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Conserved domains on  [gi|2266249370|ref|XP_048813844|]
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monoglyceride lipase isoform X1 [Lagopus muta]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 33-305 2.07e-97

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member PHA02857:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 276  Bit Score: 288.71  E-value: 2.07e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  33 IINADGQHLFCRYWKPAAAARALVFIAHGAGEHCGRYDDLAQRLTELNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSL 112
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 113 QHIDLMKKDHPGLPILILGHSMGGAISILTASERPSDFSGMLLISPLVvaNPEVATPIKVFAAKVLNLVLPNLSLGSIDP 192
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 193 NAISRNKKEMESYTSDPLVYHGGMKVSFVIQLMNAITRIERALPKLTLPILVLHGSSDKLCDIKGSYLLMDTVQSqDKTL 272
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2266249370 273 KVYEEAYHALHKELPEVTASVFTEILTWVGQKV 305
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 33-305 2.07e-97

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 288.71  E-value: 2.07e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  33 IINADGQHLFCRYWKPAAAARALVFIAHGAGEHCGRYDDLAQRLTELNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSL 112
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 113 QHIDLMKKDHPGLPILILGHSMGGAISILTASERPSDFSGMLLISPLVvaNPEVATPIKVFAAKVLNLVLPNLSLGSIDP 192
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 193 NAISRNKKEMESYTSDPLVYHGGMKVSFVIQLMNAITRIERALPKLTLPILVLHGSSDKLCDIKGSYLLMDTVQSqDKTL 272
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2266249370 273 KVYEEAYHALHKELPEVTASVFTEILTWVGQKV 305
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 50-286 7.37e-92

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: 272.94  E-value: 7.37e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  50 AAARALVFIAHGAGEHCGRYDDLAQRLTELNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSLQHIDLMKKDHPGLPILI 129
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 130 LGHSMGGAISILTASERPSDFSGMLLISPLVVANPEVATPIKVFAAKVLNLVLPNLSL-GSIDPNAISRNKKEMESYTSD 208
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2266249370 209 PLVyHGGMKVSFVIQLMNAITRIERALPKLTLPILVLHGSSDKLCDIKGSYLLMDTVQSQDKTLKVYEEAYHALHKEL 286
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
32-303 1.21e-48

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 162.09  E-value: 1.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  32 HIINADGQHLFCRYWKPAAAARALVFIAHGAGEHCGRYDDLAQRLTELNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDS 111
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 112 LQHIDLMKKdHPGLPILILGHSMGGAISILTASERPSDFSGMLLISPLVVANPEVATPIKVFAAkvlnlvlpnlslgsid 191
Cdd:COG2267    87 RAALDALRA-RPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 192 pnaisrnkkemesytsdplvyhggmkvsfviqlmnaiTRIERALPKLTLPILVLHGSSDKLCDIKGSYLLMDTVqSQDKT 271
Cdd:COG2267   150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVE 191

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2266249370 272 LKVYEEAYHALHKELPEvtASVFTEILTWVGQ 303
Cdd:COG2267   192 LVLLPGARHELLNEPAR--EEVLAAILAWLER 221
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 83-301 1.89e-06

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: 48.62  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  83 VFAHDHVGHGQSEG---DRMVVSDFHVFIRDSLQHI--------------------DLMKKDHPGLPILILGHSMGGAIS 139
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 140 -----ILTASERPSD---------FSGMLLISplVVANPEvATPIKVFAAKVLNLVlpnlslGSIDPNAISRNKKEMES- 204
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnikgcisLSGMISIK--SVGSDD-SFKFKYFYLPVMNFM------SRVFPTFRISKKIRYEKs 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 205 ------YTSDPLVYHGGMKVSFVIQLMNAITRIE---RALPKlTLPILVLHGSSDKLCDIKGSYLLMDTVQSQDKTLKVY 275
Cdd:TIGR01607 228 pyvndiIKFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTL 306

                         250       260
                  ....*....|....*....|....*.
gi 2266249370 276 EEAYHALHKElpEVTASVFTEILTWV 301
Cdd:TIGR01607 307 EDMDHVITIE--PGNEEVLKKIIEWI 330
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 104-145 7.92e-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: 40.15  E-value: 7.92e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2266249370 104 FHVFIRDSLQHIDLMKKDHPGLPILILGHSMGGAISILTASE 145
Cdd:cd00519   107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 33-305 2.07e-97

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 288.71  E-value: 2.07e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  33 IINADGQHLFCRYWKPAAAARALVFIAHGAGEHCGRYDDLAQRLTELNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSL 112
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 113 QHIDLMKKDHPGLPILILGHSMGGAISILTASERPSDFSGMLLISPLVvaNPEVATPIKVFAAKVLNLVLPNLSLGSIDP 192
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 193 NAISRNKKEMESYTSDPLVYHGGMKVSFVIQLMNAITRIERALPKLTLPILVLHGSSDKLCDIKGSYLLMDTVQSqDKTL 272
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2266249370 273 KVYEEAYHALHKELPEVTASVFTEILTWVGQKV 305
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 50-286 7.37e-92

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: 272.94  E-value: 7.37e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  50 AAARALVFIAHGAGEHCGRYDDLAQRLTELNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSLQHIDLMKKDHPGLPILI 129
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 130 LGHSMGGAISILTASERPSDFSGMLLISPLVVANPEVATPIKVFAAKVLNLVLPNLSL-GSIDPNAISRNKKEMESYTSD 208
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2266249370 209 PLVyHGGMKVSFVIQLMNAITRIERALPKLTLPILVLHGSSDKLCDIKGSYLLMDTVQSQDKTLKVYEEAYHALHKEL 286
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
32-303 1.21e-48

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 162.09  E-value: 1.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  32 HIINADGQHLFCRYWKPAAAARALVFIAHGAGEHCGRYDDLAQRLTELNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDS 111
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 112 LQHIDLMKKdHPGLPILILGHSMGGAISILTASERPSDFSGMLLISPLVVANPEVATPIKVFAAkvlnlvlpnlslgsid 191
Cdd:COG2267    87 RAALDALRA-RPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 192 pnaisrnkkemesytsdplvyhggmkvsfviqlmnaiTRIERALPKLTLPILVLHGSSDKLCDIKGSYLLMDTVqSQDKT 271
Cdd:COG2267   150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVE 191

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2266249370 272 LKVYEEAYHALHKELPEvtASVFTEILTWVGQ 303
Cdd:COG2267   192 LVLLPGARHELLNEPAR--EEVLAAILAWLER 221
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 36-301 1.02e-40

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 146.19  E-value: 1.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  36 ADGQHLFCRYWKPAAAA-RALVFIAHGAGEHCGRYDDLAQRLTELNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSLQH 114
Cdd:PLN02652  118 ARRNALFCRSWAPAAGEmRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 115 IDLMKKDHPGLPILILGHSMGGAIsILTASERPS---DFSGMLLISPLVVANPevATPIKVFAAKVLNLVLPNLSLGSID 191
Cdd:PLN02652  198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGAN 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 192 PNAI--SRNKKEMESYTSDPLVYHGGMKVSFVIQLMNAITRIERALPKLTLPILVLHGSSDKLCDIKGSYLLMDTVQSQD 269
Cdd:PLN02652  275 KRGIpvSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRH 354

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2266249370 270 KTLKVYEEAYHALHKElPEvTASVFTEILTWV 301
Cdd:PLN02652  355 KDIKLYDGFLHDLLFE-PE-REEVGRDIIDWM 384
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 35-306 1.23e-40

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 144.90  E-value: 1.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  35 NADGQHLFCRYWKPAAAA-RALVFIAHGAGEHCGRY-DDLAQRLTELNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSL 112
Cdd:PLN02385   68 NSRGVEIFSKSWLPENSRpKAAVCFCHGYGDTCTFFfEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDVI 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 113 QHIDLMK--KDHPGLPILILGHSMGGAISILTASERPSDFSGMLLISPLV-----VANPEVATPIKVFAAKVL---NLVl 182
Cdd:PLN02385  148 EHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCkiaddVVPPPLVLQILILLANLLpkaKLV- 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 183 PNLSLGSI---DPNaisrnKKEMESYtsDPLVYHGGMKVSFVIQLMNAITRIERALPKLTLPILVLHGSSDKLCDIKGSY 259
Cdd:PLN02385  227 PQKDLAELafrDLK-----KRKMAEY--NVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSK 299

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2266249370 260 LLMDTVQSQDKTLKVYEEAYHA-LHKELPEVTASVFTEILTWVGQKVS 306
Cdd:PLN02385  300 FLYEKASSSDKKLKLYEDAYHSiLEGEPDEMIFQVLDDIISWLDSHST 347
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 38-313 2.73e-35

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 130.28  E-value: 2.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  38 GQHLFCRYWKPAA--AARALVFIAHGAGEHCG-RYDDLAQRLTELNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSLQH 114
Cdd:PLN02298   42 GLSLFTRSWLPSSssPPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 115 IDLMKKD--HPGLPILILGHSMGGAISILTASERPSDFSGMLLISPLVVANPEVATP-----IKVFAAKVLNL--VLPNL 185
Cdd:PLN02298  122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPwpipqILTFVARFLPTlaIVPTA 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 186 SLgsIDPNAISRNKKEMESytSDPLVYHGGMKVSFVIQLMNAITRIERALPKLTLPILVLHGSSDKLCDIKGSYLLMDTV 265
Cdd:PLN02298  202 DL--LEKSVKVPAKKIIAK--RNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEA 277

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2266249370 266 QSQDKTLKVYEEAYHA-LHKELPEVTASVFTEILTWVGQKVSAAGETSQ 313
Cdd:PLN02298  278 KSEDKTIKIYDGMMHSlLFGEPDENIEIVRRDILSWLNERCTGKATPSE 326
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
71-306 7.82e-26

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 102.71  E-value: 7.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  71 DLAQRLTELNLFVFAHDHVGHGQSEGDrMVVSDFHVFIRDSLQHIDLMKKDHPglPILILGHSMGGAISILTASERPsDF 150
Cdd:COG1647    33 PLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KVIVIGLSMGGLLALLLAARYP-DV 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 151 SGMLLISPlvvanpevatpikvfAAKVLNLVLPNLSLGSIDPNAISRNKKEMESYTSDPLVYHGgMKVSFVIQLMNAITR 230
Cdd:COG1647   109 AGLVLLSP---------------ALKIDDPSAPLLPLLKYLARSLRGIGSDIEDPEVAEYAYDR-TPLRALAELQRLIRE 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2266249370 231 IERALPKLTLPILVLHGSSDKLCDIKGSYLLMDTVQSQDKTLKVYEEAYHALH--KELPEvtasVFTEILTWVGQKVS 306
Cdd:COG1647   173 VRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKDREE----VAEEILDFLERLAA 246
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 26-281 2.97e-19

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 84.97  E-value: 2.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  26 PYKDLPH----IINADGQHLFCRYWKPAAAA--RALVFIAHGAGEHCGRYDDLAQRLTELNLFVFAHDHVGHGQSEGD-R 98
Cdd:COG1073     4 PSDKVNKedvtFKSRDGIKLAGDLYLPAGASkkYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEpR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  99 MVVS----DFHVFIrDSLQHidlmKKDHPGLPILILGHSMGGAISILTASERPsDFSGMLLISPLVVANPEVATPIKVFA 174
Cdd:COG1073    84 EEGSperrDARAAV-DYLRT----LPGVDPERIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEAR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 175 AKVLNLV--LPNLSLgsidpnaisrnkkemesytsdplvyhggmkVSFVIQLMNAITRIEralpKLTLPILVLHGSSDKL 252
Cdd:COG1073   158 GAYLPGVpyLPNVRL------------------------------ASLLNDEFDPLAKIE----KISRPLLFIHGEKDEA 203

                         250       260
                  ....*....|....*....|....*....
gi 2266249370 253 CDIKGSYLLMDTVqSQDKTLKVYEEAYHA 281
Cdd:COG1073   204 VPFYMSEDLYEAA-AEPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
32-303 7.53e-19

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 83.53  E-value: 7.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  32 HIINADGQHLFCRYWKPAAAARA-LVFIAHGAGEH-CGRYDDLAQRLTELNLFVFAHDHVGHGQSEGDRmvvsdFHVFIR 109
Cdd:COG1506     1 TFKSADGTTLPGWLYLPADGKKYpVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 110 DSLQHIDLMKKdHPGLP---ILILGHSMGGAISILTASERPSDFSGMLLISPlvVANpevatpikvfaakvlnlvlpnls 186
Cdd:COG1506    76 DVLAAIDYLAA-RPYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAG--VSD----------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 187 LGSIDPNAISRNKKEMESYTSDPLVYhggmkvsfviQLMNAITRIEralpKLTLPILVLHGSSDKLCDIKGSYLLMDTVQ 266
Cdd:COG1506   130 LRSYYGTTREYTERLMGGPWEDPEAY----------AARSPLAYAD----KLKTPLLLIHGEADDRVPPEQAERLYEALK 195

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2266249370 267 SQ--DKTLKVYEEAYHALHKelpEVTASVFTEILTWVGQ 303
Cdd:COG1506   196 KAgkPVELLVYPGEGHGFSG---AGAPDYLERILDFLDR 231
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 31-298 7.19e-17

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: 77.73  E-value: 7.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  31 PHIINADGQHLFCRYWkpAAAARALVFIaHGAGEHCGRYDDLAQRLTElNLFVFAHDHVGHGQSEGDRMVVSdFHVFIRD 110
Cdd:COG0596     4 PRFVTVDGVRLHYREA--GPDGPPVVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYT-LDDLADD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 111 slqHIDLMkkDHPGL-PILILGHSMGGAISILTASERPSDFSGMLLISPLVVAnpevatpikvfaakvlnlVLPNLSLGS 189
Cdd:COG0596    79 ---LAALL--DALGLeRVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAA------------------LAEPLRRPG 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 190 IDPNAISRnkkemesytsdplvyhggmkvsfviqLMNAITR--IERALPKLTLPILVLHGSSDKLCDIKGSYLLMDTVqs 267
Cdd:COG0596   136 LAPEALAA--------------------------LLRALARtdLRERLARITVPTLVIWGEKDPIVPPALARRLAELL-- 187

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2266249370 268 QDKTLKVYEEAYHALHKELPEVTASVFTEIL 298
Cdd:COG0596   188 PNAELVVLPGAGHFPPLEQPEAFAAALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 55-285 2.33e-09

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: 56.74  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  55 LVFIAHGAGEHCGRYDDLAQRLTELNLFVFAHDHVGHGQSEGdRMVVSDFHV-FIRDSLQHIdlmkKDHPGL-PILILGH 132
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTdDLAEDLEYI----LEALGLeKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 133 SMGGAISILTASERPSDFSGMLLISPLV----------------------VANPEVATPIKVFAAKVLNLVLPNLSLGSI 190
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGALDppheldeadrfilalfpgffdgFVADFAPNPLGRLVAKLLALLLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 191 DPNaISRNKKEMESYTSDPLVYhggmkvsFVIQLMNAITRIERA--LPKLTLPILVLHGSSDKLCDIKGSYLLMDTVQSq 268
Cdd:pfam00561 157 LPL-LNKRFPSGDYALAKSLVT-------GALLFIETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPN- 227

                         250
                  ....*....|....*..
gi 2266249370 269 dKTLKVYEEAYHALHKE 285
Cdd:pfam00561 228 -ARLVVIPDAGHFAFLE 243
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
32-283 7.07e-08

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 52.28  E-value: 7.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  32 HIINADGQHLFCRYWKPAAAA-RALVFIAHGAGEHCGRYDDLAQRLTELNLFVFAHDHVGHGQSEGD------RMVVSDF 104
Cdd:COG0412     7 TIPTPDGVTLPGYLARPAGGGpRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearaLMGALDP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 105 HVFIRDSLQHIDLMKK--DHPGLPILILGHSMGGAISILTASERPsdfsgmllisplvvanpevatpikVFAAkvlnlvl 182
Cdd:COG0412    87 ELLAADLRAALDWLKAqpEVDAGRVGVVGFCFGGGLALLAAARGP------------------------DLAA------- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 183 pnlslgsidpnAISrnkkemesytsdplvYHGGMKVSFVIQLmnaitrieraLPKLTLPILVLHGSSDKLCDIKGSYLLM 262
Cdd:COG0412   136 -----------AVS---------------FYGGLPADDLLDL----------AARIKAPVLLLYGEKDPLVPPEQVAALE 179

                         250       260
                  ....*....|....*....|...
gi 2266249370 263 DTVQSQ--DKTLKVYEEAYHALH 283
Cdd:COG0412   180 AALAAAgvDVELHVYPGAGHGFT 202
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 55-293 1.75e-06

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 47.85  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  55 LVFIaHGAGEHCGRYDDLAQRltelNLFVFAHDHVGHGQSEGDRMVVSDfhvfIRDSLQHIDLMKKDHPglpILILGHSM 134
Cdd:pfam12697   1 VVLV-HGAGLSAAPLAALLAA----GVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 135 GGAISILTAserPSDFSGMLLISPLVVANPEVATPIKVFAAKVLNLVLPNLSLGSIDPNAISRNKKEMESYTSDPLVYHG 214
Cdd:pfam12697  69 GGAVALAAA---AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAA 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2266249370 215 gmkvsfviQLMNAITRIERALPKLTLPILVLHGSSDKLcdikGSYLLMDTVQSQDKTLKVYEEAYHALHkELPEVTASV 293
Cdd:pfam12697 146 --------LLAALALLPLAAWRDLPVPVLVLAEEDRLV----PELAQRLLAALAGARLVVLPGAGHLPL-DDPEEVAEA 211
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 83-301 1.89e-06

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: 48.62  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  83 VFAHDHVGHGQSEG---DRMVVSDFHVFIRDSLQHI--------------------DLMKKDHPGLPILILGHSMGGAIS 139
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 140 -----ILTASERPSD---------FSGMLLISplVVANPEvATPIKVFAAKVLNLVlpnlslGSIDPNAISRNKKEMES- 204
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnikgcisLSGMISIK--SVGSDD-SFKFKYFYLPVMNFM------SRVFPTFRISKKIRYEKs 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 205 ------YTSDPLVYHGGMKVSFVIQLMNAITRIE---RALPKlTLPILVLHGSSDKLCDIKGSYLLMDTVQSQDKTLKVY 275
Cdd:TIGR01607 228 pyvndiIKFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTL 306

                         250       260
                  ....*....|....*....|....*.
gi 2266249370 276 EEAYHALHKElpEVTASVFTEILTWV 301
Cdd:TIGR01607 307 EDMDHVITIE--PGNEEVLKKIIEWI 330
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 44-158 5.93e-05

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 44.16  E-value: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  44 RYWKPAAAARALVFIAHG-AGEH---CGRYDDLAQRLTelnlfVFAHDHVGHGQSeGDRMVVSDFHvFIRDSLqhIDLMk 119
Cdd:PRK14875  122 RYLRLGEGDGTPVVLIHGfGGDLnnwLFNHAALAAGRP-----VIALDLPGHGAS-SKAVGAGSLD-ELAAAV--LAFL- 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2266249370 120 kDHPGLPILIL-GHSMGGAISILTASERPSDFSGMLLISP 158
Cdd:PRK14875  192 -DALGIERAHLvGHSMGGAVALRLAARAPQRVASLTLIAP 230
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 104-145 7.92e-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: 40.15  E-value: 7.92e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2266249370 104 FHVFIRDSLQHIDLMKKDHPGLPILILGHSMGGAISILTASE 145
Cdd:cd00519   107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
YpfH COG0400
Predicted esterase [General function prediction only];
49-169 2.29e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 38.35  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  49 AAAARALVFIAHGAGehcGRYDDLAQRLTELNL----FVFAH-----DHVGHG-----------QSEGDRMVVSDFHVFI 108
Cdd:COG0400     1 GGPAAPLVVLLHGYG---GDEEDLLPLAPELALpgaaVLAPRapvpeGPGGRAwfdlsflegreDEEGLAAAAEALAAFI 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2266249370 109 RDSLQHIDLmkkdhPGLPILILGHSMGGAISILTASERPSDFSGMLLISPLVVANPEVATP 169
Cdd:COG0400    78 DELEARYGI-----DPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAP 133
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
37-158 2.59e-03

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 38.81  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  37 DGQHLFcryWKPAAAARALVFIAHGAGEHC----GRYDDLAQRLTELNLFVFAHDHVGHGQS-EGDrmvvsDFHVFIRDS 111
Cdd:COG2819    45 DGQNLF---DALAGAVGTLSRLEGGIPPAIvvgiGNGDDGERRLRDYTPPPAPGYPGPGGPGgGAD-----AFLRFLEEE 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2266249370 112 LQ-HIDlmkKDHPGLP--ILILGHSMGGAISILTASERPSDFSGMLLISP 158
Cdd:COG2819   117 LKpYID---KRYRTDPerTGLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
48-280 4.75e-03

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 38.16  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  48 PAAAARALVFIAHGAGEHCGRYDDLAQRLTELNLFVFAHDHVGH--GQSEGDRMVVSDFHVF---------IRDSLQHID 116
Cdd:COG4188    57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaADLSAALDGLADALDPeelwerpldLSFVLDQLL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 117 LMKKDHPGLP-------ILILGHSMGGAISILTASERPSDFSgmllisplvvanpevatpIKVFAAKVLNLVLPNLSLGS 189
Cdd:COG4188   137 ALNKSDPPLAgrldldrIGVIGHSLGGYTALALAGARLDFAA------------------LRQYCGKNPDLQCRALDLPR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 190 IDPNaisrnkkemesyTSDPlvyhggmKVSFVIqLMNAITRI---ERALPKLTLPILVLHGSsdklCDIKGSYL-----L 261
Cdd:COG4188   199 LAYD------------LRDP-------RIKAVV-ALAPGGSGlfgEEGLAAITIPVLLVAGS----ADDVTPAPdeqirP 254

                         250
                  ....*....|....*....
gi 2266249370 262 MDTVQSQDKTLKVYEEAYH 280
Cdd:COG4188   255 FDLLPGADKYLLTLEGATH 273
Lipase_3 pfam01764
Lipase (class 3);
108-174 5.46e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 36.47  E-value: 5.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2266249370 108 IRDSLQhiDLMKKdHPGLPILILGHSMGGAISILTASErpsdfsgmllispLVVANPEVATPIKVFA 174
Cdd:pfam01764  49 VLAELK--RLLEK-YPDYSIVVTGHSLGGALASLAALD-------------LVENGLRLSSRVTVVT 99
PRK10749 PRK10749
lysophospholipase L2; Provisional
 55-298 7.24e-03

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 37.67  E-value: 7.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370  55 LVFIAHGAGEHCGRYDDLAQRLTELNLFVFAHDHVGHGQSegDRMV--------------VSDFHVFIrdsLQHIDlmkk 120
Cdd:PRK10749   56 VVVICPGRIESYVKYAELAYDLFHLGYDVLIIDHRGQGRS--GRLLddphrghverfndyVDDLAAFW---QQEIQ---- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 121 dhPGLPI--LILGHSMGGAISILTASERPSDFSGMLLISPLVvanpEVATPIKVFAA-KVLNLVLPN--------LSLGS 189
Cdd:PRK10749  127 --PGPYRkrYALAHSMGGAILTLFLQRHPGVFDAIALCAPMF----GIVLPLPSWMArRILNWAEGHprirdgyaIGTGR 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266249370 190 IDP-----NAIS----RNKKEMESYTSDPLVYHGGMKVSFVIQLMNAITRIERALPKLTLPILVLHGSSDKLCDikgsyl 260
Cdd:PRK10749  201 WRPlpfaiNVLThsreRYRRNLRFYADDPELRVGGPTYHWVRESILAGEQVLAGAGDITTPLLLLQAEEERVVD------ 274

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2266249370 261 lmdtVQSQDKTLKVYEEAYHALHKELPEVTASVFTEIL 298
Cdd:PRK10749  275 ----NRMHDRFCEARTAAGHPCEGGKPLVIKGAYHEIL 308
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 104-145 8.95e-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: 36.32  E-value: 8.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2266249370 104 FHVFIRDSLQHIDLMKKDHPGLPILILGHSMGGAISILTASE 145
Cdd:cd00741     7 ARSLANLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
 
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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