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Conserved domains on  [gi|1879453012|ref|XP_035502228|]
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monoglyceride lipase isoform X1 [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 ...
 40-276 2.84e-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: 281.41  E-value: 2.84e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  40 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMKSRHPDLPVFI 119
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 120 VGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGT-MDSRWVSRDKTKVEAYDTD 198
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNnLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879453012 199 ELNfHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALHHDL 276
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 ...
 40-276 2.84e-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: 281.41  E-value: 2.84e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  40 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMKSRHPDLPVFI 119
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 120 VGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGT-MDSRWVSRDKTKVEAYDTD 198
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNnLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879453012 199 ELNfHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALHHDL 276
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PHA02857 PHA02857
monoglyceride lipase; Provisional
 23-291 6.32e-82

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 248.65  E-value: 6.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  23 LVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSL 102
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 103 QHIDLMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVqmNPESATPFKVFLAKVLNHLLPSLTLGTMDS 182
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 183 RWVSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApSSDKKL 262
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHA-NCNREI 241

                         250       260
                  ....*....|....*....|....*....
gi 1879453012 263 KVYEGGYHALHHDLPEVAESTLKEVTSWI 291
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWI 270
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
18-293 1.07e-46

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 156.70  E-value: 1.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  18 SELRHLVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVY 97
Cdd:COG2267     3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  98 IRDSLQHIDLMKSRhPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFkvflakvlnhllpsltl 177
Cdd:COG2267    83 VDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSA----------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 178 gtmdsRWVsrdktkveaydtdelnfhgglrvsfgmqlmgAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApS 257
Cdd:COG2267   145 -----RWL-------------------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-S 187

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1879453012 258 SDKKLKVYEGGYHALHHDlpEVAESTLKEVTSWITE 293
Cdd:COG2267   188 PDVELVLLPGARHELLNE--PAREEVLAAILAWLER 221
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 73-291 6.82e-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: 6.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  73 VFAHDHVGHGQSEG---DRMNIKNFQVYIRDSLQHI--------------------DLMKSRHPDLPVFIVGHSMGGAIS 129
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 130 -----ILTACERPSD---FAGVVLIAPMVQM----NPESATpFKVFLAKVLNHL-------LPSLTLGTMDSRWVSrdkt 190
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnIKGCISLSGMISIksvgSDDSFK-FKYFYLPVMNFMsrvfptfRISKKIRYEKSPYVN---- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 191 kvEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSI--NWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGG 268
Cdd:TIGR01607 232 --DIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309

                         250       260
                  ....*....|....*....|...
gi 1879453012 269 YHALhhDLPEVAESTLKEVTSWI 291
Cdd:TIGR01607 310 DHVI--TIEPGNEEVLKKIIEWI 330
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 100-149 1.24e-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: 1.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1879453012 100 DSLQHIDLMKSRHPDL-----PVFIVGHSMGGAISILTACERPSDFAGVVLIAPM 149
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 ...
 40-276 2.84e-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: 281.41  E-value: 2.84e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  40 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMKSRHPDLPVFI 119
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 120 VGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGT-MDSRWVSRDKTKVEAYDTD 198
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNnLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879453012 199 ELNfHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALHHDL 276
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PHA02857 PHA02857
monoglyceride lipase; Provisional
 23-291 6.32e-82

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 248.65  E-value: 6.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  23 LVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSL 102
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 103 QHIDLMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVqmNPESATPFKVFLAKVLNHLLPSLTLGTMDS 182
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 183 RWVSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApSSDKKL 262
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHA-NCNREI 241

                         250       260
                  ....*....|....*....|....*....
gi 1879453012 263 KVYEGGYHALHHDLPEVAESTLKEVTSWI 291
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWI 270
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
18-293 1.07e-46

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 156.70  E-value: 1.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  18 SELRHLVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVY 97
Cdd:COG2267     3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  98 IRDSLQHIDLMKSRhPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFkvflakvlnhllpsltl 177
Cdd:COG2267    83 VDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSA----------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 178 gtmdsRWVsrdktkveaydtdelnfhgglrvsfgmqlmgAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApS 257
Cdd:COG2267   145 -----RWL-------------------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-S 187

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1879453012 258 SDKKLKVYEGGYHALHHDlpEVAESTLKEVTSWITE 293
Cdd:COG2267   188 PDVELVLLPGARHELLNE--PAREEVLAAILAWLER 221
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 24-294 1.99e-46

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 159.92  E-value: 1.99e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  24 VNADGLHLFCRYWEP-AGPPRALVFIAHGAGEHCGPYDE-IAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDS 101
Cdd:PLN02385   67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 102 LQHIDLMKSR--HPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATP-----FKVFLAKVL--NHLL 172
Cdd:PLN02385  147 IEHYSKIKGNpeFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPplvlqILILLANLLpkAKLV 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 173 PSLTLGTMdsrwVSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMF 252
Cdd:PLN02385  227 PQKDLAEL----AFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSKFLY 302

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1879453012 253 KNAPSSDKKLKVYEGGYHALHHDLPEVAEST-LKEVTSWITEH 294
Cdd:PLN02385  303 EKASSSDKKLKLYEDAYHSILEGEPDEMIFQvLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 28-301 6.71e-37

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 134.13  E-value: 6.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  28 GLHLFCRYWEP--AGPPRALVFIAHGAGEHCG-PYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQH 104
Cdd:PLN02298   42 GLSLFTRSWLPssSSPPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 105 IDLMKSR--HPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKV-----FLAKvlnhLLPslTL 177
Cdd:PLN02298  122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPIpqiltFVAR----FLP--TL 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 178 GTMDSRWVSRDKTKVEAY----DTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFK 253
Cdd:PLN02298  196 AIVPTADLLEKSVKVPAKkiiaKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYE 275

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1879453012 254 NAPSSDKKLKVYEGGYHALHHDLP-EVAESTLKEVTSWITEHLPAKKSP 301
Cdd:PLN02298  276 EAKSEDKTIKIYDGMMHSLLFGEPdENIEIVRRDILSWLNERCTGKATP 324
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 31-295 1.48e-35

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 131.94  E-value: 1.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  31 LFCRYWEP-AGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMK 109
Cdd:PLN02652  123 LFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIR 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 110 SRHPDLPVFIVGHSMGGAIsILTACERPS---DFAGVVLIAPMVQMNPesATPFKVFLAKVLNHLLPSLTLGTMDSRW-- 184
Cdd:PLN02652  203 SENPGVPCFLFGHSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGANKRGip 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 185 VSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKV 264
Cdd:PLN02652  280 VSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRHKDIKL 359

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1879453012 265 YEGGYHALHHDlPEvAESTLKEVTSWITEHL 295
Cdd:PLN02652  360 YDGFLHDLLFE-PE-REEVGRDIIDWMEKRL 388
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
39-294 1.20e-27

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 107.72  E-value: 1.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  39 AGPPRALVFIaHGAGehCGPYD--EIAQRLKELSLLVFAHDHVGHGQSEGDrMNIKNFQVYIRDSLQHIDLMKSRHPdlP 116
Cdd:COG1647    12 EGGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--K 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 117 VFIVGHSMGGAISILTACERPsDFAGVVLIAPMVQMNPESAtpfkvFLAKVLNHLlpsltlgtmdSRWVSRDKTKVEAYD 196
Cdd:COG1647    86 VIVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-----PLLPLLKYL----------ARSLRGIGSDIEDPE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 197 TDELNFHGgLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALHHD- 275
Cdd:COG1647   150 VAEYAYDR-TPLRALAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITLDk 228

                         250       260
                  ....*....|....*....|
gi 1879453012 276 -LPEVAEstlkEVTSWITEH 294
Cdd:COG1647   229 dREEVAE----EILDFLERL 244
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 14-295 2.66e-20

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 88.05  E-value: 2.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  14 GVPYSELrHLVNADGLHLFCRYWEPAG--PPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNI 91
Cdd:COG1073     7 KVNKEDV-TFKSRDGIKLAGDLYLPAGasKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  92 KNFQvyIRDSLQHIDLMKSR--HPDLPVFIVGHSMGGAISILTACERPsDFAGVVLIAPMVQMNPESATPFKVFLAKVLN 169
Cdd:COG1073    86 GSPE--RRDARAAVDYLRTLpgVDPERIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGAYLP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 170 H--LLPSLTLgtmdsrwvsrdktkveaydtdelnfhgglrVSFGMQLMGAATRIEReipsINWPFLLLHGDADKLCDIGG 247
Cdd:COG1073   163 GvpYLPNVRL------------------------------ASLLNDEFDPLAKIEK----ISRPLLFIHGEKDEAVPFYM 208

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1879453012 248 SKMMFKNAPsSDKKLKVYEGGYHALHHDLPEvaESTLKEVTSWITEHL 295
Cdd:COG1073   209 SEDLYEAAA-EPKELLIVPGAGHVDLYDRPE--EEYFDKLAEFFKKNL 253
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
25-296 4.44e-20

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 86.99  E-value: 4.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  25 NADGLHLFCRYWEPAGP-PRALVFIAHGAGEHCGP-YDEIAQRLKELSLLVFAHDHVGHGQSEGDRmniknFQVYIRDSL 102
Cdd:COG1506     4 SADGTTLPGWLYLPADGkKYPVVVYVHGGPGSRDDsFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVDDVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 103 QHIDLMKSRhPDLP---VFIVGHSMGGAISILTACERPSDFAGVVLIAPMVqmNPESATPFKVFLAKVLNHLLPSltlgt 179
Cdd:COG1506    79 AAIDYLAAR-PYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS--DLRSYYGTTREYTERLMGGPWE----- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 180 mdsrwvsrdktKVEAYDTdelnfhgglrvsfgMQLMGAATRIEReipsinwPFLLLHGDADKLCDIGGSKMMFKNAPSS- 258
Cdd:COG1506   151 -----------DPEAYAA--------------RSPLAYADKLKT-------PLLLIHGEADDRVPPEQAERLYEALKKAg 198

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1879453012 259 -DKKLKVYEGGYHALhhdLPEVAESTLKEVTSWITEHLP 296
Cdd:COG1506   199 kPVELLVYPGEGHGF---SGAGAPDYLERILDFLDRHLK 234
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 21-294 2.14e-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: 2.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  21 RHLVNADGLHLFCRYWEPAGPPraLVFIaHGAGEHCGPYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIkNFQVYIRD 100
Cdd:COG0596     4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGY-TLDDLADD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 101 slqHIDLMKSRHPDlPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQmnpesatpfkvFLAKVLNHllpsltlgtm 180
Cdd:COG0596    79 ---LAALLDALGLE-RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA-----------ALAEPLRR---------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 181 dsrwvsrdktkveaYDTDELNFHGGLRVSFGMQLMGAATRIEReipsinwPFLLLHGDADKLCDIGGSKMMFKNAPssDK 260
Cdd:COG0596   134 --------------PGLAPEALAALLRALARTDLRERLARITV-------PTLVIWGEKDPIVPPALARRLAELLP--NA 190

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1879453012 261 KLKVYEGGYHALHHDLPEVaesTLKEVTSWITEH 294
Cdd:COG0596   191 ELVVLPGAGHFPPLEQPEA---FAAALRDFLARL 221
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
22-290 1.74e-11

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 62.68  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  22 HLVNADGLHLFCRYWEPAGP-PRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGD------RMNIKNF 94
Cdd:COG0412     7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearaLMGALDP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  95 QVYIRDSLQHIDLMKSR--HPDLPVFIVGHSMGGAISILTACERPsDFAGVVliapmvqmnpesatpfkvflakvlnhll 172
Cdd:COG0412    87 ELLAADLRAALDWLKAQpeVDAGRVGVVGFCFGGGLALLAAARGP-DLAAAV---------------------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 173 psltlgtmdsrwvsrdktkveaydtdelNFHGGLrvsfgmqlmgAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMF 252
Cdd:COG0412   138 ----------------------------SFYGGL----------PADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALE 179

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1879453012 253 K--NAPSSDKKLKVYEGGYHALHHDL-----PEVAESTLKEVTSW 290
Cdd:COG0412   180 AalAAAGVDVELHVYPGAGHGFTNPGrprydPAAAEDAWQRTLAF 224
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 45-275 1.36e-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: 60.60  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  45 LVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGdRMNIKNFQVYirDSLQHIDLMKSRHPDLPVFIVGHSM 124
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 125 GGAISILTACERPSDFAGVVLIAPMvqMNPESATPFKVFLAKVL-------------NHLLPSL-----TLGTMDSRWVS 186
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAL--DPPHELDEADRFILALFpgffdgfvadfapNPLGRLVakllaLLLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 187 RDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMfkNAPSSDKKLKVYE 266
Cdd:pfam00561 157 LPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKL--AQLFPNARLVVIP 234


                  ....*....
gi 1879453012 267 GGYHALHHD 275
Cdd:pfam00561 235 DAGHFAFLE 243
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 73-291 6.82e-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: 6.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  73 VFAHDHVGHGQSEG---DRMNIKNFQVYIRDSLQHI--------------------DLMKSRHPDLPVFIVGHSMGGAIS 129
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 130 -----ILTACERPSD---FAGVVLIAPMVQM----NPESATpFKVFLAKVLNHL-------LPSLTLGTMDSRWVSrdkt 190
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnIKGCISLSGMISIksvgSDDSFK-FKYFYLPVMNFMsrvfptfRISKKIRYEKSPYVN---- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 191 kvEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSI--NWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGG 268
Cdd:TIGR01607 232 --DIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309

                         250       260
                  ....*....|....*....|...
gi 1879453012 269 YHALhhDLPEVAESTLKEVTSWI 291
Cdd:TIGR01607 310 DHVI--TIEPGNEEVLKKIIEWI 330
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 45-281 1.72e-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: 54.02  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  45 LVFIaHGAGEHcgpYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIknfqvyiRDSLQHIDLMKSRHPDLPVFIVGHSM 124
Cdd:pfam12697   1 VVLV-HGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDL-------ADLADLAALLDELGAARPVVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 125 GGAISILTAcerPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGTMDSRWVSRDKTKVEAYDTdelnfhg 204
Cdd:pfam12697  69 GGAVALAAA---AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAA------- 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879453012 205 gLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDaDKLCDIGGSKMMfknAPSSDKKLKVYEGGYHALHHDLPEVAE 281
Cdd:pfam12697 139 -ALARLAALLAALALLPLAAWRDLPVPVLVLAEE-DRLVPELAQRLL---AALAGARLVVLPGAGHLPLDDPEEVAE 210
PRK10749 PRK10749
lysophospholipase L2; Provisional
 59-149 1.42e-07

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 51.92  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  59 YDEIAQRLKELSLLVFAHDHVGHGQS-----EGDRMNIKNFQVYIRDS----LQHIDLMKSRHpdlpVFIVGHSMGGAIS 129
Cdd:PRK10749   70 YAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLaafwQQEIQPGPYRK----RYALAHSMGGAIL 145

                          90       100
                  ....*....|....*....|
gi 1879453012 130 ILTACERPSDFAGVVLIAPM 149
Cdd:PRK10749  146 TLFLQRHPGVFDAIALCAPM 165
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 105-159 8.69e-05

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 43.45  E-value: 8.69e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012 105 IDLMKSRH---PDlPVFIVGHSMGGAISILTACERPSDFAGVVLIA--PMVQMNPESATP 159
Cdd:COG3509   122 VDDLAARYgidPK-RVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACAP 180
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 100-149 1.24e-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: 1.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1879453012 100 DSLQHIDLMKSRHPDL-----PVFIVGHSMGGAISILTACERPSDFAGVVLIAPM 149
Cdd:cd12809   151 NLAEQEALVRAAGCALldiigPAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
Abhydrolase_11 pfam20408
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ...
 42-145 1.44e-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: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  42 PRALVFIAHGAG---EHcgPY-DEIAQRLKELSLLVFAHD-------HVGHGQSEGDRMNIknFQVYIRDSLQHIdlmks 110
Cdd:pfam20408   1 PKARLLLAHGAGagmDS--PFmQAMAAALAARGIAVVRFNfpymqrrRRTGKRRPPDRAPK--LLEAFRAVIAAL----- 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1879453012 111 RHPDLPVFIVGHSMGGAISILTACErpSDFAGVVL 145
Cdd:pfam20408  72 RGPDLPLFIGGKSMGGRVASLLADD--SGVKGVIA 104
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
41-147 1.46e-04

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


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 42.18  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  41 PPRALVFIAHGAGehcGPYD-----EIAQRLKELSLLVFAHDHVG--HGQSEGDRMniknfQVYIRDSLQHIDLMKSRHP 113
Cdd:COG3571     7 DPRATLLLAHGAG---AGMDspfmvALAEALAAAGIAVARFEFPYmvAGRRPPDRA-----PVLDAAWRAVIAALRARLA 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1879453012 114 DLPVFIVGHSMGGAISILTACErPSDFAGVVLIA 147
Cdd:COG3571    79 GLPLVIGGKSMGGRVASMLAAE-GGGAAGLVCLG 111
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 100-133 1.54e-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: 1.54e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1879453012 100 DSLQHIDLMKSRHPDLPVFIVGHSMGGAISILTA 133
Cdd:cd00519   113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
YpfH COG0400
Predicted esterase [General function prediction only];
39-150 1.83e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 41.82  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  39 AGPPRALVFIAHGAGEHcgPYD--EIAQRLKELSLLVFA------HDHVGHGQSEGDRMNIKNFQVYIRDSLQHID---- 106
Cdd:COG0400     1 GGPAAPLVVLLHGYGGD--EEDllPLAPELALPGAAVLAprapvpEGPGGRAWFDLSFLEGREDEEGLAAAAEALAafid 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1879453012 107 -LMKSRHPDL-PVFIVGHSMGGAISILTACERPSDFAGVVLIAPMV 150
Cdd:COG0400    79 eLEARYGIDPeRIVLAGFSQGAAMALSLALRRPELLAGVVALSGYL 124
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 73-148 1.88e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 42.62  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  73 VFAHDHVGHGQSEGDrmniknfqvYIRDSLQH-----IDLMKSRHPDlPVFIVGHSMGGAISILTACERPSDFAGVVLIA 147
Cdd:PRK14875  160 VIALDLPGHGASSKA---------VGAGSLDElaaavLAFLDALGIE-RAHLVGHSMGGAVALRLAARAPQRVASLTLIA 229


                  .
gi 1879453012 148 P 148
Cdd:PRK14875  230 P 230
Lipase_3 pfam01764
Lipase (class 3);
109-133 9.55e-04

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 38.78  E-value: 9.55e-04
                          10        20
                  ....*....|....*....|....*
gi 1879453012 109 KSRHPDLPVFIVGHSMGGAISILTA 133
Cdd:pfam01764  57 LEKYPDYSIVVTGHSLGGALASLAA 81
COG4099 COG4099
Predicted peptidase [General function prediction only];
117-161 1.08e-03

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 39.57  E-value: 1.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1879453012 117 VFIVGHSMGGAISILTACERPSDFAGVVLIAPmvQMNPESATPFK 161
Cdd:COG4099   127 IYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 99-133 1.24e-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: 1.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1879453012  99 RDSLQHIDLMKSRHPDLPVFIVGHSMGGAISILTA 133
Cdd:cd00741    12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAG 46
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
119-148 4.13e-03

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 38.04  E-value: 4.13e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1879453012 119 IVGHSMGGAISILTACERPSDFAGVVLIAP 148
Cdd:COG2819   134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
PLN02578 PLN02578
hydrolase
 61-156 5.58e-03

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 37.90  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453012  61 EIAQRLKelsllVFAHDHVGHGQSegDRMNIKNFQVYIRDslQHIDLMKSRHPDlPVFIVGHSMGGAISILTACERPSDF 140
Cdd:PLN02578  108 ELAKKYK-----VYALDLLGFGWS--DKALIEYDAMVWRD--QVADFVKEVVKE-PAVLVGNSLGGFTALSTAVGYPELV 177

                          90
                  ....*....|....*.
gi 1879453012 141 AGVVLIAPMVQMNPES 156
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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