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Conserved domains on  [gi|1848698483|ref|XP_034732819|]
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monoglyceride lipase isoform X1 [Etheostoma cragini]

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 ...
 77-313 2.08e-96

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: 285.26  E-value: 2.08e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  77 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSLQHVDLMKSRHPDLPVFI 156
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 157 VGHSMGGAISILTACERPNDFAGVVLIAPMVQMNPDSATPFKVFLAKVLNHMAPSLTL-GSIDSKWISRDKKQVEAYEAD 235
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1848698483 236 ELNfHGGMRVSFGMQLMGAAARIEREIPSISWPFLLLHGDDDKLCDIRGSKMMYDNAPISDKKIKVYEGGYHALHHDL 313
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 ...
 77-313 2.08e-96

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: 285.26  E-value: 2.08e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  77 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSLQHVDLMKSRHPDLPVFI 156
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 157 VGHSMGGAISILTACERPNDFAGVVLIAPMVQMNPDSATPFKVFLAKVLNHMAPSLTL-GSIDSKWISRDKKQVEAYEAD 235
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1848698483 236 ELNfHGGMRVSFGMQLMGAAARIEREIPSISWPFLLLHGDDDKLCDIRGSKMMYDNAPISDKKIKVYEGGYHALHHDL 313
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PHA02857 PHA02857
monoglyceride lipase; Provisional
 60-332 4.52e-86

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 260.59  E-value: 4.52e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  60 IVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSL 139
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 140 QHVDLMKSRHPDLPVFIVGHSMGGAISILTACERPNDFAGVVLIAPMVqmNPDSATPFKVFLAKVLNHMAPSLTLGSIDS 219
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 220 KWISRDKKQVEAYEADELNFHGGMRVSFGMQLMGAAARIEREIPSISWPFLLLHGDDDKLCDIRGSKMMYDNAPiSDKKI 299
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHAN-CNREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1848698483 300 KVYEGGYHALHHDLPEVAESVLKEVTSWIIERI 332
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
55-328 5.74e-48

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 160.94  E-value: 5.74e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  55 TELQHIVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVY 134
Cdd:COG2267     3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 135 IRDSLQHVDLMKSRhPDLPVFIVGHSMGGAISILTACERPNDFAGVVLIAPMVQMNPDSATPFKVFlakvlnhmapsltl 214
Cdd:COG2267    83 VDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWL-------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 215 gsidskwisrdkkqveayeadelnfhggmrvsfgmqlmgAAARIEREIPSISWPFLLLHGDDDKLCDIRGSKMMYDNAPi 294
Cdd:COG2267   148 ---------------------------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLS- 187

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1848698483 295 SDKKIKVYEGGYHALHHDlpEVAESVLKEVTSWI 328
Cdd:COG2267   188 PDVELVLLPGARHELLNE--PAREEVLAAILAWL 219
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 110-328 1.31e-12

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: 67.50  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 110 VFAHDHVGHGQSEG---DRMNIKDFQVYIRDSLQHV--------------------DLMKSRHPDLPVFIVGHSMGGAIS 166
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 167 -----ILTACERPND---FAGVVLIAPMVQM----NPDSATpFKVFLAKVLNHMA---PSLTLGSidSKWISRDKKQVEA 231
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnIKGCISLSGMISIksvgSDDSFK-FKYFYLPVMNFMSrvfPTFRISK--KIRYEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 232 YEADELNFHGGMRVSFGMQLMGAAARIEREIPSI--SWPFLLLHGDDDKLCDIRGSKMMYDNAPISDKKIKVYEGGYHAL 309
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313

                         250
                  ....*....|....*....
gi 1848698483 310 hhDLPEVAESVLKEVTSWI 328
Cdd:TIGR01607 314 --TIEPGNEEVLKKIIEWI 330
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 137-170 3.80e-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: 41.31  E-value: 3.80e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1848698483 137 DSLQHVDLMKSRHPDLPVFIVGHSMGGAISILTA 170
Cdd:cd00519   113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
 
Name Accession Description Interval E-value
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 77-313 2.08e-96

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: 285.26  E-value: 2.08e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  77 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSLQHVDLMKSRHPDLPVFI 156
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 157 VGHSMGGAISILTACERPNDFAGVVLIAPMVQMNPDSATPFKVFLAKVLNHMAPSLTL-GSIDSKWISRDKKQVEAYEAD 235
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1848698483 236 ELNfHGGMRVSFGMQLMGAAARIEREIPSISWPFLLLHGDDDKLCDIRGSKMMYDNAPISDKKIKVYEGGYHALHHDL 313
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PHA02857 PHA02857
monoglyceride lipase; Provisional
 60-332 4.52e-86

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 260.59  E-value: 4.52e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  60 IVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSL 139
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 140 QHVDLMKSRHPDLPVFIVGHSMGGAISILTACERPNDFAGVVLIAPMVqmNPDSATPFKVFLAKVLNHMAPSLTLGSIDS 219
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 220 KWISRDKKQVEAYEADELNFHGGMRVSFGMQLMGAAARIEREIPSISWPFLLLHGDDDKLCDIRGSKMMYDNAPiSDKKI 299
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHAN-CNREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1848698483 300 KVYEGGYHALHHDLPEVAESVLKEVTSWIIERI 332
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
55-328 5.74e-48

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 160.94  E-value: 5.74e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  55 TELQHIVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVY 134
Cdd:COG2267     3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 135 IRDSLQHVDLMKSRhPDLPVFIVGHSMGGAISILTACERPNDFAGVVLIAPMVQMNPDSATPFKVFlakvlnhmapsltl 214
Cdd:COG2267    83 VDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWL-------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 215 gsidskwisrdkkqveayeadelnfhggmrvsfgmqlmgAAARIEREIPSISWPFLLLHGDDDKLCDIRGSKMMYDNAPi 294
Cdd:COG2267   148 ---------------------------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLS- 187

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1848698483 295 SDKKIKVYEGGYHALHHDlpEVAESVLKEVTSWI 328
Cdd:COG2267   188 PDVELVLLPGARHELLNE--PAREEVLAAILAWL 219
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 55-331 1.14e-46

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 161.46  E-value: 1.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  55 TELQHIVNADGLHLFCRYWEP-AGPPRALVFIAHGAGEHCGPYDE-IAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQ 132
Cdd:PLN02385   61 TEESYEVNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 133 VYIRDSLQHVDLMKSR--HPDLPVFIVGHSMGGAISILTACERPNDFAGVVLIAPMVQMNPDSATP-----FKVFLAKVL 205
Cdd:PLN02385  141 DLVDDVIEHYSKIKGNpeFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPplvlqILILLANLL 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 206 --NHMAPSLTLgsidSKWISRDKKQVEAYEADELNFHGGMRVSFGMQLMGAAARIEREIPSISWPFLLLHGDDDKLCDIR 283
Cdd:PLN02385  221 pkAKLVPQKDL----AELAFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPS 296

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1848698483 284 GSKMMYDNAPISDKKIKVYEGGYHALHHDLP-EVAESVLKEVTSWIIER 331
Cdd:PLN02385  297 VSKFLYEKASSSDKKLKLYEDAYHSILEGEPdEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 65-338 7.11e-41

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 145.69  E-value: 7.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  65 GLHLFCRYWEP--AGPPRALVFIAHGAGEHCG-PYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSLQH 141
Cdd:PLN02298   42 GLSLFTRSWLPssSSPPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 142 VDLMKSR--HPDLPVFIVGHSMGGAISILTACERPNDFAGVVLIAPMVQMNPDSATPFKV-----FLAKvlnhMAPSLTL 214
Cdd:PLN02298  122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPIpqiltFVAR----FLPTLAI 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 215 ---GSIDSKWISRDKKQVEAyEADELNFHGGMRVSFGMQLMGAAARIEREIPSISWPFLLLHGDDDKLCDIRGSKMMYDN 291
Cdd:PLN02298  198 vptADLLEKSVKVPAKKIIA-KRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEE 276

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1848698483 292 APISDKKIKVYEGGYHALHHDLP-EVAESVLKEVTSWIIERIPATTSP 338
Cdd:PLN02298  277 AKSEDKTIKIYDGMMHSLLFGEPdENIEIVRRDILSWLNERCTGKATP 324
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 68-332 1.19e-35

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 133.48  E-value: 1.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  68 LFCRYWEP-AGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSLQHVDLMK 146
Cdd:PLN02652  123 LFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIR 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 147 SRHPDLPVFIVGHSMGGAIsILTACERPN---DFAGVVLIAPMVQMNPdsATPFKVFLAKVLNHMAPSLTLGSIDSKWI- 222
Cdd:PLN02652  203 SENPGVPCFLFGHSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGANKRGIp 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 223 -SRDKKQVEAYEADELNFHGGMRVSFGMQLMGAAARIEREIPSISWPFLLLHGDDDKLCDIRGSKMMYDNAPISDKKIKV 301
Cdd:PLN02652  280 vSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRHKDIKL 359

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1848698483 302 YEGGYHALHHDlPEvAESVLKEVTSWIIERI 332
Cdd:PLN02652  360 YDGFLHDLLFE-PE-REEVGRDIIDWMEKRL 388
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
76-322 8.35e-27

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 106.18  E-value: 8.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  76 AGPPRALVFIaHGAGehCGPYD--EIAQRLKELSLLVFAHDHVGHGQSEGDrMNIKDFQVYIRDSLQHVDLMKSRHPdlP 153
Cdd:COG1647    12 EGGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--K 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 154 VFIVGHSMGGAISILTACERPnDFAGVVLIAPMVQMNPDSAtpfkvFLAKVLNHMAPSLtlgsidsKWISRDKKQVEAYE 233
Cdd:COG1647    86 VIVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-----PLLPLLKYLARSL-------RGIGSDIEDPEVAE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 234 ADelnfHGGMRVSFGMQLMGAAARIEREIPSISWPFLLLHGDDDKLCDIRGSKMMYDNAPISDKKIKVYEGGYHALHHD- 312
Cdd:COG1647   153 YA----YDRTPLRALAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITLDk 228

                         250
                  ....*....|.
gi 1848698483 313 -LPEVAESVLK 322
Cdd:COG1647   229 dREEVAEEILD 239
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 58-328 2.09e-19

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: 85.44  E-value: 2.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  58 QHIVNADGLHLFCRYWEPAGPPraLVFIaHGAGEHCGPYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIkDFQVYIRD 137
Cdd:COG0596     4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGY-TLDDLADD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 138 slqHVDLMKSRHPDlPVFIVGHSMGGAISILTACERPNDFAGVVLIAPMVQmnpdsatpfkvflakvlnhmapsltlgsi 217
Cdd:COG0596    79 ---LAALLDALGLE-RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA----------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 218 dskwisRDKKQVEAYEADELNFHGGMRVSFGMQLMGAAARIEReipsiswPFLLLHGDDDKLCDIRGSKMMYDNAPisDK 297
Cdd:COG0596   126 ------ALAEPLRRPGLAPEALAALLRALARTDLRERLARITV-------PTLVIWGEKDPIVPPALARRLAELLP--NA 190

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1848698483 298 KIKVYEGGYHALHHDLPEVaesVLKEVTSWI 328
Cdd:COG0596   191 ELVVLPGAGHFPPLEQPEA---FAAALRDFL 218
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
59-333 2.21e-19

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 85.45  E-value: 2.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  59 HIVNADGLHLFCRYWEPAGP-PRALVFIAHGAGEHCGP-YDEIAQRLKELSLLVFAHDHVGHGQSEGDRmnikdFQVYIR 136
Cdd:COG1506     1 TFKSADGTTLPGWLYLPADGkKYPVVVYVHGGPGSRDDsFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 137 DSLQHVDLMKSRhPDLP---VFIVGHSMGGAISILTACERPNDFAGVVLIAPmvqmnpdsatpfkvflakVLNHMAPSLT 213
Cdd:COG1506    76 DVLAAIDYLAAR-PYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAG------------------VSDLRSYYGT 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 214 LGSIDSKWISRDKKQVEAYEAdelnfhggmrvsfgMQLMGAAARIEReipsiswPFLLLHGDDDKLCDIRGSKMMYDNAP 293
Cdd:COG1506   137 TREYTERLMGGPWEDPEAYAA--------------RSPLAYADKLKT-------PLLLIHGEADDRVPPEQAERLYEALK 195

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1848698483 294 IS--DKKIKVYEGGYHALhhdLPEVAESVLKEVTSWIIERIP 333
Cdd:COG1506   196 KAgkPVELLVYPGEGHGF---SGAGAPDYLERILDFLDRHLK 234
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 51-323 6.72e-19

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 84.58  E-value: 6.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  51 GVPYTELqHIVNADGLHLFCRYWEPAG--PPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNI 128
Cdd:COG1073     7 KVNKEDV-TFKSRDGIKLAGDLYLPAGasKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 129 KDFQvyIRDSLQHVDLMKSR--HPDLPVFIVGHSMGGAISILTACERPNdFAGVVLIAPMVQmnpdsatpfkvfLAKVLN 206
Cdd:COG1073    86 GSPE--RRDARAAVDYLRTLpgVDPERIGLLGISLGGGYALNAAATDPR-VKAVILDSPFTS------------LEDLAA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 207 HMApsltlgsidskwisrdkKQVEAYEADELNFHGGMRVsfgMQLMGAAARIEREIPSISWPFLLLHGDDDKLCDIRGSK 286
Cdd:COG1073   151 QRA-----------------KEARGAYLPGVPYLPNVRL---ASLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSE 210

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1848698483 287 MMYDNAPiSDKKIKVYEGGYHA-LHHDLPEVAESVLKE 323
Cdd:COG1073   211 DLYEAAA-EPKELLIVPGAGHVdLYDRPEEEYFDKLAE 247
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 110-328 1.31e-12

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: 67.50  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 110 VFAHDHVGHGQSEG---DRMNIKDFQVYIRDSLQHV--------------------DLMKSRHPDLPVFIVGHSMGGAIS 166
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 167 -----ILTACERPND---FAGVVLIAPMVQM----NPDSATpFKVFLAKVLNHMA---PSLTLGSidSKWISRDKKQVEA 231
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnIKGCISLSGMISIksvgSDDSFK-FKYFYLPVMNFMSrvfPTFRISK--KIRYEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 232 YEADELNFHGGMRVSFGMQLMGAAARIEREIPSI--SWPFLLLHGDDDKLCDIRGSKMMYDNAPISDKKIKVYEGGYHAL 309
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313

                         250
                  ....*....|....*....
gi 1848698483 310 hhDLPEVAESVLKEVTSWI 328
Cdd:TIGR01607 314 --TIEPGNEEVLKKIIEWI 330
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 82-312 1.15e-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: 63.68  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  82 LVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGdRMNIKDFQVYirDSLQHVDLMKSRHPDLPVFIVGHSM 161
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 162 GGAISILTACERPNDFAGVVLIAPMvqMNPDSATPFKVFLAKVLNHM----------APSLTLGSIDSKWISRDKKQVEA 231
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAL--DPPHELDEADRFILALFPGFfdgfvadfapNPLGRLVAKLLALLLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 232 YEADELNFHGGMRVSFGMQLMGAAARIER--------EIPSISWPFLLLHGDDDKLCDIRGSKmmYDNAPISDKKIKVYE 303
Cdd:pfam00561 157 LPLLNKRFPSGDYALAKSLVTGALLFIETwstelrakFLGRLDEPTLIIWGDQDPLVPPQALE--KLAQLFPNARLVVIP 234


                  ....*....
gi 1848698483 304 GGYHALHHD 312
Cdd:pfam00561 235 DAGHFAFLE 243
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
59-327 1.43e-11

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 63.06  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  59 HIVNADGLHLFCRYWEPAGP-PRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGD------RMNIKDF 131
Cdd:COG0412     7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearaLMGALDP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 132 QVYIRDSLQHVDLMKSR--HPDLPVFIVGHSMGGAISILTACERPnDFAGVVliapmvqmnpdsatpfkvflakvlnhma 209
Cdd:COG0412    87 ELLAADLRAALDWLKAQpeVDAGRVGVVGFCFGGGLALLAAARGP-DLAAAV---------------------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 210 psltlgsidskwisrdkkqveayeadelNFHGGmrvsfgmqlmGAAARIEREIPSISWPFLLLHGDDDKLCDIRGSKMMY 289
Cdd:COG0412   138 ----------------------------SFYGG----------LPADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALE 179

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1848698483 290 D--NAPISDKKIKVYEGGYHALHHDL-----PEVAESVLKEVTSW 327
Cdd:COG0412   180 AalAAAGVDVELHVYPGAGHGFTNPGrprydPAAAEDAWQRTLAF 224
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 82-318 1.54e-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: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  82 LVFIaHGAGEHcgpYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIKDFQvyirdslQHVDLMKSRHPDLPVFIVGHSM 161
Cdd:pfam12697   1 VVLV-HGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLADLA-------DLAALLDELGAARPVVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 162 GGAISILTAcerPNDFAGVVLIAPMVQMNPDSATPFKVFLAKVLNHMAPSLTLGSIDSKWISRDKKQVEAYEAdelnfhg 241
Cdd:pfam12697  69 GGAVALAAA---AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAA------- 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1848698483 242 gMRVSFGMQLMGAAARIEREIPSISWPFLLLHGDDDKLcdirGSKMMYDNAPISDKKIKVYEGGYHALHHDLPEVAE 318
Cdd:pfam12697 139 -ALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLV----PELAQRLLAALAGARLVVLPGAGHLPLDDPEEVAE 210
PRK10749 PRK10749
lysophospholipase L2; Provisional
 96-186 1.27e-06

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 49.61  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  96 YDEIAQRLKELSLLVFAHDHVGHGQS-----EGDRMNIKDFQVYIRDS----LQHVDLMKSRHpdlpVFIVGHSMGGAIS 166
Cdd:PRK10749   70 YAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLaafwQQEIQPGPYRK----RYALAHSMGGAIL 145

                          90       100
                  ....*....|....*....|
gi 1848698483 167 ILTACERPNDFAGVVLIAPM 186
Cdd:PRK10749  146 TLFLQRHPGVFDAIALCAPM 165
YpfH COG0400
Predicted esterase [General function prediction only];
76-187 4.55e-05

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 43.74  E-value: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  76 AGPPRALVFIAHGAGEHcgPYD--EIAQRLKELSLLVFA------HDHVGHG----QSEGDRMNIKDfqvyIRDSLQHVD 143
Cdd:COG0400     1 GGPAAPLVVLLHGYGGD--EEDllPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEG----LAAAAEALA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1848698483 144 -----LMKSRHPDL-PVFIVGHSMGGAISILTACERPNDFAGVVLIAPMV 187
Cdd:COG0400    75 afideLEARYGIDPeRIVLAGFSQGAAMALSLALRRPELLAGVVALSGYL 124
Abhydrolase_11 pfam20408
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ...
 79-182 6.10e-05

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: 43.34  E-value: 6.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  79 PRALVFIAHGAG---EHcgPY-DEIAQRLKELSLLVFAHD-------HVGHGQSEGDRMNIkdFQVYIRDSLQHVdlmks 147
Cdd:pfam20408   1 PKARLLLAHGAGagmDS--PFmQAMAAALAARGIAVVRFNfpymqrrRRTGKRRPPDRAPK--LLEAFRAVIAAL----- 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1848698483 148 RHPDLPVFIVGHSMGGAISILTACERpnDFAGVVL 182
Cdd:pfam20408  72 RGPDLPLFIGGKSMGGRVASLLADDS--GVKGVIA 104
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 142-196 9.13e-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: 9.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 142 VDLMKSRH---PDlPVFIVGHSMGGAISILTACERPNDFAGVVLIA--PMVQMNPDSATP 196
Cdd:COG3509   122 VDDLAARYgidPK-RVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACAP 180
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
78-184 1.78e-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: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  78 PPRALVFIAHGAGehcGPYD-----EIAQRLKELSLLVFAHDHVG--HGQSEGDRMnikdfQVYIRDSLQHVDLMKSRHP 150
Cdd:COG3571     7 DPRATLLLAHGAG---AGMDspfmvALAEALAAAGIAVARFEFPYmvAGRRPPDRA-----PVLDAAWRAVIAALRARLA 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1848698483 151 DLPVFIVGHSMGGAISILTACERPnDFAGVVLIA 184
Cdd:COG3571    79 GLPLVIGGKSMGGRVASMLAAEGG-GAAGLVCLG 111
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 137-170 3.80e-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: 41.31  E-value: 3.80e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1848698483 137 DSLQHVDLMKSRHPDLPVFIVGHSMGGAISILTA 170
Cdd:cd00519   113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 137-186 4.00e-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: 41.44  E-value: 4.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1848698483 137 DSLQHVDLMKSRHPDL-----PVFIVGHSMGGAISILTACERPNDFAGVVLIAPM 186
Cdd:cd12809   151 NLAEQEALVRAAGCALldiigPAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
COG4099 COG4099
Predicted peptidase [General function prediction only];
154-198 5.38e-04

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 40.72  E-value: 5.38e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1848698483 154 VFIVGHSMGGAISILTACERPNDFAGVVLIAPmvQMNPDSATPFK 198
Cdd:COG4099   127 IYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 110-185 6.64e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 41.08  E-value: 6.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 110 VFAHDHVGHGQSEgdrmniKDFQvyiRDSLQH-----VDLMKSRHPDlPVFIVGHSMGGAISILTACERPNDFAGVVLIA 184
Cdd:PRK14875  160 VIALDLPGHGASS------KAVG---AGSLDElaaavLAFLDALGIE-RAHLVGHSMGGAVALRLAARAPQRVASLTLIA 229


                  .
gi 1848698483 185 P 185
Cdd:PRK14875  230 P 230
Lipase_3 pfam01764
Lipase (class 3);
146-170 1.16e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 38.78  E-value: 1.16e-03
                          10        20
                  ....*....|....*....|....*
gi 1848698483 146 KSRHPDLPVFIVGHSMGGAISILTA 170
Cdd:pfam01764  57 LEKYPDYSIVVTGHSLGGALASLAA 81
PLN02847 PLN02847
triacylglycerol lipase
 147-230 1.38e-03

triacylglycerol lipase


Pssm-ID: 178439 [Multi-domain]  Cd Length: 633  Bit Score: 40.63  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483 147 SRHPDLPVFIVGHSMGGAI-SILTACERPN-DFAGV--VLIAPMVQMNPDSATPFKVFLAKVLN--HMAPSLTLGSID-- 218
Cdd:PLN02847  246 DEYPDFKIKIVGHSLGGGTaALLTYILREQkEFSSTtcVTFAPAACMTWDLAESGKHFITTIINgsDLVPTFSAASVDdl 325

                          90
                  ....*....|....*...
gi 1848698483 219 ------SKWISRDKKQVE 230
Cdd:PLN02847  326 rsevtaSSWLNDLRDQVE 343
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 136-170 1.97e-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: 38.25  E-value: 1.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1848698483 136 RDSLQHVDLMKSRHPDLPVFIVGHSMGGAISILTA 170
Cdd:cd00741    12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAG 46
PLN02578 PLN02578
hydrolase
 98-188 2.46e-03

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 39.44  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848698483  98 EIAQRLKelsllVFAHDHVGHGQSegDRMNIK-DFQVYIRdslQHVDLMKSRHPDlPVFIVGHSMGGAISILTACERPND 176
Cdd:PLN02578  108 ELAKKYK-----VYALDLLGFGWS--DKALIEyDAMVWRD---QVADFVKEVVKE-PAVLVGNSLGGFTALSTAVGYPEL 176

                          90
                  ....*....|..
gi 1848698483 177 FAGVVLIAPMVQ 188
Cdd:PLN02578  177 VAGVALLNSAGQ 188
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
156-185 3.52e-03

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 38.43  E-value: 3.52e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1848698483 156 IVGHSMGGAISILTACERPNDFAGVVLIAP 185
Cdd:COG2819   134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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