLVLHGGADRVVPPEA---ARRLAARLSP--DVELVLLPGARHELLNEPareevLAAILAWLER 221
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 17-178 9.16e-08

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 51.54  E-value: 9.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147   17 IIFLHGLG------DTGSGW-------GFLAQYLQQRDPAAFQHTNFVFPNapelHVTANGGalmpawfdilewDPSFsk 83
Cdd:COG3509  56 VVALHGCGgsaadfAAGTGLnaladreGFIVVYPEGTGRAPGRCWNWFDGR----DQRRGRD------------DVAF-- 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147   84 vdsdgfmnsLNSIEKTVKQEIdkGIKPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSGfcSIPGILKQHKNGINVKT 163
Cdd:COG3509 118 ---------IAALVDDLAARY--GIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAG--LPYGAASDAACAPGRPV 184

                       170
                ....*....|....*
gi 6323147  164 PIFHGHGDMDPVVPI 178
Cdd:COG3509 185 PVLVIHGTADPTVPY 199
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 2-224 2.74e-06

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: 46.53  E-value: 2.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147    2 NGLRVAAKIQ-PARQTIIFLHGLGDTGSGWGFLAQYLQQRDPA-AFQHTNFVFPNAPELHVTanggalMPAWFDILEwdp 79
Cdd:COG0596  10 DGVRLHYREAgPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRViAPDLRGHGRSDKPAGGYT------LDDLADDLA--- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147   80 sfskvdsdGFMNSLNsiektvkqeidkgikPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSGF------------CS 147
Cdd:COG0596  81 --------ALLDALG---------------LERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVlaalaeplrrpgLA 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147  148 IPGILKQHKNGI---------NVKTPIFHGHGDMDPVVPIGLGIKAKQfyqdscEIQNYEFKVYKGMAHS---TVPDEL- 214
Cdd:COG0596 138 PEALAALLRALArtdlrerlaRITVPTLVIWGEKDPIVPPALARRLAE------LLPNAELVVLPGAGHFpplEQPEAFa 211

                       250
                ....*....|
gi 6323147  215 EDLASFIKKS 224
Cdd:COG0596 212 AALRDFLARL 221
COG4099 COG4099
Predicted peptidase [General function prediction only];
17-207 4.19e-06

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 46.11  E-value: 4.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147   17 IIFLHGLGDTGSG------WG---FLAQYLQQRDPAAfqhtnFVFPNAPELHvtanggalmpawfdilEWDPSfskVDSD 87
Cdd:COG4099  52 VLFLHGAGERGTDnekqltHGapkFINPENQAKFPAI-----VLAPQCPEDD----------------YWSDT---KALD 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147   88 GFMNSLNSIEKTVKqeIDkgikPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSGFCSiPGILKQHKNginvkTPIFH 167
Cdd:COG4099 108 AVLALLDDLIAEYR--ID----PDRIYLTGLSMGGYGTWDLAARYPDLFAAAVPICGGGD-PANAANLKK-----VPVWI 175

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 6323147  168 GHGDMDPVVPIGLgikAKQFYQdscEIQNY----EFKVYKGMAH 207
Cdd:COG4099 176 FHGAKDDVVPVEE---SRAMVE---ALKAAgadvKYTEYPGVGH 213
DLH pfam01738
Dienelactone hydrolase family;
77-208 2.42e-03

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 37.72  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323147     77 WDPSFSKVDS----DGFMNSLNSIEKtvkqeiDKGIKPEQIIIGGFSQGAALALATSVTLPwKIGGIVALSGfcsiPGIL 152
Cdd:pfam01738  64 MFELVSKRVMekvlDDLEAAVNYLKS------QPEVSPKKVGVVGYCMGGALAVLLAAKGP-LVDAAVGFYG----VGPE 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323147    153 KQHKNGINVKTPIFHGHGDMDPVVPIGL------GIKAKQfyqdsceiQNYEFKVYKGMAHS 208
Cdd:pfam01738 133 PPLIEAPDIKAPILFHFGEEDHFVPADSrelieeALKAAN--------VDHQIHSYPGAGHA 186
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 67-132 2.48e-03

Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 37.84  E-value: 2.48e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323147   67 LMPAWFDILEWDPSFSKVDSdGFMNSLNSIEKTVKQEIDKGIK--PE-QIIIGGFSQGAALALATSVTL 132
Cdd:cd00519  82 LDFSPVPLDPPLCSGGKVHS-GFYSAYKSLYNQVLPELKSALKqyPDyKIIVTGHSLGGALASLLALDL 149
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 11-40 6.62e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 35.19  E-value: 6.62e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 6323147   11 QPARQTIIFLHGLGDTGSGWGFLAQYLQQR 40
Cdd:COG1075   2 AATRYPVVLVHGLGGSAASWAPLAPRLRAA 31
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
107-144 7.54e-03

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 36.39  E-value: 7.54e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 6323147  107 GIKPEQIIIGGFSQGAALALATSVTLP----WKIGGIVALSG 144
Cdd:COG0657  82 GIDPDRIAVAGDSAGGHLAAALALRARdrggPRPAAQVLIYP 123
 
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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