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Conserved domains on  [gi|1879453004|ref|XP_035502224|]
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monoglyceride lipase isoform X2 [Scophthalmus maximus]

Protein Classification

alpha/beta hydrolase( domain architecture ID 12114401)

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

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  12369917|19508187|37582413

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 78-314 1.82e-95

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: 283.34  E-value: 1.82e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  78 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMKSRHPDLPVFI 157
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 158 VGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGT-MDSRWVSRDKTKVEAYDTD 236
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNnLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879453004 237 ELNfHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALHHDL 314
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
 
Name Accession Description Interval E-value
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 78-314 1.82e-95

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: 283.34  E-value: 1.82e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  78 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMKSRHPDLPVFI 157
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 158 VGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGT-MDSRWVSRDKTKVEAYDTD 236
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNnLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879453004 237 ELNfHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALHHDL 314
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PHA02857 PHA02857
monoglyceride lipase; Provisional
 61-329 5.63e-82

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 250.19  E-value: 5.63e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  61 LVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSL 140
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 141 QHIDLMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVqmNPESATPFKVFLAKVLNHLLPSLTLGTMDS 220
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 221 RWVSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApSSDKKL 300
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHA-NCNREI 241

                         250       260
                  ....*....|....*....|....*....
gi 1879453004 301 KVYEGGYHALHHDLPEVAESTLKEVTSWI 329
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWI 270
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
56-331 1.96e-46

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 157.09  E-value: 1.96e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  56 SELRHLVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVY 135
Cdd:COG2267     3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 136 IRDSLQHIDLMKSRhPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFkvflakvlnhllpsltl 215
Cdd:COG2267    83 VDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSA----------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 216 gtmdsRWVsrdktkveaydtdelnfhgglrvsfgmqlmgAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApS 295
Cdd:COG2267   145 -----RWL-------------------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-S 187

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1879453004 296 SDKKLKVYEGGYHALHHDlpEVAESTLKEVTSWITE 331
Cdd:COG2267   188 PDVELVLLPGARHELLNE--PAREEVLAAILAWLER 221
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 111-329 9.12e-09

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: 55.94  E-value: 9.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 111 VFAHDHVGHGQSEG---DRMNIKNFQVYIRDSLQHI--------------------DLMKSRHPDLPVFIVGHSMGGAIS 167
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 168 -----ILTACERPSD---FAGVVLIAPMVQM----NPESATpFKVFLAKVLNHL-------LPSLTLGTMDSRWVSrdkt 228
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnIKGCISLSGMISIksvgSDDSFK-FKYFYLPVMNFMsrvfptfRISKKIRYEKSPYVN---- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 229 kvEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSI--NWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGG 306
Cdd:TIGR01607 232 --DIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309

                         250       260
                  ....*....|....*....|...
gi 1879453004 307 YHALhhDLPEVAESTLKEVTSWI 329
Cdd:TIGR01607 310 DHVI--TIEPGNEEVLKKIIEWI 330
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 138-187 1.17e-04

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: 43.37  E-value: 1.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1879453004 138 DSLQHIDLMKSRHPDL-----PVFIVGHSMGGAISILTACERPSDFAGVVLIAPM 187
Cdd:cd12809   151 NLAEQEALVRAAGCALldiigPAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
 
Name Accession Description Interval E-value
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 78-314 1.82e-95

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: 283.34  E-value: 1.82e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  78 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMKSRHPDLPVFI 157
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 158 VGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGT-MDSRWVSRDKTKVEAYDTD 236
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNnLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879453004 237 ELNfHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALHHDL 314
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PHA02857 PHA02857
monoglyceride lipase; Provisional
 61-329 5.63e-82

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 250.19  E-value: 5.63e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  61 LVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSL 140
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 141 QHIDLMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVqmNPESATPFKVFLAKVLNHLLPSLTLGTMDS 220
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 221 RWVSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApSSDKKL 300
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHA-NCNREI 241

                         250       260
                  ....*....|....*....|....*....
gi 1879453004 301 KVYEGGYHALHHDLPEVAESTLKEVTSWI 329
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWI 270
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
56-331 1.96e-46

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 157.09  E-value: 1.96e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  56 SELRHLVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVY 135
Cdd:COG2267     3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 136 IRDSLQHIDLMKSRhPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFkvflakvlnhllpsltl 215
Cdd:COG2267    83 VDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSA----------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 216 gtmdsRWVsrdktkveaydtdelnfhgglrvsfgmqlmgAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApS 295
Cdd:COG2267   145 -----RWL-------------------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-S 187

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1879453004 296 SDKKLKVYEGGYHALHHDlpEVAESTLKEVTSWITE 331
Cdd:COG2267   188 PDVELVLLPGARHELLNE--PAREEVLAAILAWLER 221
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 62-332 2.53e-46

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 160.69  E-value: 2.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  62 VNADGLHLFCRYWEP-AGPPRALVFIAHGAGEHCGPYDE-IAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDS 139
Cdd:PLN02385   67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 140 LQHIDLMKSR--HPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATP-----FKVFLAKVL--NHLL 210
Cdd:PLN02385  147 IEHYSKIKGNpeFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPplvlqILILLANLLpkAKLV 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 211 PSLTLGTMdsrwVSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMF 290
Cdd:PLN02385  227 PQKDLAEL----AFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSKFLY 302

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1879453004 291 KNAPSSDKKLKVYEGGYHALHHDLPEVAEST-LKEVTSWITEH 332
Cdd:PLN02385  303 EKASSSDKKLKLYEDAYHSILEGEPDEMIFQvLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 66-339 7.72e-37

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 135.29  E-value: 7.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  66 GLHLFCRYWEP--AGPPRALVFIAHGAGEHCG-PYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQH 142
Cdd:PLN02298   42 GLSLFTRSWLPssSSPPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 143 IDLMKSR--HPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKV-----FLAKvlnhLLPslTL 215
Cdd:PLN02298  122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPIpqiltFVAR----FLP--TL 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 216 GTMDSRWVSRDKTKVEAY----DTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFK 291
Cdd:PLN02298  196 AIVPTADLLEKSVKVPAKkiiaKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYE 275

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1879453004 292 NAPSSDKKLKVYEGGYHALHHDLP-EVAESTLKEVTSWITEHLPAKKSP 339
Cdd:PLN02298  276 EAKSEDKTIKIYDGMMHSLLFGEPdENIEIVRRDILSWLNERCTGKATP 324
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 69-333 3.30e-35

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 132.32  E-value: 3.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  69 LFCRYWEP-AGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMK 147
Cdd:PLN02652  123 LFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIR 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 148 SRHPDLPVFIVGHSMGGAIsILTACERPS---DFAGVVLIAPMVQMNPesATPFKVFLAKVLNHLLPSLTLGTMDSRW-- 222
Cdd:PLN02652  203 SENPGVPCFLFGHSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGANKRGip 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 223 VSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKV 302
Cdd:PLN02652  280 VSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRHKDIKL 359

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1879453004 303 YEGGYHALHHDlPEvAESTLKEVTSWITEHL 333
Cdd:PLN02652  360 YDGFLHDLLFE-PE-REEVGRDIIDWMEKRL 388
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
77-332 1.30e-27

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 108.49  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  77 AGPPRALVFIaHGAGehCGPYD--EIAQRLKELSLLVFAHDHVGHGQSEGDrMNIKNFQVYIRDSLQHIDLMKSRHPdlP 154
Cdd:COG1647    12 EGGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--K 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 155 VFIVGHSMGGAISILTACERPsDFAGVVLIAPMVQMNPESAtpfkvFLAKVLNHLlpsltlgtmdSRWVSRDKTKVEAYD 234
Cdd:COG1647    86 VIVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-----PLLPLLKYL----------ARSLRGIGSDIEDPE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 235 TDELNFHGgLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALHHD- 313
Cdd:COG1647   150 VAEYAYDR-TPLRALAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITLDk 228

                         250       260
                  ....*....|....*....|
gi 1879453004 314 -LPEVAEstlkEVTSWITEH 332
Cdd:COG1647   229 dREEVAE----EILDFLERL 244
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 52-333 2.68e-20

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 88.43  E-value: 2.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  52 GVPYSELrHLVNADGLHLFCRYWEPAG--PPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNI 129
Cdd:COG1073     7 KVNKEDV-TFKSRDGIKLAGDLYLPAGasKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 130 KNFQvyIRDSLQHIDLMKSR--HPDLPVFIVGHSMGGAISILTACERPsDFAGVVLIAPMVQMNPESATPFKVFLAKVLN 207
Cdd:COG1073    86 GSPE--RRDARAAVDYLRTLpgVDPERIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGAYLP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 208 H--LLPSLTLgtmdsrwvsrdktkveaydtdelnfhgglrVSFGMQLMGAATRIEReipsINWPFLLLHGDADKLCDIGG 285
Cdd:COG1073   163 GvpYLPNVRL------------------------------ASLLNDEFDPLAKIEK----ISRPLLFIHGEKDEAVPFYM 208

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1879453004 286 SKMMFKNAPsSDKKLKVYEGGYHALHHDLPEvaESTLKEVTSWITEHL 333
Cdd:COG1073   209 SEDLYEAAA-EPKELLIVPGAGHVDLYDRPE--EEYFDKLAEFFKKNL 253
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
63-334 2.95e-20

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 88.15  E-value: 2.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  63 NADGLHLFCRYWEPAGP-PRALVFIAHGAGEHCGP-YDEIAQRLKELSLLVFAHDHVGHGQSEGDRmniknFQVYIRDSL 140
Cdd:COG1506     4 SADGTTLPGWLYLPADGkKYPVVVYVHGGPGSRDDsFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVDDVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 141 QHIDLMKSRhPDLP---VFIVGHSMGGAISILTACERPSDFAGVVLIAPMVqmNPESATPFKVFLAKVLNHLLPSltlgt 217
Cdd:COG1506    79 AAIDYLAAR-PYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS--DLRSYYGTTREYTERLMGGPWE----- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 218 mdsrwvsrdktKVEAYDTdelnfhgglrvsfgMQLMGAATRIEReipsinwPFLLLHGDADKLCDIGGSKMMFKNAPSS- 296
Cdd:COG1506   151 -----------DPEAYAA--------------RSPLAYADKLKT-------PLLLIHGEADDRVPPEQAERLYEALKKAg 198

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1879453004 297 -DKKLKVYEGGYHALhhdLPEVAESTLKEVTSWITEHLP 334
Cdd:COG1506   199 kPVELLVYPGEGHGF---SGAGAPDYLERILDFLDRHLK 234
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 59-332 3.59e-18

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: 81.97  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  59 RHLVNADGLHLFCRYWEPAGPPraLVFIaHGAGEHCGPYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIkNFQVYIRD 138
Cdd:COG0596     4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGY-TLDDLADD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 139 slqHIDLMKSRHPDlPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQmnpesatpfkvFLAKVLNHllpsltlgtm 218
Cdd:COG0596    79 ---LAALLDALGLE-RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA-----------ALAEPLRR---------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 219 dsrwvsrdktkveaYDTDELNFHGGLRVSFGMQLMGAATRIEReipsinwPFLLLHGDADKLCDIGGSKMMFKNAPssDK 298
Cdd:COG0596   134 --------------PGLAPEALAALLRALARTDLRERLARITV-------PTLVIWGEKDPIVPPALARRLAELLP--NA 190

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1879453004 299 KLKVYEGGYHALHHDLPEVaesTLKEVTSWITEH 332
Cdd:COG0596   191 ELVVLPGAGHFPPLEQPEA---FAAALRDFLARL 221
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
60-328 3.48e-11

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 62.29  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  60 HLVNADGLHLFCRYWEPAGP-PRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGD------RMNIKNF 132
Cdd:COG0412     7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearaLMGALDP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 133 QVYIRDSLQHIDLMKSR--HPDLPVFIVGHSMGGAISILTACERPsDFAGVVliapmvqmnpesatpfkvflakvlnhll 210
Cdd:COG0412    87 ELLAADLRAALDWLKAQpeVDAGRVGVVGFCFGGGLALLAAARGP-DLAAAV---------------------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 211 psltlgtmdsrwvsrdktkveaydtdelNFHGGLrvsfgmqlmgAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMF 290
Cdd:COG0412   138 ----------------------------SFYGGL----------PADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALE 179

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1879453004 291 K--NAPSSDKKLKVYEGGYHALHHDL-----PEVAESTLKEVTSW 328
Cdd:COG0412   180 AalAAAGVDVELHVYPGAGHGFTNPGrprydPAAAEDAWQRTLAF 224
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 83-313 1.00e-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: 60.98  E-value: 1.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  83 LVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGdRMNIKNFQVYirDSLQHIDLMKSRHPDLPVFIVGHSM 162
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 163 GGAISILTACERPSDFAGVVLIAPMvqMNPESATPFKVFLAKVL-------------NHLLPSL-----TLGTMDSRWVS 224
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAL--DPPHELDEADRFILALFpgffdgfvadfapNPLGRLVakllaLLLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 225 RDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMfkNAPSSDKKLKVYE 304
Cdd:pfam00561 157 LPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKL--AQLFPNARLVVIP 234


                  ....*....
gi 1879453004 305 GGYHALHHD 313
Cdd:pfam00561 235 DAGHFAFLE 243
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 111-329 9.12e-09

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: 55.94  E-value: 9.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 111 VFAHDHVGHGQSEG---DRMNIKNFQVYIRDSLQHI--------------------DLMKSRHPDLPVFIVGHSMGGAIS 167
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 168 -----ILTACERPSD---FAGVVLIAPMVQM----NPESATpFKVFLAKVLNHL-------LPSLTLGTMDSRWVSrdkt 228
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnIKGCISLSGMISIksvgSDDSFK-FKYFYLPVMNFMsrvfptfRISKKIRYEKSPYVN---- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 229 kvEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSI--NWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGG 306
Cdd:TIGR01607 232 --DIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309

                         250       260
                  ....*....|....*....|...
gi 1879453004 307 YHALhhDLPEVAESTLKEVTSWI 329
Cdd:TIGR01607 310 DHVI--TIEPGNEEVLKKIIEWI 330
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 83-319 3.16e-08

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 53.25  E-value: 3.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  83 LVFIaHGAGEHcgpYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIknfqvyiRDSLQHIDLMKSRHPDLPVFIVGHSM 162
Cdd:pfam12697   1 VVLV-HGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDL-------ADLADLAALLDELGAARPVVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 163 GGAISILTAcerPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGTMDSRWVSRDKTKVEAYDTdelnfhg 242
Cdd:pfam12697  69 GGAVALAAA---AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAA------- 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879453004 243 gLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDaDKLCDIGGSKMMfknAPSSDKKLKVYEGGYHALHHDLPEVAE 319
Cdd:pfam12697 139 -ALARLAALLAALALLPLAAWRDLPVPVLVLAEE-DRLVPELAQRLL---AALAGARLVVLPGAGHLPLDDPEEVAE 210
PRK10749 PRK10749
lysophospholipase L2; Provisional
 97-187 1.14e-07

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 52.69  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  97 YDEIAQRLKELSLLVFAHDHVGHGQS-----EGDRMNIKNFQVYIRDS----LQHIDLMKSRHpdlpVFIVGHSMGGAIS 167
Cdd:PRK10749   70 YAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLaafwQQEIQPGPYRK----RYALAHSMGGAIL 145

                          90       100
                  ....*....|....*....|
gi 1879453004 168 ILTACERPSDFAGVVLIAPM 187
Cdd:PRK10749  146 TLFLQRHPGVFDAIALCAPM 165
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 138-187 1.17e-04

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: 43.37  E-value: 1.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1879453004 138 DSLQHIDLMKSRHPDL-----PVFIVGHSMGGAISILTACERPSDFAGVVLIAPM 187
Cdd:cd12809   151 NLAEQEALVRAAGCALldiigPAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 143-197 1.32e-04

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 43.07  E-value: 1.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 143 IDLMKSRH---PDlPVFIVGHSMGGAISILTACERPSDFAGVVLIA--PMVQMNPESATP 197
Cdd:COG3509   122 VDDLAARYgidPK-RVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACAP 180
Abhydrolase_11 pfam20408
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ...
 80-183 1.40e-04

Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta hydrolase superfamily. Although proteins in this family are uncharacterized they are likely to have an enzymatic activity.


Pssm-ID: 466557 [Multi-domain]  Cd Length: 193  Bit Score: 42.19  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  80 PRALVFIAHGAG---EHcgPY-DEIAQRLKELSLLVFAHD-------HVGHGQSEGDRMNIknFQVYIRDSLQHIdlmks 148
Cdd:pfam20408   1 PKARLLLAHGAGagmDS--PFmQAMAAALAARGIAVVRFNfpymqrrRRTGKRRPPDRAPK--LLEAFRAVIAAL----- 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1879453004 149 RHPDLPVFIVGHSMGGAISILTACErpSDFAGVVL 183
Cdd:pfam20408  72 RGPDLPLFIGGKSMGGRVASLLADD--SGVKGVIA 104
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 138-171 1.86e-04

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: 42.08  E-value: 1.86e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1879453004 138 DSLQHIDLMKSRHPDLPVFIVGHSMGGAISILTA 171
Cdd:cd00519   113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
79-185 2.01e-04

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


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 41.79  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  79 PPRALVFIAHGAGehcGPYD-----EIAQRLKELSLLVFAHDHVG--HGQSEGDRMniknfQVYIRDSLQHIDLMKSRHP 151
Cdd:COG3571     7 DPRATLLLAHGAG---AGMDspfmvALAEALAAAGIAVARFEFPYmvAGRRPPDRA-----PVLDAAWRAVIAALRARLA 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1879453004 152 DLPVFIVGHSMGGAISILTACErPSDFAGVVLIA 185
Cdd:COG3571    79 GLPLVIGGKSMGGRVASMLAAE-GGGAAGLVCLG 111
YpfH COG0400
Predicted esterase [General function prediction only];
77-188 2.21e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 41.82  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  77 AGPPRALVFIAHGAGEHcgPYD--EIAQRLKELSLLVFA------HDHVGHGQSEGDRMNIKNFQVYIRDSLQHID---- 144
Cdd:COG0400     1 GGPAAPLVVLLHGYGGD--EEDllPLAPELALPGAAVLAprapvpEGPGGRAWFDLSFLEGREDEEGLAAAAEALAafid 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1879453004 145 -LMKSRHPDL-PVFIVGHSMGGAISILTACERPSDFAGVVLIAPMV 188
Cdd:COG0400    79 eLEARYGIDPeRIVLAGFSQGAAMALSLALRRPELLAGVVALSGYL 124
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 111-186 2.84e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 42.24  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 111 VFAHDHVGHGQSEGDrmniknfqvYIRDSLQH-----IDLMKSRHPDlPVFIVGHSMGGAISILTACERPSDFAGVVLIA 185
Cdd:PRK14875  160 VIALDLPGHGASSKA---------VGAGSLDElaaavLAFLDALGIE-RAHLVGHSMGGAVALRLAARAPQRVASLTLIA 229


                  .
gi 1879453004 186 P 186
Cdd:PRK14875  230 P 230
COG4099 COG4099
Predicted peptidase [General function prediction only];
142-199 1.05e-03

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 39.95  E-value: 1.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1879453004 142 HIDlmKSRhpdlpVFIVGHSMGGAISILTACERPSDFAGVVLIAPmvQMNPESATPFK 199
Cdd:COG4099   121 RID--PDR-----IYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
Lipase_3 pfam01764
Lipase (class 3);
147-171 1.13e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 38.78  E-value: 1.13e-03
                          10        20
                  ....*....|....*....|....*
gi 1879453004 147 KSRHPDLPVFIVGHSMGGAISILTA 171
Cdd:pfam01764  57 LEKYPDYSIVVTGHSLGGALASLAA 81
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 137-171 1.32e-03

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: 38.64  E-value: 1.32e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1879453004 137 RDSLQHIDLMKSRHPDLPVFIVGHSMGGAISILTA 171
Cdd:cd00741    12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAG 46
PLN02578 PLN02578
hydrolase
 31-194 1.50e-03

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 40.21  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004  31 VSVADPSSMPEPGAAPRR---SPQGVPYSELR----HLVNadglhlfcrywEPAGPPRALVfiaHGAGEHCGPY----DE 99
Cdd:PLN02578   43 VSVMGSSSASQSVQGLERlpfKKEGYNFWTWRghkiHYVV-----------QGEGLPIVLI---HGFGASAFHWryniPE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453004 100 IAQRLKelsllVFAHDHVGHGQSegDRMNIKNFQVYIRDslQHIDLMKSRHPDlPVFIVGHSMGGAISILTACERPSDFA 179
Cdd:PLN02578  109 LAKKYK-----VYALDLLGFGWS--DKALIEYDAMVWRD--QVADFVKEVVKE-PAVLVGNSLGGFTALSTAVGYPELVA 178

                         170
                  ....*....|....*
gi 1879453004 180 GVVLIAPMVQMNPES 194
Cdd:PLN02578  179 GVALLNSAGQFGSES 193
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
157-186 3.68e-03

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 38.43  E-value: 3.68e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1879453004 157 IVGHSMGGAISILTACERPSDFAGVVLIAP 186
Cdd:COG2819   134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
 
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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