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Conserved domains on  [gi|375268702|ref|NP_001243514|]
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monoglyceride lipase isoform 3 [Homo sapiens]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 32-274 1.09e-92

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 PHA02857:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 276  Bit Score: 275.23  E-value: 1.09e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  32 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 111
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 112 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLA--------------------------NPES 165
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNAeavprlnllaaklmgifypnkivgklCPES 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 166 ATTFK--VDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSqDKTLKI 243
Cdd:PHA02857 165 VSRDMdeVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREIKI 243

                        250       260       270
                 ....*....|....*....|....*....|.
gi 375268702 244 YEGAYHVLHKELPEVTNSVFHEINMWVSQRT 274
Cdd:PHA02857 244 YEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 32-274 1.09e-92

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 275.23  E-value: 1.09e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  32 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 111
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 112 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLA--------------------------NPES 165
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNAeavprlnllaaklmgifypnkivgklCPES 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 166 ATTFK--VDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSqDKTLKI 243
Cdd:PHA02857 165 VSRDMdeVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREIKI 243

                        250       260       270
                 ....*....|....*....|....*....|.
gi 375268702 244 YEGAYHVLHKELPEVTNSVFHEINMWVSQRT 274
Cdd:PHA02857 244 YEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 51-255 3.92e-77

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: 234.42  E-value: 3.92e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702   51 PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLG 130
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  131 HSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFK-------------------------------VDIYNSDPL 179
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILkllakllgklfprlrvpnnllpdslsrdpevVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375268702  180 ICRaGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKEL 255
Cdd:pfam12146 163 VHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
31-272 1.30e-54

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 176.35  E-value: 1.30e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  31 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 110
Cdd:COG2267    7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 111 LQHVDSMQKDyPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFkvdiynsdplicraglkvcfg 190
Cdd:COG2267   87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSA--------------------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 191 iQLLNAVsRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAkSQDKTLKIYEGAYHVLHKELPEvtNSVFHEINMWV 270
Cdd:COG2267  145 -RWLRAL-RLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVELVLLPGARHELLNEPAR--EEVLAAILAWL 219


                 ..
gi 375268702 271 SQ 272
Cdd:COG2267  220 ER 221
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 103-144 2.07e-05

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: 44.77  E-value: 2.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 375268702 103 FHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 144
Cdd:cd00519  107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 82-254 1.86e-03

Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in Plasmodium falciparum and Plasmodium yoelii, which are closely related to various phospholipases and lysophospholipases of plants as well as generally being related to the alpha/beta-fold superfamily of hydrolases. These genes are preferentially located in the subtelomeric regions of the chromosomes of both P. falciparum and P. yoelii.


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 39.38  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702   82 VFAHDHVGHGQSEGE---RMVVSDFHVFVRDVLQHVDSMQK-------------DY-------PGLPVFLLGHSMGGAIA 138
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYdivntkeNRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  139 iLTAAERPGH---------------FAGMVLI---------------SPLVLANPESATTFKV-------------DIYN 175
Cdd:TIGR01607 157 -LRLLELLGKsnenndklnikgcisLSGMISIksvgsddsfkfkyfyLPVMNFMSRVFPTFRIskkiryekspyvnDIIK 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  176 SDPLICRAGLKVCFGIQLLNAVSRVE---RALPKlTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLH 252
Cdd:TIGR01607 236 FDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVIT 314


                  ..
gi 375268702  253 KE 254
Cdd:TIGR01607 315 IE 316
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 32-274 1.09e-92

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 275.23  E-value: 1.09e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  32 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 111
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 112 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLA--------------------------NPES 165
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNAeavprlnllaaklmgifypnkivgklCPES 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 166 ATTFK--VDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSqDKTLKI 243
Cdd:PHA02857 165 VSRDMdeVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREIKI 243

                        250       260       270
                 ....*....|....*....|....*....|.
gi 375268702 244 YEGAYHVLHKELPEVTNSVFHEINMWVSQRT 274
Cdd:PHA02857 244 YEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 51-255 3.92e-77

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: 234.42  E-value: 3.92e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702   51 PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLG 130
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  131 HSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFK-------------------------------VDIYNSDPL 179
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILkllakllgklfprlrvpnnllpdslsrdpevVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375268702  180 ICRaGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKEL 255
Cdd:pfam12146 163 VHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
31-272 1.30e-54

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 176.35  E-value: 1.30e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  31 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 110
Cdd:COG2267    7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 111 LQHVDSMQKDyPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFkvdiynsdplicraglkvcfg 190
Cdd:COG2267   87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSA--------------------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 191 iQLLNAVsRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAkSQDKTLKIYEGAYHVLHKELPEvtNSVFHEINMWV 270
Cdd:COG2267  145 -RWLRAL-RLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVELVLLPGARHELLNEPAR--EEVLAAILAWL 219


                 ..
gi 375268702 271 SQ 272
Cdd:COG2267  220 ER 221
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 33-273 2.77e-35

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 129.87  E-value: 2.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  33 VNADGQYLFCRYWKP-TGTPKALIFVSHGAGEHSGRY-EELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 110
Cdd:PLN02385  67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFfEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 111 LQHVDSMQ--KDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPL------------------VLAN--PESATT 168
Cdd:PLN02385 147 IEHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMckiaddvvppplvlqiliLLANllPKAKLV 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 169 FKVDI---------------YNsdpLIC---RAGLKVcfGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLL 230
Cdd:PLN02385 227 PQKDLaelafrdlkkrkmaeYN---VIAykdKPRLRT--AVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSKFL 301

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 375268702 231 MELAKSQDKTLKIYEGAYH-VLHKELPEVTNSVFHEINMWVSQR 273
Cdd:PLN02385 302 YEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 37-281 1.31e-34

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 127.59  E-value: 1.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  37 GQYLFCRYWKPTGT--PKALIFVSHGAG-EHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQH 113
Cdd:PLN02298  42 GLSLFTRSWLPSSSspPRALIFMVHGYGnDISWTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 114 VDSMQKD--YPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANP--------ESATTF-------------- 169
Cdd:PLN02298 122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDkirppwpiPQILTFvarflptlaivpta 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 170 -----------KVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQD 238
Cdd:PLN02298 202 dlleksvkvpaKKIIAKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEAKSED 281

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 375268702 239 KTLKIYEGAYH-VLHKELPEVTNSVFHEINMWVSQRTATAGTAS 281
Cdd:PLN02298 282 KTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKATPS 325
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 35-273 6.22e-33

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 124.24  E-value: 6.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  35 ADGQYLFCRYWKP-TGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQH 113
Cdd:PLN02652 118 ARRNALFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 114 VDSMQKDYPGLPVFLLGHSMGGAIaILTAAERP---GHFAGMVLISPLVLANPES-------------ATTFKVDIYN-- 175
Cdd:PLN02652 198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPsieDKLEGIVLTSPALRVKPAHpivgavapifslvAPRFQFKGANkr 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 176 ---------------SDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKT 240
Cdd:PLN02652 277 gipvsrdpaallakySDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRHKD 356

                        250       260       270
                 ....*....|....*....|....*....|...
gi 375268702 241 LKIYEGAYHVLHKElPEvTNSVFHEINMWVSQR 273
Cdd:PLN02652 357 IKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKR 387
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 30-265 1.45e-25

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: 100.85  E-value: 1.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  30 PHLVNADGQYLFCRYWKPTGTPkaLIFVsHGAGEHSGRYEELARMLMGlDLLVFAHDHVGHGQSEGERMVVSdFHVFVRD 109
Cdd:COG0596    4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYT-LDDLADD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 110 VLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATtfkvdiynsDPLICRAGLkvcf 189
Cdd:COG0596   79 LAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLR---------RPGLAPEAL---- 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375268702 190 gIQLLNAVSR--VERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKsqDKTLKIYEGAYHVLHKELPEVTNSVFHE 265
Cdd:COG0596  142 -AALLRALARtdLRERLARITVPTLVIWGEKDPIVPPALARRLAELLP--NAELVVLPGAGHFPPLEQPEAFAAALRD 216
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
49-262 2.98e-25

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 100.40  E-value: 2.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  49 GTPKALIFVsHG--AGEHSGRYeeLARMLMGLDLLVFAHDHVGHGQSEGErMVVSDFHVFVRDVLQHVDSMQKDYPglPV 126
Cdd:COG1647   13 GGRKGVLLL-HGftGSPAEMRP--LAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 127 FLLGHSMGGAIAILTAAERPgHFAGMVLISPLVLANPESA-----------TTFKVDIYNSDPLICRAGLK---VCFGIQ 192
Cdd:COG1647   87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSApllpllkylarSLRGIGSDIEDPEVAEYAYDrtpLRALAE 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375268702 193 LLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLH--KELPEVTNSV 262
Cdd:COG1647  166 LQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKDREEVAEEI 237
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 23-250 7.46e-22

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 91.51  E-value: 7.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  23 SIPYQDLpHLVNADGQYLFCRYWKPTGTPKAL--IFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGE-RMV 99
Cdd:COG1073    7 KVNKEDV-TFKSRDGIKLAGDLYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEpREE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 100 VS----DFHVFVRDVLQhvdsmQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLISP---LVLANPESATTFKVD 172
Cdd:COG1073   86 GSperrDARAAVDYLRT-----LPGVDPERIGLLGISLGGGYALNAAATDPR-VKAVILDSPftsLEDLAAQRAKEARGA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375268702 173 IYNSDPLICRAGLKvcfgiQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAkSQDKTLKIYEGAYHV 250
Cdd:COG1073  160 YLPGVPYLPNVRLA-----SLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAA-AEPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
34-254 7.33e-21

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 88.54  E-value: 7.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  34 NADGQYLFCRYWKPTGTPKA-LIFVSHGAGEH-SGRYEELARMLMGLDLLVFAHDHVGHGQSEGERmvvsdFHVFVRDVL 111
Cdd:COG1506    4 SADGTTLPGWLYLPADGKKYpVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVDDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 112 QHVDSM--QKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLV-LANPESATTFKVDIYNSDPLICRAGLKvc 188
Cdd:COG1506   79 AAIDYLaaRPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSdLRSYYGTTREYTERLMGGPWEDPEAYA-- 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375268702 189 fgiqllnAVSRVERAlPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQ--DKTLKIYEGAYHVLHKE 254
Cdd:COG1506  157 -------ARSPLAYA-DKLKTPLLLIHGEADDRVPPEQAERLYEALKKAgkPVELLVYPGEGHGFSGA 216
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 52-158 4.57e-10

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: 58.67  E-value: 4.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702   52 KALIFVsHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGeRMVVSDFHV--FVRDVLQHVDSMQKDypglPVFLL 129
Cdd:pfam00561   1 PPVLLL-HGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTddLAEDLEYILEALGLE----KVNLV 74

                          90       100
                  ....*....|....*....|....*....
gi 375268702  130 GHSMGGAIAILTAAERPGHFAGMVLISPL 158
Cdd:pfam00561  75 GHSMGGLIALAYAAKYPDRVKALVLLGAL 103
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
31-252 2.41e-09

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 56.13  E-value: 2.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  31 HLVNADGQYLFCRYWKPTGT-PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFA---HDHVGHGQSEGE---RMVVSDF 103
Cdd:COG0412    7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 104 HVFVRDVLQHVD--SMQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLISPLVLANPESAttfkvdiynsdplic 181
Cdd:COG0412   87 ELLAADLRAALDwlKAQPEVDAGRVGVVGFCFGGGLALLAAARGPD-LAAAVSFYGGLPADDLLD--------------- 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375268702 182 raglkvcfgiqllnavsrverALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQ--DKTLKIYEGAYHVLH 252
Cdd:COG0412  151 ---------------------LAARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAgvDVELHVYPGAGHGFT 202
YpfH COG0400
Predicted esterase [General function prediction only];
48-164 1.92e-08

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 53.37  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  48 TGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFA------HDHVGHG----QSEGERMVVSDFHVFVRDVLQHVDSM 117
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 375268702 118 QKDYpGLP---VFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPE 164
Cdd:COG0400   81 EARY-GIDperIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEA 129
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
47-249 8.71e-08

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 52.42  E-value: 8.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  47 PTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGH--GQSEGERMVVSDFHVF---------VRDVLQHVD 115
Cdd:COG4188   57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaADLSAALDGLADALDPeelwerpldLSFVLDQLL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 116 SMQKDYPGLP-------VFLLGHSMGGAIAILTAAERP------GHFAGMVLISPLVLANPESATTFKvdiynsDPLIcR 182
Cdd:COG4188  137 ALNKSDPPLAgrldldrIGVIGHSLGGYTALALAGARLdfaalrQYCGKNPDLQCRALDLPRLAYDLR------DPRI-K 209

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375268702 183 AGLkvcfgiqLLNAVSR---VERALPKLTVPFLLLQGSADRlcDSKGAY---LLMELAKSQDKTLKIYEGAYH 249
Cdd:COG4188  210 AVV-------ALAPGGSglfGEEGLAAITIPVLLVAGSADD--VTPAPDeqiRPFDLLPGADKYLLTLEGATH 273
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 43-157 2.96e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 51.10  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  43 RYWK-PTGTPKALIFVsHG-AGEHS---GRYEELARmlmglDLLVFAHDHVGHGQSeGERMVVSDFHVFVRDVLQHVDSM 117
Cdd:PRK14875 122 RYLRlGEGDGTPVVLI-HGfGGDLNnwlFNHAALAA-----GRPVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAL 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 375268702 118 QKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISP 157
Cdd:PRK14875 195 GIE----RAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
PRK10749 PRK10749
lysophospholipase L2; Provisional
 67-266 2.88e-06

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 47.69  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  67 RYEELARMLMGLDLLVFAHDHVGHGQS-----EGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILT 141
Cdd:PRK10749  69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLF 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 142 AAERPGHFAGMVLISPL---VLANPESATTFKVDIYNSDPLIcRAGLKVC--------FGIQLL-NAVSRVERAL----- 204
Cdd:PRK10749 149 LQRHPGVFDAIALCAPMfgiVLPLPSWMARRILNWAEGHPRI-RDGYAIGtgrwrplpFAINVLtHSRERYRRNLrfyad 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 205 ----------------------------PKLTVPFLLLQGSADRLCDSkgayllmelaKSQDKTLKIYEGAYHVLHKELP 256
Cdd:PRK10749 228 dpelrvggptyhwvresilageqvlagaGDITTPLLLLQAEEERVVDN----------RMHDRFCEARTAAGHPCEGGKP 297

                        250
                 ....*....|
gi 375268702 257 EVTNSVFHEI 266
Cdd:PRK10749 298 LVIKGAYHEI 307
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 54-170 4.32e-06

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 46.70  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702   54 LIFVsHGAGEHSGRYEELARmlmgLDLLVFAHDHVGHGQSEGERMVVSDfhvfVRDVLQHVDSMQKDYPglpVFLLGHSM 133
Cdd:pfam12697   1 VVLV-HGAGLSAAPLAALLA----AGVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 375268702  134 GGAIAILTAAerpGHFAGMVLISPLVLANPESATTFK 170
Cdd:pfam12697  69 GGAVALAAAA---AALVVGVLVAPLAAPPGLLAALLA 102
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
109-223 5.71e-06

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 46.03  E-value: 5.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702 109 DVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLIS-PLVLAN-PESattfkvdiynsdplicraglk 186
Cdd:COG3571   65 AWRAVIAALRARLAGLPLVIGGKSMGGRVASMLAAEGGG-AAGLVCLGyPFHPPGkPEK--------------------- 122

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 375268702 187 vcfgiqllnavSRVERaLPKLTVPFLLLQGSADRLCD 223
Cdd:COG3571  123 -----------LRTEH-LADLTVPTLIVQGERDPFGT 147
COG4099 COG4099
Predicted peptidase [General function prediction only];
107-170 1.20e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 45.34  E-value: 1.20e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375268702 107 VRDVLQHVDSMQKDYPGLP--VFLLGHSMGGAIAILTAAERPGHFAGMVLISPlvLANPESATTFK 170
Cdd:COG4099  106 LDAVLALLDDLIAEYRIDPdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 103-144 2.07e-05

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: 44.77  E-value: 2.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 375268702 103 FHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 144
Cdd:cd00519  107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 125-158 2.25e-05

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214008  Cd Length: 280  Bit Score: 44.91  E-value: 2.25e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 375268702 125 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISPL 158
Cdd:cd12809  172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 49-167 3.10e-05

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 44.61  E-value: 3.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  49 GTPKALIFVSHGAG------EHSGRYEELARmlmGLDLLV----------------FAHDHVGHGQSEgermvvsdfHVF 106
Cdd:COG3509   50 GAPLPLVVALHGCGgsaadfAAGTGLNALAD---REGFIVvypegtgrapgrcwnwFDGRDQRRGRDD---------VAF 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375268702 107 VRDVlqhVDSMQKDYPGLP--VFLLGHSMGGAIAILTAAERPGHFAGMVLIS--PLVLANPESAT 167
Cdd:COG3509  118 IAAL---VDDLAARYGIDPkrVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACA 179
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 108-144 1.01e-04

Lipase. 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: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 41.72  E-value: 1.01e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 375268702 108 RDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 144
Cdd:cd00741   12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
106-157 5.56e-04

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 40.35  E-value: 5.56e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 375268702 106 FVRDVLQ-HVDsmqKDYPGLPVF--LLGHSMGGAIAILTAAERPGHFAGMVLISP 157
Cdd:COG2819  112 FLEEELKpYID---KRYRTDPERtgLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 47-157 1.08e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 37.89  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  47 PTGTPKALIFVsHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERmvvsdfhvfVRDVLQHVDSMQKDYPGLPV 126
Cdd:COG1075    1 YAATRYPVVLV-HGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDS---------AEQLAAFVDAVLAATGAEKV 70

                         90       100       110
                 ....*....|....*....|....*....|...
gi 375268702 127 FLLGHSMGGAIA--ILTAAERPGHFAGMVLISP 157
Cdd:COG1075   71 DLVGHSMGGLVAryYLKRLGGAAKVARVVTLGT 103
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 82-254 1.86e-03

Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in Plasmodium falciparum and Plasmodium yoelii, which are closely related to various phospholipases and lysophospholipases of plants as well as generally being related to the alpha/beta-fold superfamily of hydrolases. These genes are preferentially located in the subtelomeric regions of the chromosomes of both P. falciparum and P. yoelii.


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 39.38  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702   82 VFAHDHVGHGQSEGE---RMVVSDFHVFVRDVLQHVDSMQK-------------DY-------PGLPVFLLGHSMGGAIA 138
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYdivntkeNRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  139 iLTAAERPGH---------------FAGMVLI---------------SPLVLANPESATTFKV-------------DIYN 175
Cdd:TIGR01607 157 -LRLLELLGKsnenndklnikgcisLSGMISIksvgsddsfkfkyfyLPVMNFMSRVFPTFRIskkiryekspyvnDIIK 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  176 SDPLICRAGLKVCFGIQLLNAVSRVE---RALPKlTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLH 252
Cdd:TIGR01607 236 FDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVIT 314


                  ..
gi 375268702  253 KE 254
Cdd:TIGR01607 315 IE 316
PLN02578 PLN02578
hydrolase
 49-157 2.19e-03

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 39.05  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  49 GTPKALIfvsHGAGEHS--GRYE--ELARMLMgldllVFAHDHVGHGQS-----EGERMVVSDFHV-FVRDVLQHvdsmq 118
Cdd:PLN02578  86 GLPIVLI---HGFGASAfhWRYNipELAKKYK-----VYALDLLGFGWSdkaliEYDAMVWRDQVAdFVKEVVKE----- 152

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 375268702 119 kdypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISP 157
Cdd:PLN02578 153 ------PAVLVGNSLGGFTALSTAVGYPELVAGVALLNS 185
Lipase_3 pfam01764
Lipase (class 3);
121-169 2.69e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 37.24  E-value: 2.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 375268702  121 YPGLPVFLLGHSMGGAIAILTAAerpghfagMVLISPLVLANPESATTF 169
Cdd:pfam01764  60 YPDYSIVVTGHSLGGALASLAAL--------DLVENGLRLSSRVTVVTF 100
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 61-175 3.02e-03

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: 38.11  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702   61 AGEHSGRYEELARMLM---GLDLLVFAHDHVG-----HGQSegermvVSDFHVFVRDVLQHVDSMQKDYPGLP--VFLLG 130
Cdd:pfam07819  24 ASVAANLYQVLRKLLQndnGFHLDFFSVDFNEelsafHGRT------LLDQAEYLNDAIRYILSLYASGRPGPtsVILIG 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 375268702  131 HSMGGAIAiLTAAERPGHFAGMV-LIspLVLANPESAT--TFKVDIYN 175
Cdd:pfam07819  98 HSMGGIVA-RAALTLPNYIPQSVnTI--ITLSSPHAKPplTFDGDILK 142
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
15-161 3.06e-03

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 38.59  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  15 SSPRRTPQsIPYQ----DLPhlvnaDGQYLFCRYWKPTGTPKALIFVSHG-AGEHSGRY-EELARMLMGLDLLVFAHDHV 88
Cdd:COG0429   26 SLFRRRPA-LPYRrerlELP-----DGDFVDLDWSDPPAPSKPLVVLLHGlEGSSDSHYaRGLARALYARGWDVVRLNFR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  89 GHGQSE---------GErmvVSDfhvfVRDVLQHVdsmQKDYPGLPVFLLGHSMGGAIAILTAAERPGH---FAGMVLIS 156
Cdd:COG0429  100 GCGGEPnllprlyhsGD---TED----LVWVLAHL---RARYPYAPLYAVGFSLGGNLLLKYLGEQGDDappLKAAVAVS 169


                 ....*.
gi 375268702 157 -PLVLA 161
Cdd:COG0429  170 pPLDLA 175
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
83-144 4.13e-03

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 37.81  E-value: 4.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375268702  83 FAHDHVGHGQSEGerMVVSDFHVFVRDVLQHVDSM-QKDYPGLPVFLLGHSMGGAIAILTAAE 144
Cdd:COG3675   48 AAQVPYPFAKTGG--KVHRGFYRALQSLRELLEDAlRPLSPGKRLYVTGHSLGGALATLAAAD 108
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 47-144 4.25e-03

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 37.91  E-value: 4.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375268702  47 PTGTPKALIFVSHGAGEHSGRYEELARmLMGLDLLVFAHDHVGHGQSEGERMVvSDFHVFVRDVLQHVdsmqKDYPGLPV 126
Cdd:COG3208    1 PRPDARLRLFCFPYAGGSASAYRPWAA-ALPPDIEVLAVQLPGRGDRLGEPPL-TSLEELADDLAEEL----APLLDRPF 74

                         90
                 ....*....|....*...
gi 375268702 127 FLLGHSMGGAIAILTAAE 144
Cdd:COG3208   75 ALFGHSMGALLAFELARR 92
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 128-159 4.75e-03

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 37.83  E-value: 4.75e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 375268702  128 LLGHSMGGAIAILTAAERPGHFAGMVLISPLV 159
Cdd:pfam00756 114 LAGQSMGGLGALYLALKYPDLFGSVSSFSPIL 145
PRK10673 PRK10673
esterase;
90-155 5.72e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 37.40  E-value: 5.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375268702  90 HGQSEgeRMVVSDFHVFVRDVLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLI 155
Cdd:PRK10673  53 HGLSP--RDPVMNYPAMAQDLLDTLDALQIE----KATFIGHSMGGKAVMALTALAPDRIDKLVAI 112
 
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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