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Conserved domains on  [gi|1879453010|ref|XP_035502227|]
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monoglyceride lipase isoform X3 [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 ...
 76-312 2.09e-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: 282.95  E-value: 2.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  76 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMKSRHPDLPVFI 155
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 156 VGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGT-MDSRWVSRDKTKVEAYDTD 234
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNnLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879453010 235 ELNfHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALHHDL 312
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 ...
 76-312 2.09e-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: 282.95  E-value: 2.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  76 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMKSRHPDLPVFI 155
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 156 VGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGT-MDSRWVSRDKTKVEAYDTD 234
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNnLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879453010 235 ELNfHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALHHDL 312
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PHA02857 PHA02857
monoglyceride lipase; Provisional
 59-327 4.06e-82

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 250.57  E-value: 4.06e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  59 LVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSL 138
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 139 QHIDLMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVqmNPESATPFKVFLAKVLNHLLPSLTLGTMDS 218
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 219 RWVSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApSSDKKL 298
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHA-NCNREI 241

                         250       260
                  ....*....|....*....|....*....
gi 1879453010 299 KVYEGGYHALHHDLPEVAESTLKEVTSWI 327
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWI 270
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
54-329 8.52e-47

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 157.86  E-value: 8.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  54 SELRHLVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVY 133
Cdd:COG2267     3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 134 IRDSLQHIDLMKSRhPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFkvflakvlnhllpsltl 213
Cdd:COG2267    83 VDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSA----------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 214 gtmdsRWVsrdktkveaydtdelnfhgglrvsfgmqlmgAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApS 293
Cdd:COG2267   145 -----RWL-------------------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-S 187

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1879453010 294 SDKKLKVYEGGYHALHHDlpEVAESTLKEVTSWITE 329
Cdd:COG2267   188 PDVELVLLPGARHELLNE--PAREEVLAAILAWLER 221
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 109-327 9.00e-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: 9.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 109 VFAHDHVGHGQSEG---DRMNIKNFQVYIRDSLQHI--------------------DLMKSRHPDLPVFIVGHSMGGAIS 165
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 166 -----ILTACERPSD---FAGVVLIAPMVQM----NPESATpFKVFLAKVLNHL-------LPSLTLGTMDSRWVSrdkt 226
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnIKGCISLSGMISIksvgSDDSFK-FKYFYLPVMNFMsrvfptfRISKKIRYEKSPYVN---- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 227 kvEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSI--NWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGG 304
Cdd:TIGR01607 232 --DIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309

                         250       260
                  ....*....|....*....|...
gi 1879453010 305 YHALhhDLPEVAESTLKEVTSWI 327
Cdd:TIGR01607 310 DHVI--TIEPGNEEVLKKIIEWI 330
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 136-185 1.42e-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: 42.98  E-value: 1.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1879453010 136 DSLQHIDLMKSRHPDL-----PVFIVGHSMGGAISILTACERPSDFAGVVLIAPM 185
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 ...
 76-312 2.09e-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: 282.95  E-value: 2.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  76 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMKSRHPDLPVFI 155
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 156 VGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGT-MDSRWVSRDKTKVEAYDTD 234
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNnLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879453010 235 ELNfHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALHHDL 312
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PHA02857 PHA02857
monoglyceride lipase; Provisional
 59-327 4.06e-82

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 250.57  E-value: 4.06e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  59 LVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSL 138
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 139 QHIDLMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVqmNPESATPFKVFLAKVLNHLLPSLTLGTMDS 218
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 219 RWVSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApSSDKKL 298
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHA-NCNREI 241

                         250       260
                  ....*....|....*....|....*....
gi 1879453010 299 KVYEGGYHALHHDLPEVAESTLKEVTSWI 327
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWI 270
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
54-329 8.52e-47

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 157.86  E-value: 8.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  54 SELRHLVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVY 133
Cdd:COG2267     3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 134 IRDSLQHIDLMKSRhPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFkvflakvlnhllpsltl 213
Cdd:COG2267    83 VDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSA----------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 214 gtmdsRWVsrdktkveaydtdelnfhgglrvsfgmqlmgAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApS 293
Cdd:COG2267   145 -----RWL-------------------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-S 187

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1879453010 294 SDKKLKVYEGGYHALHHDlpEVAESTLKEVTSWITE 329
Cdd:COG2267   188 PDVELVLLPGARHELLNE--PAREEVLAAILAWLER 221
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 60-330 4.87e-46

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 159.92  E-value: 4.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  60 VNADGLHLFCRYWEP-AGPPRALVFIAHGAGEHCGPYDE-IAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDS 137
Cdd:PLN02385   67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 138 LQHIDLMKSR--HPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATP-----FKVFLAKVL--NHLL 208
Cdd:PLN02385  147 IEHYSKIKGNpeFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPplvlqILILLANLLpkAKLV 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 209 PSLTLGTMdsrwVSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMF 288
Cdd:PLN02385  227 PQKDLAEL----AFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSKFLY 302

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1879453010 289 KNAPSSDKKLKVYEGGYHALHHDLPEVAEST-LKEVTSWITEH 330
Cdd:PLN02385  303 EKASSSDKKLKLYEDAYHSILEGEPDEMIFQvLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 64-337 2.68e-36

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 133.75  E-value: 2.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  64 GLHLFCRYWEP--AGPPRALVFIAHGAGEHCG-PYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQH 140
Cdd:PLN02298   42 GLSLFTRSWLPssSSPPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 141 IDLMKSR--HPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKV-----FLAKvlnhLLPslTL 213
Cdd:PLN02298  122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPIpqiltFVAR----FLP--TL 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 214 GTMDSRWVSRDKTKVEAY----DTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFK 289
Cdd:PLN02298  196 AIVPTADLLEKSVKVPAKkiiaKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYE 275

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1879453010 290 NAPSSDKKLKVYEGGYHALHHDLP-EVAESTLKEVTSWITEHLPAKKSP 337
Cdd:PLN02298  276 EAKSEDKTIKIYDGMMHSLLFGEPdENIEIVRRDILSWLNERCTGKATP 324
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 1-331 4.51e-35

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 131.94  E-value: 4.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010   1 MSPGSLTVGSSPPGHCeVRARRRSCGSP--------RALKDPSSMPEPGAAPRRSPQGVPyselrhlvNADGLHLFCRYW 72
Cdd:PLN02652   58 VSPLSSPEAGAVPAPS-RRWRRRMAWKLeeedtrrrRALAEGVEMVEDGEGTRWATSLFY--------GARRNALFCRSW 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  73 EP-AGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMKSRHPDL 151
Cdd:PLN02652  129 APaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIRSENPGV 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 152 PVFIVGHSMGGAIsILTACERPS---DFAGVVLIAPMVQMNPesATPFKVFLAKVLNHLLPSLTLGTMDSRW--VSRDKT 226
Cdd:PLN02652  209 PCFLFGHSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGANKRGipVSRDPA 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 227 KVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYH 306
Cdd:PLN02652  286 ALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRHKDIKLYDGFLH 365

                         330       340
                  ....*....|....*....|....*
gi 1879453010 307 ALHHDlPEvAESTLKEVTSWITEHL 331
Cdd:PLN02652  366 DLLFE-PE-REEVGRDIIDWMEKRL 388
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
75-330 7.49e-28

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 108.88  E-value: 7.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  75 AGPPRALVFIaHGAGehCGPYD--EIAQRLKELSLLVFAHDHVGHGQSEGDrMNIKNFQVYIRDSLQHIDLMKSRHPdlP 152
Cdd:COG1647    12 EGGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--K 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 153 VFIVGHSMGGAISILTACERPsDFAGVVLIAPMVQMNPESAtpfkvFLAKVLNHLlpsltlgtmdSRWVSRDKTKVEAYD 232
Cdd:COG1647    86 VIVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-----PLLPLLKYL----------ARSLRGIGSDIEDPE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 233 TDELNFHGgLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALH--H 310
Cdd:COG1647   150 VAEYAYDR-TPLRALAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldK 228

                         250       260
                  ....*....|....*....|
gi 1879453010 311 DLPEVAEstlkEVTSWITEH 330
Cdd:COG1647   229 DREEVAE----EILDFLERL 244
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 50-331 1.78e-20

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 89.20  E-value: 1.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  50 GVPYSELrHLVNADGLHLFCRYWEPAG--PPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNI 127
Cdd:COG1073     7 KVNKEDV-TFKSRDGIKLAGDLYLPAGasKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 128 KNFQvyIRDSLQHIDLMKSR--HPDLPVFIVGHSMGGAISILTACERPsDFAGVVLIAPMVQMNPESATPFKVFLAKVLN 205
Cdd:COG1073    86 GSPE--RRDARAAVDYLRTLpgVDPERIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGAYLP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 206 H--LLPSLTLgtmdsrwvsrdktkveaydtdelnfhgglrVSFGMQLMGAATRIEReipsINWPFLLLHGDADKLCDIGG 283
Cdd:COG1073   163 GvpYLPNVRL------------------------------ASLLNDEFDPLAKIEK----ISRPLLFIHGEKDEAVPFYM 208

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1879453010 284 SKMMFKNAPsSDKKLKVYEGGYHALHHDLPEvaESTLKEVTSWITEHL 331
Cdd:COG1073   209 SEDLYEAAA-EPKELLIVPGAGHVDLYDRPE--EEYFDKLAEFFKKNL 253
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
61-332 2.47e-20

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 88.15  E-value: 2.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  61 NADGLHLFCRYWEPAGP-PRALVFIAHGAGEHCGP-YDEIAQRLKELSLLVFAHDHVGHGQSEGDRmniknFQVYIRDSL 138
Cdd:COG1506     4 SADGTTLPGWLYLPADGkKYPVVVYVHGGPGSRDDsFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVDDVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 139 QHIDLMKSRhPDLP---VFIVGHSMGGAISILTACERPSDFAGVVLIAPMVqmNPESATPFKVFLAKVLNHLLPSltlgt 215
Cdd:COG1506    79 AAIDYLAAR-PYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS--DLRSYYGTTREYTERLMGGPWE----- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 216 mdsrwvsrdktKVEAYDTdelnfhgglrvsfgMQLMGAATRIEReipsinwPFLLLHGDADKLCDIGGSKMMFKNAPSS- 294
Cdd:COG1506   151 -----------DPEAYAA--------------RSPLAYADKLKT-------PLLLIHGEADDRVPPEQAERLYEALKKAg 198

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1879453010 295 -DKKLKVYEGGYHALhhdLPEVAESTLKEVTSWITEHLP 332
Cdd:COG1506   199 kPVELLVYPGEGHGF---SGAGAPDYLERILDFLDRHLK 234
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 57-330 1.73e-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: 82.74  E-value: 1.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  57 RHLVNADGLHLFCRYWEPAGPPraLVFIaHGAGEHCGPYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIkNFQVYIRD 136
Cdd:COG0596     4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGY-TLDDLADD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 137 slqHIDLMKSRHPDlPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQmnpesatpfkvFLAKVLNHllpsltlgtm 216
Cdd:COG0596    79 ---LAALLDALGLE-RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA-----------ALAEPLRR---------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 217 dsrwvsrdktkveaYDTDELNFHGGLRVSFGMQLMGAATRIEReipsinwPFLLLHGDADKLCDIGGSKMMFKNAPssDK 296
Cdd:COG0596   134 --------------PGLAPEALAALLRALARTDLRERLARITV-------PTLVIWGEKDPIVPPALARRLAELLP--NA 190

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1879453010 297 KLKVYEGGYHALHHDLPEVaesTLKEVTSWITEH 330
Cdd:COG0596   191 ELVVLPGAGHFPPLEQPEA---FAAALRDFLARL 221
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
58-326 1.35e-11

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 63.45  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  58 HLVNADGLHLFCRYWEPAGP-PRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGD------RMNIKNF 130
Cdd:COG0412     7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearaLMGALDP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 131 QVYIRDSLQHIDLMKSrHPDL---PVFIVGHSMGGAISILTACERPsDFAGVVliapmvqmnpesatpfkvflakvlnhl 207
Cdd:COG0412    87 ELLAADLRAALDWLKA-QPEVdagRVGVVGFCFGGGLALLAAARGP-DLAAAV--------------------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 208 lpsltlgtmdsrwvsrdktkveaydtdelNFHGGLrvsfgmqlmgAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMM 287
Cdd:COG0412   138 -----------------------------SFYGGL----------PADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAAL 178

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1879453010 288 FK--NAPSSDKKLKVYEGGYHALHHDL-----PEVAESTLKEVTSW 326
Cdd:COG0412   179 EAalAAAGVDVELHVYPGAGHGFTNPGrprydPAAAEDAWQRTLAF 224
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 81-311 8.41e-11

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: 61.37  E-value: 8.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  81 LVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGdRMNIKNFQVYirDSLQHIDLMKSRHPDLPVFIVGHSM 160
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 161 GGAISILTACERPSDFAGVVLIAPMvqMNPESATPFKVFLAKVL-------------NHLLPSL-----TLGTMDSRWVS 222
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAL--DPPHELDEADRFILALFpgffdgfvadfapNPLGRLVakllaLLLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 223 RDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMfkNAPSSDKKLKVYE 302
Cdd:pfam00561 157 LPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKL--AQLFPNARLVVIP 234


                  ....*....
gi 1879453010 303 GGYHALHHD 311
Cdd:pfam00561 235 DAGHFAFLE 243
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 109-327 9.00e-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: 9.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 109 VFAHDHVGHGQSEG---DRMNIKNFQVYIRDSLQHI--------------------DLMKSRHPDLPVFIVGHSMGGAIS 165
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 166 -----ILTACERPSD---FAGVVLIAPMVQM----NPESATpFKVFLAKVLNHL-------LPSLTLGTMDSRWVSrdkt 226
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnIKGCISLSGMISIksvgSDDSFK-FKYFYLPVMNFMsrvfptfRISKKIRYEKSPYVN---- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 227 kvEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSI--NWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGG 304
Cdd:TIGR01607 232 --DIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309

                         250       260
                  ....*....|....*....|...
gi 1879453010 305 YHALhhDLPEVAESTLKEVTSWI 327
Cdd:TIGR01607 310 DHVI--TIEPGNEEVLKKIIEWI 330
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 81-317 1.37e-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: 54.40  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  81 LVFIaHGAGEHcgpYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIknfqvyiRDSLQHIDLMKSRHPDLPVFIVGHSM 160
Cdd:pfam12697   1 VVLV-HGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDL-------ADLADLAALLDELGAARPVVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 161 GGAISILTAcerPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGTMDSRWVSRDKTKVEAYDTdelnfhg 240
Cdd:pfam12697  69 GGAVALAAA---AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAA------- 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879453010 241 gLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDaDKLCDIGGSKMMfknAPSSDKKLKVYEGGYHALHHDLPEVAE 317
Cdd:pfam12697 139 -ALARLAALLAALALLPLAAWRDLPVPVLVLAEE-DRLVPELAQRLL---AALAGARLVVLPGAGHLPLDDPEEVAE 210
PRK10749 PRK10749
lysophospholipase L2; Provisional
 95-185 1.63e-07

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 52.31  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  95 YDEIAQRLKELSLLVFAHDHVGHGQS-----EGDRMNIKNFQVYIRDS----LQHIDLMKSRHpdlpVFIVGHSMGGAIS 165
Cdd:PRK10749   70 YAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLaafwQQEIQPGPYRK----RYALAHSMGGAIL 145

                          90       100
                  ....*....|....*....|
gi 1879453010 166 ILTACERPSDFAGVVLIAPM 185
Cdd:PRK10749  146 TLFLQRHPGVFDAIALCAPM 165
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 141-195 1.22e-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: 1.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 141 IDLMKSRH---PDlPVFIVGHSMGGAISILTACERPSDFAGVVLIA--PMVQMNPESATP 195
Cdd:COG3509   122 VDDLAARYgidPK-RVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACAP 180
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 136-185 1.42e-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: 42.98  E-value: 1.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1879453010 136 DSLQHIDLMKSRHPDL-----PVFIVGHSMGGAISILTACERPSDFAGVVLIAPM 185
Cdd:cd12809   151 NLAEQEALVRAAGCALldiigPAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 136-169 1.42e-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: 42.46  E-value: 1.42e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1879453010 136 DSLQHIDLMKSRHPDLPVFIVGHSMGGAISILTA 169
Cdd:cd00519   113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
YpfH COG0400
Predicted esterase [General function prediction only];
75-186 1.78e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 41.82  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  75 AGPPRALVFIAHGAGEHcgPYD--EIAQRLKELSLLVFA------HDHVGHGQSEGDRMNIKNFQVYIRDSLQHID---- 142
Cdd:COG0400     1 GGPAAPLVVLLHGYGGD--EEDllPLAPELALPGAAVLAprapvpEGPGGRAWFDLSFLEGREDEEGLAAAAEALAafid 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1879453010 143 -LMKSRHPDL-PVFIVGHSMGGAISILTACERPSDFAGVVLIAPMV 186
Cdd:COG0400    79 eLEARYGIDPeRIVLAGFSQGAAMALSLALRRPELLAGVVALSGYL 124
Abhydrolase_11 pfam20408
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ...
 78-181 1.88e-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: 41.80  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  78 PRALVFIAHGAG---EHcgPY-DEIAQRLKELSLLVFAHD-------HVGHGQSEGDRMNIknFQVYIRDSLQHIdlmks 146
Cdd:pfam20408   1 PKARLLLAHGAGagmDS--PFmQAMAAALAARGIAVVRFNfpymqrrRRTGKRRPPDRAPK--LLEAFRAVIAAL----- 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1879453010 147 RHPDLPVFIVGHSMGGAISILTACErpSDFAGVVL 181
Cdd:pfam20408  72 RGPDLPLFIGGKSMGGRVASLLADD--SGVKGVIA 104
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 109-184 2.23e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 42.62  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010 109 VFAHDHVGHGQSEGDrmniknfqvYIRDSLQH-----IDLMKSRHPDlPVFIVGHSMGGAISILTACERPSDFAGVVLIA 183
Cdd:PRK14875  160 VIALDLPGHGASSKA---------VGAGSLDElaaavLAFLDALGIE-RAHLVGHSMGGAVALRLAARAPQRVASLTLIA 229


                  .
gi 1879453010 184 P 184
Cdd:PRK14875  230 P 230
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
77-183 2.35e-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: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  77 PPRALVFIAHGAGehcGPYD-----EIAQRLKELSLLVFAHDHVG--HGQSEGDRMniknfQVYIRDSLQHIDLMKSRHP 149
Cdd:COG3571     7 DPRATLLLAHGAG---AGMDspfmvALAEALAAAGIAVARFEFPYmvAGRRPPDRA-----PVLDAAWRAVIAALRARLA 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1879453010 150 DLPVFIVGHSMGGAISILTACErPSDFAGVVLIA 183
Cdd:COG3571    79 GLPLVIGGKSMGGRVASMLAAE-GGGAAGLVCLG 111
Lipase_3 pfam01764
Lipase (class 3);
145-169 9.74e-04

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 38.78  E-value: 9.74e-04
                          10        20
                  ....*....|....*....|....*
gi 1879453010 145 KSRHPDLPVFIVGHSMGGAISILTA 169
Cdd:pfam01764  57 LEKYPDYSIVVTGHSLGGALASLAA 81
COG4099 COG4099
Predicted peptidase [General function prediction only];
140-197 1.00e-03

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 39.95  E-value: 1.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1879453010 140 HIDlmKSRhpdlpVFIVGHSMGGAISILTACERPSDFAGVVLIAPmvQMNPESATPFK 197
Cdd:COG4099   121 RID--PDR-----IYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 135-169 1.27e-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: 39.02  E-value: 1.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1879453010 135 RDSLQHIDLMKSRHPDLPVFIVGHSMGGAISILTA 169
Cdd:cd00741    12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAG 46
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
155-184 4.06e-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: 4.06e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1879453010 155 IVGHSMGGAISILTACERPSDFAGVVLIAP 184
Cdd:COG2819   134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
PLN02578 PLN02578
hydrolase
 97-192 6.36e-03

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 37.90  E-value: 6.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453010  97 EIAQRLKelsllVFAHDHVGHGQSegDRMNIKNFQVYIRDslQHIDLMKSRHPDlPVFIVGHSMGGAISILTACERPSDF 176
Cdd:PLN02578  108 ELAKKYK-----VYALDLLGFGWS--DKALIEYDAMVWRD--QVADFVKEVVKE-PAVLVGNSLGGFTALSTAVGYPELV 177

                          90
                  ....*....|....*.
gi 1879453010 177 AGVVLIAPMVQMNPES 192
Cdd:PLN02578  178 AGVALLNSAGQFGSES 193
 
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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