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Conserved domains on  [gi|19923092|ref|NP_612511|]
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monoglyceride lipase isoform 2 [Rattus norvegicus]

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, ...
 22-296 1.22e-106

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: 311.43  E-value: 1.22e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   22 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLL 101
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  102 QHVNTVQKDYPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLIlaNPESASTLKVLAAKLLNFVLPNISLGRIDS 181
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  182 SVLSRNKSEVDLYNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSqDKTL 261
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 19923092  262 KMYEGAYHVLHKELPEVTNSVLHEINTWVSHRIAV 296
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRVKV 276
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-296 1.22e-106

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 311.43  E-value: 1.22e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   22 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLL 101
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  102 QHVNTVQKDYPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLIlaNPESASTLKVLAAKLLNFVLPNISLGRIDS 181
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  182 SVLSRNKSEVDLYNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSqDKTL 261
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 19923092  262 KMYEGAYHVLHKELPEVTNSVLHEINTWVSHRIAV 296
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRVKV 276
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-275 2.51e-91

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: 271.01  E-value: 2.51e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092    41 PKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLLQHVNTVQKDYPEVPVFLLG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   121 HSMGGAISILAAAERPTHFSGMILISPLILANPESASTLKVLAAKLLNFVLPNISL-GRIDSSVLSRNKSEVDLYNSDPL 199
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923092   200 iCHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSQDKTLKMYEGAYHVLHKEL 275
Cdd:pfam12146 163 -VHGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-290 2.24e-48

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 160.94  E-value: 2.24e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  21 HLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDL 100
Cdd:COG2267   7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092 101 LQHVNTVQKDyPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLILANPESASTLKVLAAkllnfvlpnislgrid 180
Cdd:COG2267  87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092 181 ssvlsrnksevdlynsdplichagvkvcfgiqllnavSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSqDKT 260
Cdd:COG2267 150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSP-DVE 191

                       250       260       270
                ....*....|....*....|....*....|
gi 19923092 261 LKMYEGAYHVLHKELPEvtNSVLHEINTWV 290
Cdd:COG2267 192 LVLLPGARHELLNEPAR--EEVLAAILAWL 219
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 72-291 1.68e-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: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092    72 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDLLQHVNTVQK-------------DYPEV-------PVFLLGHSMGGAIS 128
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   129 ILA------AAERPTH--------FSGMILISPLILANPESASTLKVLAAKLLNFVLPNIslgRIDSSV-LSRNKSEVDL 193
Cdd:TIGR01607 157 LRLlellgkSNENNDKlnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTF---RISKKIrYEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   194 YNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRL--TLPFLLLQGSADRLCDSKGAYLLMESSPSQDKTLKMYEGAYHVL 271
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313

                         250       260
                  ....*....|....*....|
gi 19923092   272 HKElpEVTNSVLHEINTWVS 291
Cdd:TIGR01607 314 TIE--PGNEEVLKKIIEWIS 331
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 115-148 1.44e-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: 42.60  E-value: 1.44e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 19923092 115 PVFLLGHSMGGAISILAAAERPTHFSGMILISPL 148
Cdd:cd12809 172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-296 1.22e-106

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 311.43  E-value: 1.22e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   22 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLL 101
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  102 QHVNTVQKDYPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLIlaNPESASTLKVLAAKLLNFVLPNISLGRIDS 181
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  182 SVLSRNKSEVDLYNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSqDKTL 261
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 19923092  262 KMYEGAYHVLHKELPEVTNSVLHEINTWVSHRIAV 296
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRVKV 276
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-275 2.51e-91

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: 271.01  E-value: 2.51e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092    41 PKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLLQHVNTVQKDYPEVPVFLLG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   121 HSMGGAISILAAAERPTHFSGMILISPLILANPESASTLKVLAAKLLNFVLPNISL-GRIDSSVLSRNKSEVDLYNSDPL 199
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923092   200 iCHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSQDKTLKMYEGAYHVLHKEL 275
Cdd:pfam12146 163 -VHGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-290 2.24e-48

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 160.94  E-value: 2.24e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  21 HLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDL 100
Cdd:COG2267   7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092 101 LQHVNTVQKDyPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLILANPESASTLKVLAAkllnfvlpnislgrid 180
Cdd:COG2267  87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092 181 ssvlsrnksevdlynsdplichagvkvcfgiqllnavSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSqDKT 260
Cdd:COG2267 150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSP-DVE 191

                       250       260       270
                ....*....|....*....|....*....|
gi 19923092 261 LKMYEGAYHVLHKELPEvtNSVLHEINTWV 290
Cdd:COG2267 192 LVLLPGARHELLNEPAR--EEVLAAILAWL 219
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 23-293 1.53e-34

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 128.33  E-value: 1.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   23 VNADGQYLFCRYWKP-SGTPKALIFVSHGAGEHCGRYDE-LAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDL 100
Cdd:PLN02385  67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  101 LQHVNTVqKDYPEV---PVFLLGHSMGGAISILAAAERPTHFSGMILISPLI-----LANPESASTLKVLAAKLL--NFV 170
Cdd:PLN02385 147 IEHYSKI-KGNPEFrglPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCkiaddVVPPPLVLQILILLANLLpkAKL 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  171 LPNISLGriDSSVLSRNKSEVDLYNsdpLICHAG-VKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYL 249
Cdd:PLN02385 226 VPQKDLA--ELAFRDLKKRKMAEYN---VIAYKDkPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSKF 300

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 19923092  250 LMESSPSQDKTLKMYEGAYH-VLHKELPEVTNSVLHEINTWVSHR 293
Cdd:PLN02385 301 LYEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 27-295 1.57e-33

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 125.27  E-value: 1.57e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   27 GQYLFCRYWKPSGT--PKALIFVSHGAGEHCG-RYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLLQH 103
Cdd:PLN02298  42 GLSLFTRSWLPSSSspPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  104 VNTVQKD--YPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLI-----LANPESASTLKVLAAKLLNF--VLPNI 174
Cdd:PLN02298 122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCkisdkIRPPWPIPQILTFVARFLPTlaIVPTA 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  175 SLgrIDSSVLSRNKSEVDLYNsdPLICHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESS 254
Cdd:PLN02298 202 DL--LEKSVKVPAKKIIAKRN--PMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEA 277

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 19923092  255 PSQDKTLKMYEGAYH-VLHKELPEVTNSVLHEINTWVSHRIA 295
Cdd:PLN02298 278 KSEDKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCT 319
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 25-295 1.40e-32

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 123.85  E-value: 1.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   25 ADGQYLFCRYWKP-SGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLLQH 103
Cdd:PLN02652 118 ARRNALFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  104 VNTVQKDYPEVPVFLLGHSMGGAIsILAAAERPT---HFSGMILISPLILANPesASTLKVLAAKLLNFVLPNISLGRID 180
Cdd:PLN02652 198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGAN 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  181 SS--VLSRNKSEVDLYNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSQD 258
Cdd:PLN02652 275 KRgiPVSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRH 354

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 19923092  259 KTLKMYEGAYHVLHKElPEvTNSVLHEINTWVSHRIA 295
Cdd:PLN02652 355 KDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKRLD 389
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
39-284 2.84e-24

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 98.48  E-value: 2.84e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  39 GTPKALIFVsHGAGehCGRYD--ELAQMLKRLDMLVFAHDHVGHGQSEGErMVVSDFQVFVRDLLQHVNTVQKDYPEVpv 116
Cdd:COG1647  13 GGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYDKV-- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092 117 FLLGHSMGGAISILAAAERPtHFSGMILISPLILANPESAstlkvLAAKLLNFVLPNISLGRIDssvLSRNKSEVDLYNS 196
Cdd:COG1647  87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-----PLLPLLKYLARSLRGIGSD---IEDPEVAEYAYDR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092 197 DPLIChagvkvcfGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSQDKTLKMYEGAYHVLH--KE 274
Cdd:COG1647 158 TPLRA--------LAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKD 229

                       250
                ....*....|
gi 19923092 275 LPEVTNSVLH 284
Cdd:COG1647 230 REEVAEEILD 239
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 20-285 3.90e-20

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: 86.59  E-value: 3.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  20 PHLVNADGQYLFCRYWKPSGTPkaLIFVsHGAGEHCGRYDELAQMLKRlDMLVFAHDHVGHGQSEGERMVVSdFQVFVRD 99
Cdd:COG0596   4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYT-LDDLADD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092 100 LLQHVNTVQKDypevPVFLLGHSMGGAISILAAAERPTHFSGMILISPLIlanpesastlKVLAAKLLNFVLPNISLGRi 179
Cdd:COG0596  79 LAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL----------AALAEPLRRPGLAPEALAA- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092 180 dssvlsrnksevdlynsdplichagvkvcfgiqLLNAVSR--VERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPsq 257
Cdd:COG0596 144 ---------------------------------LLRALARtdLRERLARITVPTLVIWGEKDPIVPPALARRLAELLP-- 188

                       250       260
                ....*....|....*....|....*...
gi 19923092 258 DKTLKMYEGAYHVLHKELPEVTNSVLHE 285
Cdd:COG0596 189 NAELVVLPGAGHFPPLEQPEAFAAALRD 216
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 13-270 2.09e-18

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 82.66  E-value: 2.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  13 NVPYQDLpHLVNADGQYLFCRYWKPSGTPKAL--IFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGE-RMV 89
Cdd:COG1073   7 KVNKEDV-TFKSRDGIKLAGDLYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEpREE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  90 VS----DFQVFVRDLLQhvntvQKDYPEVPVFLLGHSMGGAISILAAAERPtHFSGMILISPLILANPESASTLKVLAAK 165
Cdd:COG1073  86 GSperrDARAAVDYLRT-----LPGVDPERIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092 166 LLNFV--LPNISLGridssvlsrnksevdlynsdplichagvkvcfgiQLLNAVSRVERAMPRLTLPFLLLQGSADRLCD 243
Cdd:COG1073 160 YLPGVpyLPNVRLA----------------------------------SLLNDEFDPLAKIEKISRPLLFIHGEKDEAVP 205

                       250       260
                ....*....|....*....|....*..
gi 19923092 244 SKGAYLLMESSPsQDKTLKMYEGAYHV 270
Cdd:COG1073 206 FYMSEDLYEAAA-EPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
24-294 2.22e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 73.90  E-value: 2.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  24 NADGQYLFCRYWKPSGTPKA-LIFVSHGAGEH-CGRYDELAQMLKRLDMLVFAHDHVGHGQSEGE--RMVVSDFQVFVRD 99
Cdd:COG1506   4 SADGTTLPGWLYLPADGKKYpVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDwgGDEVDDVLAAIDY 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092 100 LLQhvntvQKDYPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLilanpesastlkvlaakllnfvlpnISLGRI 179
Cdd:COG1506  84 LAA-----RPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGV-------------------------SDLRSY 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092 180 DSSVLSRNKSEVDLYNSDPlichagvkvcfgiQLLNAVSRVERAmPRLTLPFLLLQGSADRLCDSKGAYLLME--SSPSQ 257
Cdd:COG1506 134 YGTTREYTERLMGGPWEDP-------------EAYAARSPLAYA-DKLKTPLLLIHGEADDRVPPEQAERLYEalKKAGK 199

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 19923092 258 DKTLKMYEGAYHVLHKelpEVTNSVLHEINTWVSHRI 294
Cdd:COG1506 200 PVELLVYPGEGHGFSG---AGAPDYLERILDFLDRHL 233
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 42-274 1.46e-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: 63.29  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092    42 KALIFVsHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGeRMVVSDFQVFvrDLLQHVNTVQKDYPEVPVFLLGH 121
Cdd:pfam00561   1 PPVLLL-HGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   122 SMGGAISILAAAERPTHFSGMILISPlILANPESASTLKVLAAKLLNFV------LPNISLGRI-----------DSSVL 184
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGA-LDPPHELDEADRFILALFPGFFdgfvadFAPNPLGRLvakllallllrLRLLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   185 SRNKSEVDLYNSDPLIchAGVKVCFGIQLLNAVSRVERA--MPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSqdKTLK 262
Cdd:pfam00561 156 ALPLLNKRFPSGDYAL--AKSLVTGALLFIETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPN--ARLV 231

                         250
                  ....*....|..
gi 19923092   263 MYEGAYHVLHKE 274
Cdd:pfam00561 232 VIPDAGHFAFLE 243
YpfH COG0400
Predicted esterase [General function prediction only];
38-163 2.61e-07

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 50.29  E-value: 2.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  38 SGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFA------HDHVGHG----QSEGERMVVSDFQVFVRDLLQHVNTV 107
Cdd:COG0400   1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDEL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19923092 108 QKDY--PEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLILANPESASTLKVLA 163
Cdd:COG0400  81 EARYgiDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAALA 138
PLN02578 PLN02578
hydrolase
 39-291 1.08e-06

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 49.45  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   39 GTPKALIfvsHGAGE---HCgRYD--ELAQMLKrldmlVFAHDHVGHGQSEgERMVVSDFQVFVRDLLQHVNTVQKDype 113
Cdd:PLN02578  86 GLPIVLI---HGFGAsafHW-RYNipELAKKYK-----VYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE--- 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  114 vPVFLLGHSMGGAISILAAAERPTHFSGMILI----------SPLILANPESASTLKVLAAKLLNFVLPNISLG------ 177
Cdd:PLN02578 153 -PAVLVGNSLGGFTALSTAVGYPELVAGVALLnsagqfgsesREKEEAIVVEETVLTRFVVKPLKEWFQRVVLGflfwqa 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  178 ----RIDSSVLS--RNKSEVDLY--------NSDPlicHAGvKVCFGIQ---LLNAvSR--VERAMPRLTLPFLLLQGSA 238
Cdd:PLN02578 232 kqpsRIESVLKSvyKDKSNVDDYlvesitepAADP---NAG-EVYYRLMsrfLFNQ-SRytLDSLLSKLSCPLLLLWGDL 306

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19923092  239 DRLCDSKGAYLLMESSPsqDKTLKMYEgAYHVLHKELPEVTNSVLHEintWVS 291
Cdd:PLN02578 307 DPWVGPAKAEKIKAFYP--DTTLVNLQ-AGHCPHDEVPEQVNKALLE---WLS 353
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 44-272 1.66e-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: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092    44 LIFVsHGAGEHcgrYDELAQMLKRlDMLVFAHDHVGHGQSEGERMVVSDfqvfVRDLLQHVNTVQKDYPevpVFLLGHSM 123
Cdd:pfam12697   1 VVLV-HGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   124 GGAISILAAAERPTHfsgMILISPLILANPESASTLKVLAAKLLNFVLPNISLGRIDSSVLSRNKSEVDLYNsdplicha 203
Cdd:pfam12697  69 GGAVALAAAAAALVV---GVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWA-------- 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19923092   204 gVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMEsspSQDKTLKMYEGAYHVLH 272
Cdd:pfam12697 138 -AALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPELAQRLLAA---LAGARLVVLPGAGHLPL 202
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 72-291 1.68e-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: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092    72 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDLLQHVNTVQK-------------DYPEV-------PVFLLGHSMGGAIS 128
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   129 ILA------AAERPTH--------FSGMILISPLILANPESASTLKVLAAKLLNFVLPNIslgRIDSSV-LSRNKSEVDL 193
Cdd:TIGR01607 157 LRLlellgkSNENNDKlnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTF---RISKKIrYEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   194 YNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRL--TLPFLLLQGSADRLCDSKGAYLLMESSPSQDKTLKMYEGAYHVL 271
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313

                         250       260
                  ....*....|....*....|
gi 19923092   272 HKElpEVTNSVLHEINTWVS 291
Cdd:TIGR01607 314 TIE--PGNEEVLKKIIEWIS 331
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
21-136 1.28e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 45.34  E-value: 1.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  21 HLVNADGQYLFCRYWKPSGT-PKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFA---HDHVGHGQSEGE---RMVVSDF 93
Cdd:COG0412   7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDP 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 19923092  94 QVFVRDLLQHVNTVQKDyPEV---PVFLLGHSMGGAISILAAAERP 136
Cdd:COG0412  87 ELLAADLRAALDWLKAQ-PEVdagRVGVVGFCFGGGLALLAAARGP 131
PRK10749 PRK10749
lysophospholipase L2; Provisional
 57-148 1.48e-05

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 45.76  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   57 RYDELAQMLKRLDMLVFAHDHVGHGQS-----EGERMVVSDFQVFVRDL----LQHVNTvqkdYPEVPVFLLGHSMGGAI 127
Cdd:PRK10749  69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLaafwQQEIQP----GPYRKRYALAHSMGGAI 144

                         90       100
                 ....*....|....*....|.
gi 19923092  128 SILAAAERPTHFSGMILISPL 148
Cdd:PRK10749 145 LTLFLQRHPGVFDAIALCAPM 165
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 33-147 9.37e-05

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 43.39  E-value: 9.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   33 RYWK-PSGTPKALIFVsHG-AGEH---CGRYDELAqmlkrLDMLVFAHDHVGHGQSeGERMVVSDFQVFVRDLLQHVNTV 107
Cdd:PRK14875 122 RYLRlGEGDGTPVVLI-HGfGGDLnnwLFNHAALA-----AGRPVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAL 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 19923092  108 QKDypevPVFLLGHSMGGAISILAAAERPTHFSGMILISP 147
Cdd:PRK14875 195 GIE----RAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 115-148 1.44e-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: 42.60  E-value: 1.44e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 19923092 115 PVFLLGHSMGGAISILAAAERPTHFSGMILISPL 148
Cdd:cd12809 172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
118-147 1.64e-04

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 42.28  E-value: 1.64e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 19923092 118 LLGHSMGGAISILAAAERPTHFSGMILISP 147
Cdd:COG2819 134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 99-134 4.73e-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: 40.92  E-value: 4.73e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 19923092  99 DLLQHVNTVQKDYPEVPVFLLGHSMGGAISILAAAE 134
Cdd:cd00519 113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
COG4099 COG4099
Predicted peptidase [General function prediction only];
44-160 5.63e-04

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 40.72  E-value: 5.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  44 LIFVSHGAGEhcgRYDELAQML-------------KRLDMLVFAhdhvghGQ-SEGERMVVSDFQVFVRDLLQHVntvQK 109
Cdd:COG4099  51 LVLFLHGAGE---RGTDNEKQLthgapkfinpenqAKFPAIVLA------PQcPEDDYWSDTKALDAVLALLDDL---IA 118

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 19923092 110 DYPEVP--VFLLGHSMGGAISILAAAERPTHFSGMILISPliLANPESASTLK 160
Cdd:COG4099 119 EYRIDPdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 98-134 1.25e-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: 1.25e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 19923092  98 RDLLQHVNTVQKDYPEVPVFLLGHSMGGAISILAAAE 134
Cdd:cd00741  12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 77-156 1.35e-03

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 39.37  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092    77 HVGHGQSEGERMvvSDFQVFVRD-LLQhvnTVQKDYPEVPVF--LLGHSMGGAISILAAAERPTHFSGMILISPliLANP 153
Cdd:pfam00756  75 DRGLNATEGPGA--YAYETFLTQeLPP---LLDANFPTAPDGraLAGQSMGGLGALYLALKYPDLFGSVSSFSP--ILNP 147


                  ...
gi 19923092   154 ESA 156
Cdd:pfam00756 148 SNS 150
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 37-147 1.63e-03

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 37.50  E-value: 1.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  37 PSGTPKALIFVsHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSegermvvsdFQVFVRDLLQHVNTVQKDYPEVPV 116
Cdd:COG1075   1 YAATRYPVVLV-HGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGS---------IEDSAEQLAAFVDAVLAATGAEKV 70

                        90       100       110
                ....*....|....*....|....*....|...
gi 19923092 117 FLLGHSMGGAIS--ILAAAERPTHFSGMILISP 147
Cdd:COG1075  71 DLVGHSMGGLVAryYLKRLGGAAKVARVVTLGT 103
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
37-269 4.39e-03

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 38.16  E-value: 4.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092  37 PSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGH-----GQSEGERMVVSDFQVF------VRDLLQHVN 105
Cdd:COG4188  57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaadlSAALDGLADALDPEELwerpldLSFVLDQLL 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092 106 TVQKDYPEVP-------VFLLGHSMGGAISILAAAERPthfsgmilisplilanpeSASTLKVLAAKLLNFVLPNISLGR 178
Cdd:COG4188 137 ALNKSDPPLAgrldldrIGVIGHSLGGYTALALAGARL------------------DFAALRQYCGKNPDLQCRALDLPR 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092 179 IDSSVlsrnksevdlynSDPLIcHAGVkvcfgiqLLNAVSR---VERAMPRLTLPFLLLQGSADRlcDSKGAY---LLME 252
Cdd:COG4188 199 LAYDL------------RDPRI-KAVV-------ALAPGGSglfGEEGLAAITIPVLLVAGSADD--VTPAPDeqiRPFD 256

                       250
                ....*....|....*..
gi 19923092 253 SSPSQDKTLKMYEGAYH 269
Cdd:COG4188 257 LLPGADKYLLTLEGATH 273
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
4-138 6.02e-03

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 37.82  E-value: 6.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923092   4 ASSPRRTPQnVPYQ----DLPhlvnaDGQYLFCRYWKPSGTPKALIFVSHG-AGEHCGRY-DELAQMLKRLDMLVFAHDH 77
Cdd:COG0429  25 PSLFRRRPA-LPYRrerlELP-----DGDFVDLDWSDPPAPSKPLVVLLHGlEGSSDSHYaRGLARALYARGWDVVRLNF 98

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19923092  78 VGHGqseGE--RMVVS----DFQvfvrDLLQHVNTVQKDYPEVPVFLLGHSMGGAISILAAAERPTH 138
Cdd:COG0429  99 RGCG---GEpnLLPRLyhsgDTE----DLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGEQGDD 158
 
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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