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Conserved domains on  [gi|1868363335|ref|XP_035304764|]
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monoglyceride lipase isoform X1 [Cricetulus griseus]

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, ...
 32-304 4.24e-105

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: 307.97  E-value: 4.24e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  32 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 111
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 112 QHVDTIQKDYPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLVlaNPESASTFKVLAAKVLNLVLPNMSLGRIDS 191
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 192 SVLSRNKSEVDIYDSDPLICRAGVKVCFGIQLLNAVSRVERAMPKLTLPFLLLQGSADRLCDSKGAYLLMESSRSqDKTL 271
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1868363335 272 KMYEGAYHVLHKELPEVTKSVLHEINMWLSHRT 304
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 32-304 4.24e-105

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 307.97  E-value: 4.24e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  32 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 111
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 112 QHVDTIQKDYPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLVlaNPESASTFKVLAAKVLNLVLPNMSLGRIDS 191
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 192 SVLSRNKSEVDIYDSDPLICRAGVKVCFGIQLLNAVSRVERAMPKLTLPFLLLQGSADRLCDSKGAYLLMESSRSqDKTL 271
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1868363335 272 KMYEGAYHVLHKELPEVTKSVLHEINMWLSHRT 304
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 51-285 6.18e-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: 6.18e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  51 PKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPGVPVFLLG 130
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 131 HSMGGAISILAAAERPAHFSGMVLISPLVLANPESASTFKVLAAKVLNLVLPNMSL-GRIDSSVLSRNKSEVDIYDSDPL 209
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1868363335 210 ICRaGVKVCFGIQLLNAVSRVERAMPKLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHKEL 285
Cdd:pfam12146 163 VHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
31-300 5.25e-50

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 165.56  E-value: 5.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  31 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDV 110
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 111 LQHVDTIQKDyPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLVLANPESASTFKVLAAkvlnlvlpnmslgrid 190
Cdd:COG2267    87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 191 ssvlsrnksevdiydsdplicragvkvcfgiqllnavSRVERAMPKLTLPFLLLQGSADRLCDSKGAYLLMEsSRSQDKT 270
Cdd:COG2267   150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAA-RLSPDVE 191

                         250       260       270
                  ....*....|....*....|....*....|
gi 1868363335 271 LKMYEGAYHVLHKELPEvtKSVLHEINMWL 300
Cdd:COG2267   192 LVLLPGARHELLNEPAR--EEVLAAILAWL 219
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 79-301 2.60e-05

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: 45.16  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  79 GMMVFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPGV-------PVFLLGHSMGG 135
Cdd:TIGR01607  74 GYSVYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGG 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 136 AISI----LAAAERPAH----------FSGMVLISplVLANPESAStFKVLAAKVLNLVLPNMSLGRIDSSV-LSRNKSE 200
Cdd:TIGR01607 154 NIALrlleLLGKSNENNdklnikgcisLSGMISIK--SVGSDDSFK-FKYFYLPVMNFMSRVFPTFRISKKIrYEKSPYV 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 201 VDIYDSDPLICRAGVKVCFGIQLLNAVSRVERAM---PKlTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGA 277
Cdd:TIGR01607 231 NDIIKFDKFRYDGGITFNLASELIKATDTLDCDIdyiPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309

                         250       260
                  ....*....|....*....|....
gi 1868363335 278 YHVLHKElpEVTKSVLHEINMWLS 301
Cdd:TIGR01607 310 DHVITIE--PGNEEVLKKIIEWIS 331
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 125-158 1.35e-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: 1.35e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1868363335 125 PVFLLGHSMGGAISILAAAERPAHFSGMVLISPL 158
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 32-304 4.24e-105

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 307.97  E-value: 4.24e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  32 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 111
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 112 QHVDTIQKDYPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLVlaNPESASTFKVLAAKVLNLVLPNMSLGRIDS 191
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 192 SVLSRNKSEVDIYDSDPLICRAGVKVCFGIQLLNAVSRVERAMPKLTLPFLLLQGSADRLCDSKGAYLLMESSRSqDKTL 271
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1868363335 272 KMYEGAYHVLHKELPEVTKSVLHEINMWLSHRT 304
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 51-285 6.18e-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: 6.18e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  51 PKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPGVPVFLLG 130
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 131 HSMGGAISILAAAERPAHFSGMVLISPLVLANPESASTFKVLAAKVLNLVLPNMSL-GRIDSSVLSRNKSEVDIYDSDPL 209
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1868363335 210 ICRaGVKVCFGIQLLNAVSRVERAMPKLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHKEL 285
Cdd:pfam12146 163 VHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
31-300 5.25e-50

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 165.56  E-value: 5.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  31 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDV 110
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 111 LQHVDTIQKDyPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLVLANPESASTFKVLAAkvlnlvlpnmslgrid 190
Cdd:COG2267    87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 191 ssvlsrnksevdiydsdplicragvkvcfgiqllnavSRVERAMPKLTLPFLLLQGSADRLCDSKGAYLLMEsSRSQDKT 270
Cdd:COG2267   150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAA-RLSPDVE 191

                         250       260       270
                  ....*....|....*....|....*....|
gi 1868363335 271 LKMYEGAYHVLHKELPEvtKSVLHEINMWL 300
Cdd:COG2267   192 LVLLPGARHELLNEPAR--EEVLAAILAWL 219
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 33-303 2.35e-38

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 138.73  E-value: 2.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  33 VNADGQYLFCRYWKP-TGTPKALIFVSHGAGEHCGRYDE-LAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDV 110
Cdd:PLN02385   67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 111 LQHVDTIQ--KDYPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLV-----LANPESASTFKVLAAKVL---NLV 180
Cdd:PLN02385  147 IEHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCkiaddVVPPPLVLQILILLANLLpkaKLV 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 181 lPNMSLGRI---DSSVLSRNKSEVDIYDSDPLICRAgvkvcfgIQLLNAVSRVERAMPKLTLPFLLLQGSADRLCDSKGA 257
Cdd:PLN02385  227 -PQKDLAELafrDLKKRKMAEYNVIAYKDKPRLRTA-------VELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVS 298

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1868363335 258 YLLMESSRSQDKTLKMYEGAYH-VLHKELPEVTKSVLHEINMWLSHR 303
Cdd:PLN02385  299 KFLYEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 37-310 1.61e-35

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 130.67  E-value: 1.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  37 GQYLFCRYWKPTGT--PKALIFVSHGAGEHCG-RYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQH 113
Cdd:PLN02298   42 GLSLFTRSWLPSSSspPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 114 VDTIQKD--YPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLV-----LANPESASTFKVLAAKVLNL--VLPNM 184
Cdd:PLN02298  122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCkisdkIRPPWPIPQILTFVARFLPTlaIVPTA 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 185 SLgrIDSSVlsRNKSEVDIYDSDPLICRAGVKVCFGIQLLNAVSRVERAMPKLTLPFLLLQGSADRLCDSKGAYLLMESS 264
Cdd:PLN02298  202 DL--LEKSV--KVPAKKIIAKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEA 277

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1868363335 265 RSQDKTLKMYEGAYH-VLHKELPEVTKSVLHEINMWLSHRTAATGAG 310
Cdd:PLN02298  278 KSEDKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKATP 324
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 35-303 1.74e-35

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 132.32  E-value: 1.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  35 ADGQYLFCRYWKP-TGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQH 113
Cdd:PLN02652  118 ARRNALFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 114 VDTIQKDYPGVPVFLLGHSMGGAIsILAAAERP---AHFSGMVLISPLVLANPESASTFKVlaAKVLNLVLPNMSLGRID 190
Cdd:PLN02652  198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPsieDKLEGIVLTSPALRVKPAHPIVGAV--APIFSLVAPRFQFKGAN 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 191 SS--VLSRNKSEVDIYDSDPLICRAGVKVCFGIQLLNAVSRVERAMPKLTLPFLLLQGSADRLCDSKGAYLLMESSRSQD 268
Cdd:PLN02652  275 KRgiPVSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRH 354

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1868363335 269 KTLKMYEGAYHVLHKElPEvTKSVLHEINMWLSHR 303
Cdd:PLN02652  355 KDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKR 387
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
49-294 9.12e-25

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 100.02  E-value: 9.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  49 GTPKALIFVsHGAGehCGRYD--ELAQMLKGLGMMVFAHDHVGHGQSEGErMVVSDFQVFVRDVLQHVDTIQKDYPgvPV 126
Cdd:COG1647    13 GGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 127 FLLGHSMGGAISILAAAERPaHFSGMVLISPLVLANPESAstfkvLAAKVLNLVLPNMSLGRIDssvLSRNKSEVDIYDS 206
Cdd:COG1647    87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-----PLLPLLKYLARSLRGIGSD---IEDPEVAEYAYDR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 207 DPLICragvkvcfGIQLLNAVSRVERAMPKLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLH--KE 284
Cdd:COG1647   158 TPLRA--------LAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKD 229

                         250
                  ....*....|
gi 1868363335 285 LPEVTKSVLH 294
Cdd:COG1647   230 REEVAEEILD 239
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 30-295 4.61e-19

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 83.90  E-value: 4.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  30 PHLVNADGQYLFCRYWKPTGTPkaLIFVsHGAGEHCGRYDELAQMLKGlGMMVFAHDHVGHGQSEGERMVVSdFQVFVRD 109
Cdd:COG0596     4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYT-LDDLADD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 110 VLQHVDTIQKDypgvPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLVlanpesastfKVLAAkvlNLVLPNMSLGRI 189
Cdd:COG0596    79 LAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL----------AALAE---PLRRPGLAPEAL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 190 DSSVLSRNKSEvdiydsdplicragvkvcfgiqllnavsrVERAMPKLTLPFLLLQGSADRLCDSKGAYLLMEssRSQDK 269
Cdd:COG0596   142 AALLRALARTD-----------------------------LRERLARITVPTLVIWGEKDPIVPPALARRLAE--LLPNA 190

                         250       260
                  ....*....|....*....|....*.
gi 1868363335 270 TLKMYEGAYHVLHKELPEVTKSVLHE 295
Cdd:COG0596   191 ELVVLPGAGHFPPLEQPEAFAAALRD 216
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 23-280 1.11e-18

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 83.43  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  23 NVPYQDLpHLVNADGQYLFCRYWKPTGTPKAL--IFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVV 100
Cdd:COG1073     7 KVNKEDV-TFKSRDGIKLAGDLYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 101 SDFQvfVRDVLQHVDTIQKdYPGVP---VFLLGHSMGGAISILAAAERPaHFSGMVLISPlvLANPESASTFKVLAAKVL 177
Cdd:COG1073    86 GSPE--RRDARAAVDYLRT-LPGVDperIGLLGISLGGGYALNAAATDP-RVKAVILDSP--FTSLEDLAAQRAKEARGA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 178 NL----VLPNMSLGridssvlsrnksevdiydsdplicragvkvcfgiQLLNAVSRVERAMPKLTLPFLLLQGSADRLCD 253
Cdd:COG1073   160 YLpgvpYLPNVRLA----------------------------------SLLNDEFDPLAKIEKISRPLLFIHGEKDEAVP 205

                         250       260
                  ....*....|....*....|....*..
gi 1868363335 254 SKGAYLLMESSrSQDKTLKMYEGAYHV 280
Cdd:COG1073   206 FYMSEDLYEAA-AEPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
34-302 2.05e-17

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 79.68  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  34 NADGQYLFCRYWKPTGTPKA-LIFVSHGAGEH-CGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSdfqvfVRDVL 111
Cdd:COG1506     4 SADGTTLPGWLYLPADGKKYpVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDE-----VDDVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 112 QHVDTI--QKDYPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLVlanpesastfkvlaakvlnlvlpnmSLGRI 189
Cdd:COG1506    79 AAIDYLaaRPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS-------------------------DLRSY 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 190 DSSVLSRNKSEVDIYDSDPlicragvkvcfgiQLLNAVSRVERAmPKLTLPFLLLQGSADRLCDSKGAYLLME--SSRSQ 267
Cdd:COG1506   134 YGTTREYTERLMGGPWEDP-------------EAYAARSPLAYA-DKLKTPLLLIHGEADDRVPPEQAERLYEalKKAGK 199

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1868363335 268 DKTLKMYEGAYHVLHKelpEVTKSVLHEINMWLSH 302
Cdd:COG1506   200 PVELLVYPGEGHGFSG---AGAPDYLERILDFLDR 231
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 52-284 5.42e-11

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 61.75  E-value: 5.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  52 KALIFVsHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGeRMVVSDFQVFvrDVLQHVDTIQKDYPGVPVFLLGH 131
Cdd:pfam00561   1 PPVLLL-HGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 132 SMGGAISILAAAERPAHFSGMVLISPLVLAN-------------PESASTFKVLAAKVLNLVLPNMSLGRI---DSSVLS 195
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGALDPPHeldeadrfilalfPGFFDGFVADFAPNPLGRLVAKLLALLllrLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 196 RNKSEVDIYDSDPLIcrAGVKVCFGIQLLNAVSRVERA--MPKLTLPFLLLQGSADRLCDSKGAYLLmeSSRSQDKTLKM 273
Cdd:pfam00561 157 LPLLNKRFPSGDYAL--AKSLVTGALLFIETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKL--AQLFPNARLVV 232

                         250
                  ....*....|.
gi 1868363335 274 YEGAYHVLHKE 284
Cdd:pfam00561 233 IPDAGHFAFLE 243
PRK10749 PRK10749
lysophospholipase L2; Provisional
 67-296 2.52e-08

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 54.23  E-value: 2.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  67 RYDELAQMLKGLGMMVFAHDHVGHGQS-----EGERMVVSDFQVFVRDVLQHVDTIQKDYPGVPVFLLGHSMGGAISILA 141
Cdd:PRK10749   69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 142 AAERPAHFSGMVLISPL---VLANPESASTFKVLAAKVLNLVLPNMSLG---------RIDSSVLSRNKSE--VDIYDSD 207
Cdd:PRK10749  149 LQRHPGVFDAIALCAPMfgiVLPLPSWMARRILNWAEGHPRIRDGYAIGtgrwrplpfAINVLTHSRERYRrnLRFYADD 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 208 PLI---------CRAGVKVcfGIQLLnavsrveRAMPKLTLPFLLLQGSADRLCDskgayllmesSRSQDKTLKMYEGAY 278
Cdd:PRK10749  229 PELrvggptyhwVRESILA--GEQVL-------AGAGDITTPLLLLQAEEERVVD----------NRMHDRFCEARTAAG 289

                         250
                  ....*....|....*...
gi 1868363335 279 HVLHKELPEVTKSVLHEI 296
Cdd:PRK10749  290 HPCEGGKPLVIKGAYHEI 307
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 54-282 1.66e-07

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 50.94  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  54 LIFVsHGAGEHcgrYDELAQMLKGlGMMVFAHDHVGHGQSEGERMVVSDfqvfVRDVLQHVDTIQKDYPgvpVFLLGHSM 133
Cdd:pfam12697   1 VVLV-HGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 134 GGAIsILAAAERPAHFSgmVLISPLVLANPESASTFKVLAAKVLNLVLPNMSLGRIDSSVLSRNKSEVDIYDsdplicra 213
Cdd:pfam12697  69 GGAV-ALAAAAAALVVG--VLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWA-------- 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1868363335 214 gVKVCFGIQLLNAVSRVERAMPKLTLPFLLLQGSADRLCDskgAYLLMESSRSQDKTLKMYEGAYHVLH 282
Cdd:pfam12697 138 -AALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVP---ELAQRLLAALAGARLVVLPGAGHLPL 202
YpfH COG0400
Predicted esterase [General function prediction only];
48-164 4.24e-07

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 49.52  E-value: 4.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  48 TGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFA------HDHVGHG----QSEGERMVVSDFQVFVRDVLQHVDTI 117
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDEL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1868363335 118 QKDYpGVP---VFLLGHSMGGAISILAAAERPAHFSGMVLISPLVLANPE 164
Cdd:COG0400    81 EARY-GIDperIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEA 129
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
47-279 1.52e-06

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 48.95  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  47 PTGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGH-----GQSEGERMVVSDFQVF------VRDVLQHVD 115
Cdd:COG4188    57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaadlSAALDGLADALDPEELwerpldLSFVLDQLL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 116 TIQKDYPGVP-------VFLLGHSMGGAISILAAAERPahfsgmvlisplvlanpeSASTFKVLAAKVLNLVLPNMSLGR 188
Cdd:COG4188   137 ALNKSDPPLAgrldldrIGVIGHSLGGYTALALAGARL------------------DFAALRQYCGKNPDLQCRALDLPR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 189 IDSSVlsrnksevdiydSDPLIcRAGVkvcfgiqLLNAVSR---VERAMPKLTLPFLLLQGSADRlcDSKGAY---LLME 262
Cdd:COG4188   199 LAYDL------------RDPRI-KAVV-------ALAPGGSglfGEEGLAAITIPVLLVAGSADD--VTPAPDeqiRPFD 256

                         250
                  ....*....|....*..
gi 1868363335 263 SSRSQDKTLKMYEGAYH 279
Cdd:COG4188   257 LLPGADKYLLTLEGATH 273
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
31-146 1.59e-06

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 48.04  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  31 HLVNADGQYLFCRYWKPTGT-PKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFA---HDHVGHGQSEGE---RMVVSDF 103
Cdd:COG0412     7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDP 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1868363335 104 QVFVRDVLQHVDTIQKDyPGV---PVFLLGHSMGGAISILAAAERP 146
Cdd:COG0412    87 ELLAADLRAALDWLKAQ-PEVdagRVGVVGFCFGGGLALLAAARGP 131
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 43-157 1.75e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 48.79  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  43 RYWK-PTGTPKALIFVsHG-AGEH---CGRYDELAqmlkgLGMMVFAHDHVGHGQSeGERMVVSDFQVFVRDVLQHVDT- 116
Cdd:PRK14875  122 RYLRlGEGDGTPVVLI-HGfGGDLnnwLFNHAALA-----AGRPVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAl 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1868363335 117 -IQKdypgvpVFLLGHSMGGAISILAAAERPAHFSGMVLISP 157
Cdd:PRK14875  195 gIER------AHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
PLN02578 PLN02578
hydrolase
 49-301 8.39e-06

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 46.76  E-value: 8.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  49 GTPKALIfvsHGAGE---HCgRYD--ELAQMLKglgmmVFAHDHVGHGQSEgERMVVSDFQVFVRDVLQHVDTIQKDypg 123
Cdd:PLN02578   86 GLPIVLI---HGFGAsafHW-RYNipELAKKYK-----VYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE--- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 124 vPVFLLGHSMGGAISILAAAERPAHFSGMVLI----------SPLVLANPESASTFKVLAAKVLNLVLPNMSLG------ 187
Cdd:PLN02578  153 -PAVLVGNSLGGFTALSTAVGYPELVAGVALLnsagqfgsesREKEEAIVVEETVLTRFVVKPLKEWFQRVVLGflfwqa 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 188 ----RIDSSVLS--RNKSEVDIY--DS------DP--------LICRAgvkvcfgiqLLNAvSR--VERAMPKLTLPFLL 243
Cdd:PLN02578  232 kqpsRIESVLKSvyKDKSNVDDYlvESitepaaDPnagevyyrLMSRF---------LFNQ-SRytLDSLLSKLSCPLLL 301

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1868363335 244 LQGSADRLCDSKGAYLLMESsrSQDKTLKMYEgAYHVLHKELPEVTKSVLHEinmWLS 301
Cdd:PLN02578  302 LWGDLDPWVGPAKAEKIKAF--YPDTTLVNLQ-AGHCPHDEVPEQVNKALLE---WLS 353
COG4099 COG4099
Predicted peptidase [General function prediction only];
54-170 9.10e-06

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 46.11  E-value: 9.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  54 LIFVSHGAGEhcgRYDELAQMLKgLGMMVFAHDHVGHgqsegermvvsDFQVFV-----------------RDVLQHVDT 116
Cdd:COG4099    51 LVLFLHGAGE---RGTDNEKQLT-HGAPKFINPENQA-----------KFPAIVlapqcpeddywsdtkalDAVLALLDD 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1868363335 117 IQKDYPGVP--VFLLGHSMGGAISILAAAERPAHFSGMVLISPlvLANPESASTFK 170
Cdd:COG4099   116 LIAEYRIDPdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 79-301 2.60e-05

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: 45.16  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  79 GMMVFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPGV-------PVFLLGHSMGG 135
Cdd:TIGR01607  74 GYSVYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGG 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 136 AISI----LAAAERPAH----------FSGMVLISplVLANPESAStFKVLAAKVLNLVLPNMSLGRIDSSV-LSRNKSE 200
Cdd:TIGR01607 154 NIALrlleLLGKSNENNdklnikgcisLSGMISIK--SVGSDDSFK-FKYFYLPVMNFMSRVFPTFRISKKIrYEKSPYV 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335 201 VDIYDSDPLICRAGVKVCFGIQLLNAVSRVERAM---PKlTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGA 277
Cdd:TIGR01607 231 NDIIKFDKFRYDGGITFNLASELIKATDTLDCDIdyiPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309

                         250       260
                  ....*....|....*....|....
gi 1868363335 278 YHVLHKElpEVTKSVLHEINMWLS 301
Cdd:TIGR01607 310 DHVITIE--PGNEEVLKKIIEWIS 331
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 47-157 5.53e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 41.74  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  47 PTGTPKALIFVsHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSegermvvsdFQVFVRDVLQHVDTIQKDYPGVPV 126
Cdd:COG1075     1 YAATRYPVVLV-HGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGS---------IEDSAEQLAAFVDAVLAATGAEKV 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1868363335 127 FLLGHSMGGAIS--ILAAAERPAHFSGMVLISP 157
Cdd:COG1075    71 DLVGHSMGGLVAryYLKRLGGAAKVARVVTLGT 103
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 125-158 1.35e-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: 1.35e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1868363335 125 PVFLLGHSMGGAISILAAAERPAHFSGMVLISPL 158
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 109-144 1.46e-04

Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 42.46  E-value: 1.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1868363335 109 DVLQHVDTIQKDYPGVPVFLLGHSMGGAISILAAAE 144
Cdd:cd00519   113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
14-161 1.91e-04

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 42.44  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  14 ASSPRRTPQnVPYQ----DLPhlvnaDGQYLFCRYWKPTGTPKALIFVSHG-AGEHCGRY-DELAQMLKGLGMMVFAHDH 87
Cdd:COG0429    25 PSLFRRRPA-LPYRrerlELP-----DGDFVDLDWSDPPAPSKPLVVLLHGlEGSSDSHYaRGLARALYARGWDVVRLNF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  88 VGHGQSE---------GErmvVSDfqvfVRDVLQHvdtIQKDYPGVPVFLLGHSMGGAISILAAAERPAH---FSGMVLI 155
Cdd:COG0429    99 RGCGGEPnllprlyhsGD---TED----LVWVLAH---LRARYPYAPLYAVGFSLGGNLLLKYLGEQGDDappLKAAVAV 168


                  ....*..
gi 1868363335 156 S-PLVLA 161
Cdd:COG0429   169 SpPLDLA 175
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
117-157 3.22e-04

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 41.51  E-value: 3.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1868363335 117 IQKDYPGVPVF--LLGHSMGGAISILAAAERPAHFSGMVLISP 157
Cdd:COG2819   121 IDKRYRTDPERtgLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 108-144 3.83e-04

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: 40.18  E-value: 3.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1868363335 108 RDVLQHVDTIQKDYPGVPVFLLGHSMGGAISILAAAE 144
Cdd:cd00741    12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 87-159 1.24e-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: 39.75  E-value: 1.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1868363335  87 HVGHGQSEGERMvvSDFQVFVRDVLqhVDTIQKDYP--GVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLV 159
Cdd:pfam00756  75 DRGLNATEGPGA--YAYETFLTQEL--PPLLDANFPtaPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPIL 145
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 49-167 2.01e-03

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 39.22  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363335  49 GTPKALIFVSHGAG------EHCGRYDELAQmlkGLGMMV----------------FAHDHVGHGQSEgermvVSdfqvF 106
Cdd:COG3509    50 GAPLPLVVALHGCGgsaadfAAGTGLNALAD---REGFIVvypegtgrapgrcwnwFDGRDQRRGRDD-----VA----F 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1868363335 107 VRDVlqhVDTIQKDYPGVP--VFLLGHSMGGAISILAAAERPAHFSGMVLIS--PLVLANPESAS 167
Cdd:COG3509   118 IAAL---VDDLAARYGIDPkrVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACA 179
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
83-144 2.37e-03

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 38.97  E-value: 2.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1868363335  83 FAHDHVGHGQSEGerMVVSDFQVFVRDVLQH-VDTIQKDYPGVPVFLLGHSMGGAISILAAAE 144
Cdd:COG3675    48 AAQVPYPFAKTGG--KVHRGFYRALQSLRELlEDALRPLSPGKRLYVTGHSLGGALATLAAAD 108
Lipase_3 pfam01764
Lipase (class 3);
121-169 9.82e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 35.70  E-value: 9.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1868363335 121 YPGVPVFLLGHSMGGAISILAAAerpahfsgMVLISPLVLANPESASTF 169
Cdd:pfam01764  60 YPDYSIVVTGHSLGGALASLAAL--------DLVENGLRLSSRVTVVTF 100
PRK10673 PRK10673
esterase;
90-155 9.84e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 37.02  E-value: 9.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1868363335  90 HGQSEgeRMVVSDFQVFVRDVLQHVDTIQKDypgvPVFLLGHSMGGAISILAAAERPAHFSGMVLI 155
Cdd:PRK10673   53 HGLSP--RDPVMNYPAMAQDLLDTLDALQIE----KATFIGHSMGGKAVMALTALAPDRIDKLVAI 112
 
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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