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Conserved domains on  [gi|1868363337|ref|XP_035304765|]
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monoglyceride lipase isoform X2 [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, ...
 22-249 8.23e-83

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: 249.03  E-value: 8.23e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  22 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 101
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 102 QHVDTIQKDYPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLVlaNPESASTFKVLAAKVLNLVLPNMSLGRIDS 181
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 182 SVLSRNKSE---------------------------------------------GSADRLCDSKGAYLLMESSRSqDKTL 216
Cdd:PHA02857  163 ESVSRDMDEvykyqydplvnhekikagfasqvlkatnkvrkiipkiktpililqGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1868363337 217 KMYEGAYHVLHKELPEVTKSVLHEINMWLSHRT 249
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-249 8.23e-83

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 249.03  E-value: 8.23e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  22 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 101
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 102 QHVDTIQKDYPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLVlaNPESASTFKVLAAKVLNLVLPNMSLGRIDS 181
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 182 SVLSRNKSE---------------------------------------------GSADRLCDSKGAYLLMESSRSqDKTL 216
Cdd:PHA02857  163 ESVSRDMDEvykyqydplvnhekikagfasqvlkatnkvrkiipkiktpililqGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1868363337 217 KMYEGAYHVLHKELPEVTKSVLHEINMWLSHRT 249
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-230 6.92e-68

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: 209.76  E-value: 6.92e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  41 PKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPGVPVFLLG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 121 HSMGGAISILAAAERPAHFSGMVLISPLVLANPESASTFKVLAAKVLNLVLPNMSL-GRIDSSVLSRNKSE--------- 190
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVvaayaadpl 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1868363337 191 -----------------------------------GSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHKEL 230
Cdd:pfam12146 163 vhggisartlyelldagerllrraaaitvpllllhGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-245 4.86e-49

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 160.94  E-value: 4.86e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  21 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDV 100
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 101 LQHVDTIQKDyPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLVLANPESASTFKVLAAkvlnlVLPNMSLGRID 180
Cdd:COG2267    87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA-----LRLAEALARID 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1868363337 181 SSVL--SrnkseGSADRLCDSKGAYLLMEsSRSQDKTLKMYEGAYHVLHKELPEvtKSVLHEINMWL 245
Cdd:COG2267   161 VPVLvlH-----GGADRVVPPEAARRLAA-RLSPDVELVLLPGARHELLNEPAR--EEVLAAILAWL 219
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 115-148 1.20e-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: 1.20e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1868363337 115 PVFLLGHSMGGAISILAAAERPAHFSGMVLISPL 148
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 69-129 2.85e-03

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: 38.61  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  69 GMMVFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPGV-------PVFLLGHSMGG 125
Cdd:TIGR01607  74 GYSVYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGG 153


                  ....
gi 1868363337 126 AISI 129
Cdd:TIGR01607 154 NIAL 157
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-249 8.23e-83

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 249.03  E-value: 8.23e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  22 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 101
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 102 QHVDTIQKDYPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLVlaNPESASTFKVLAAKVLNLVLPNMSLGRIDS 181
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 182 SVLSRNKSE---------------------------------------------GSADRLCDSKGAYLLMESSRSqDKTL 216
Cdd:PHA02857  163 ESVSRDMDEvykyqydplvnhekikagfasqvlkatnkvrkiipkiktpililqGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1868363337 217 KMYEGAYHVLHKELPEVTKSVLHEINMWLSHRT 249
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-230 6.92e-68

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: 209.76  E-value: 6.92e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  41 PKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPGVPVFLLG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 121 HSMGGAISILAAAERPAHFSGMVLISPLVLANPESASTFKVLAAKVLNLVLPNMSL-GRIDSSVLSRNKSE--------- 190
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVvaayaadpl 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1868363337 191 -----------------------------------GSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHKEL 230
Cdd:pfam12146 163 vhggisartlyelldagerllrraaaitvpllllhGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-245 4.86e-49

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 160.94  E-value: 4.86e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  21 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDV 100
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 101 LQHVDTIQKDyPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLVLANPESASTFKVLAAkvlnlVLPNMSLGRID 180
Cdd:COG2267    87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA-----LRLAEALARID 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1868363337 181 SSVL--SrnkseGSADRLCDSKGAYLLMEsSRSQDKTLKMYEGAYHVLHKELPEvtKSVLHEINMWL 245
Cdd:COG2267   161 VPVLvlH-----GGADRVVPPEAARRLAA-RLSPDVELVLLPGARHELLNEPAR--EEVLAAILAWL 219
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 23-248 5.72e-28

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 109.46  E-value: 5.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  23 VNADGQYLFCRYWKP-TGTPKALIFVSHGAGEHCGRYDE-LAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDV 100
Cdd:PLN02385   67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 101 LQHVDTIQ--KDYPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLV-----LANPESASTFKVLAAKVL---NLV 170
Cdd:PLN02385  147 IEHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCkiaddVVPPPLVLQILILLANLLpkaKLV 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 171 lPNMSLG------------------------RIDSSV-LSRNKSE----------------GSADRLCDSKGAYLLMESS 209
Cdd:PLN02385  227 -PQKDLAelafrdlkkrkmaeynviaykdkpRLRTAVeLLRTTQEiemqleevslpllilhGEADKVTDPSVSKFLYEKA 305

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1868363337 210 RSQDKTLKMYEGAYH-VLHKELPEVTKSVLHEINMWLSHR 248
Cdd:PLN02385  306 SSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 27-255 1.10e-26

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 105.63  E-value: 1.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  27 GQYLFCRYWKPTGT--PKALIFVSHGAGEHCG-RYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQH 103
Cdd:PLN02298   42 GLSLFTRSWLPSSSspPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 104 VDTIQKD--YPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPL-------------------------VLANPESA 156
Cdd:PLN02298  122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMckisdkirppwpipqiltfvarflpTLAIVPTA 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 157 S----TFKVLAAKVLNLVLPN-----------MSLGRIDSSvLSRNKSE---------GSADRLCDSKGAYLLMESSRSQ 212
Cdd:PLN02298  202 DllekSVKVPAKKIIAKRNPMryngkprlgtvVELLRVTDY-LGKKLKDvsipfivlhGSADVVTDPDVSRALYEEAKSE 280

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1868363337 213 DKTLKMYEGAYH-VLHKELPEVTKSVLHEINMWLSHRTAATGAG 255
Cdd:PLN02298  281 DKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKATP 324
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 25-248 6.06e-23

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 96.50  E-value: 6.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  25 ADGQYLFCRYWKP-TGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQH 103
Cdd:PLN02652  118 ARRNALFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 104 VDTIQKDYPGVPVFLLGHSMGGAIsILAAAERP---AHFSGMVLISPLVLANPESASTFKVlaAKVLNLVLPNMSLG--- 177
Cdd:PLN02652  198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPsieDKLEGIVLTSPALRVKPAHPIVGAV--APIFSLVAPRFQFKgan 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 178 ------------------------------------RIDSSVLSRNKS--------EGSADRLCDSKGAYLLMESSRSQD 213
Cdd:PLN02652  275 krgipvsrdpaallakysdplvytgpirvrtgheilRISSYLTRNFKSvtvpfmvlHGTADRVTDPLASQDLYNEAASRH 354

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1868363337 214 KTLKMYEGAYHVLHKElPEvTKSVLHEINMWLSHR 248
Cdd:PLN02652  355 KDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKR 387
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 20-240 1.35e-18

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


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 81.59  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  20 PHLVNADGQYLFCRYWKPTGTPkaLIFVsHGAGEHCGRYDELAQMLKGlGMMVFAHDHVGHGQSEGERMVVSdFQVFVRD 99
Cdd:COG0596     4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYT-LDDLADD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 100 VLQHVDTIQKDypgvPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLVLANPES----ASTFKVLAAKVLNLVLPNMS 175
Cdd:COG0596    79 LAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPlrrpGLAPEALAALLRALARTDLR 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1868363337 176 --LGRID--SSVLSrnkseGSADRLCDSKGAYLLMEssRSQDKTLKMYEGAYHVLHKELPEVTKSVLHE 240
Cdd:COG0596   155 erLARITvpTLVIW-----GEKDPIVPPALARRLAE--LLPNAELVVLPGAGHFPPLEQPEAFAAALRD 216
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 13-225 4.17e-17

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 78.03  E-value: 4.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  13 NVPYQDLpHLVNADGQYLFCRYWKPTGTPKAL--IFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVV 90
Cdd:COG1073     7 KVNKEDV-TFKSRDGIKLAGDLYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  91 SDFQvfVRDVLQHVDTIQKdYPGVP---VFLLGHSMGGAISILAAAERPaHFSGMVLISPlvLANPESASTFKVLAAKVL 167
Cdd:COG1073    86 GSPE--RRDARAAVDYLRT-LPGVDperIGLLGISLGGGYALNAAATDP-RVKAVILDSP--FTSLEDLAAQRAKEARGA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1868363337 168 NL----VLPNMSLGR-IDSSVLSRNKSE----------GSADRLCDSKGAYLLMESSrSQDKTLKMYEGAYHV 225
Cdd:COG1073   160 YLpgvpYLPNVRLASlLNDEFDPLAKIEkisrpllfihGEKDEAVPFYMSEDLYEAA-AEPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
24-247 3.05e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 72.74  E-value: 3.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  24 NADGQYLFCRYWKPTGTPKA-LIFVSHGAGEH-CGRYDELAQMLKGLGMMVFAHDHVGHGQSEGERMVVSdfqvfVRDVL 101
Cdd:COG1506     4 SADGTTLPGWLYLPADGKKYpVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDE-----VDDVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 102 QHVDTI--QKDYPGVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPlvLANPESASTFKVLAAKVLNLVLPNMSLGRI 179
Cdd:COG1506    79 AAIDYLaaRPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG--VSDLRSYYGTTREYTERLMGGPWEDPEAYA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1868363337 180 DSSVLSRNKS--------EGSADRLCDSKGAYLLME--SSRSQDKTLKMYEGAYHVLHKelpEVTKSVLHEINMWLSH 247
Cdd:COG1506   157 ARSPLAYADKlktpllliHGEADDRVPPEQAERLYEalKKAGKPVELLVYPGEGHGFSG---AGAPDYLERILDFLDR 231
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
39-239 9.80e-15

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 71.51  E-value: 9.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  39 GTPKALIFVsHGAGehCGRYD--ELAQMLKGLGMMVFAHDHVGHGQSEGErMVVSDFQVFVRDVLQHVDTIQKDYPgvPV 116
Cdd:COG1647    13 GGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 117 FLLGHSMGGAISILAAAERPaHFSGMVLISPLVLANPESASTFKVL--AAKVLNLVLPNMSLGRIDSSVLSRNKSE---- 190
Cdd:COG1647    87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSAPLLPLLkyLARSLRGIGSDIEDPEVAEYAYDRTPLRalae 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1868363337 191 -----------------------GSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLH--KELPEVTKSVLH 239
Cdd:COG1647   166 lqrlirevrrdlpkitaptliiqSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKDREEVAEEILD 239
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 42-148 4.60e-10

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 58.28  E-value: 4.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  42 KALIFVsHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSEGeRMVVSDFQVFvrDVLQHVDTIQKDYPGVPVFLLGH 121
Cdd:pfam00561   1 PPVLLL-HGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGH 76

                          90       100
                  ....*....|....*....|....*..
gi 1868363337 122 SMGGAISILAAAERPAHFSGMVLISPL 148
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGAL 103
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 44-229 5.66e-08

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 51.71  E-value: 5.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  44 LIFVsHGAGEHcgrYDELAQMLKGlGMMVFAHDHVGHGQSEGERMVVSDfqvfVRDVLQHVDTIQKDYPgvpVFLLGHSM 123
Cdd:pfam12697   1 VVLV-HGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337 124 GGAISILAAAERPAHfsgMVLISPLVLANPESASTFKVLAAKVLNLVLPNMSLGRIDSSVLSRNKSEGSADRLCDSKGAY 203
Cdd:pfam12697  69 GGAVALAAAAAALVV---GVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAA 145

                         170       180
                  ....*....|....*....|....*.
gi 1868363337 204 LLMESSRSQDKTLKMYEGAYHVLHKE 229
Cdd:pfam12697 146 LLAALALLPLAAWRDLPVPVLVLAEE 171
PRK10749 PRK10749
lysophospholipase L2; Provisional
 57-148 1.30e-07

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 51.54  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  57 RYDELAQMLKGLGMMVFAHDHVGHGQS-----EGERMVVSDFQVFVRDVLQHVDTIQKDYPGVPVFLLGHSMGGAISILA 131
Cdd:PRK10749   69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLF 148

                          90
                  ....*....|....*..
gi 1868363337 132 AAERPAHFSGMVLISPL 148
Cdd:PRK10749  149 LQRHPGVFDAIALCAPM 165
YpfH COG0400
Predicted esterase [General function prediction only];
38-154 3.96e-07

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 49.14  E-value: 3.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  38 TGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFA------HDHVGHG----QSEGERMVVSDFQVFVRDVLQHVDTI 107
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDEL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1868363337 108 QKDYpGVP---VFLLGHSMGGAISILAAAERPAHFSGMVLISPLVLANPE 154
Cdd:COG0400    81 EARY-GIDperIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEA 129
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
21-227 7.00e-07

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 48.81  E-value: 7.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  21 HLVNADGQYLFCRYWKPTGT-PKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFA---HDHVGHGQSEGE---RMVVSDF 93
Cdd:COG0412     7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  94 QVFVRDVLQHVDTIQKDyPGV---PVFLLGHSMGGAISILAAAERPAhFSGMVLISPLVLANPESASTFKVlAAKVLNLV 170
Cdd:COG0412    87 ELLAADLRAALDWLKAQ-PEVdagRVGVVGFCFGGGLALLAAARGPD-LAAAVSFYGGLPADDLLDLAARI-KAPVLLLY 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1868363337 171 lpnmslgridssvlsrnkseGSADRLCDSKGAYLLME--SSRSQDKTLKMYEGAYHVLH 227
Cdd:COG0412   164 --------------------GEKDPLVPPEQVAALEAalAAAGVDVELHVYPGAGHGFT 202
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 33-147 1.33e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 48.79  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  33 RYWK-PTGTPKALIFVsHG-AGEH---CGRYDELAqmlkgLGMMVFAHDHVGHGQSeGERMVVSDFQVFVRDVLQHVDT- 106
Cdd:PRK14875  122 RYLRlGEGDGTPVVLI-HGfGGDLnnwLFNHAALA-----AGRPVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAl 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1868363337 107 -IQKdypgvpVFLLGHSMGGAISILAAAERPAHFSGMVLISP 147
Cdd:PRK14875  195 gIER------AHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
COG4099 COG4099
Predicted peptidase [General function prediction only];
44-160 9.53e-06

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 45.34  E-value: 9.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  44 LIFVSHGAGEhcgRYDELAQMLKgLGMMVFAHDHVGHgqsegermvvsDFQVFV-----------------RDVLQHVDT 106
Cdd:COG4099    51 LVLFLHGAGE---RGTDNEKQLT-HGAPKFINPENQA-----------KFPAIVlapqcpeddywsdtkalDAVLALLDD 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1868363337 107 IQKDYPGVP--VFLLGHSMGGAISILAAAERPAHFSGMVLISPlvLANPESASTFK 160
Cdd:COG4099   116 LIAEYRIDPdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
37-136 1.21e-05

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 45.48  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  37 PTGTPKALIFVSHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGH-----GQSEGERMVVSDFQVF------VRDVLQHVD 105
Cdd:COG4188    57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaadlSAALDGLADALDPEELwerpldLSFVLDQLL 136

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1868363337 106 TIQKDYPGVP-------VFLLGHSMGGAISILAAAERP 136
Cdd:COG4188   137 ALNKSDPPLAgrldldrIGVIGHSLGGYTALALAGARL 174
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 37-147 7.14e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 40.97  E-value: 7.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  37 PTGTPKALIFVsHGAGEHCGRYDELAQMLKGLGMMVFAHDHVGHGQSegermvvsdFQVFVRDVLQHVDTIQKDYPGVPV 116
Cdd:COG1075     1 YAATRYPVVLV-HGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGS---------IEDSAEQLAAFVDAVLAATGAEKV 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1868363337 117 FLLGHSMGGAIS--ILAAAERPAHFSGMVLISP 147
Cdd:COG1075    71 DLVGHSMGGLVAryYLKRLGGAAKVARVVTLGT 103
PLN02578 PLN02578
hydrolase
 39-147 8.96e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 42.91  E-value: 8.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  39 GTPKALIfvsHGAGE---HCgRYD--ELAQMLKglgmmVFAHDHVGHGQSEgERMVVSDFQVFVRDVLQHVDTIQKDypg 113
Cdd:PLN02578   86 GLPIVLI---HGFGAsafHW-RYNipELAKKYK-----VYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE--- 152

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1868363337 114 vPVFLLGHSMGGAISILAAAERPAHFSGMVLISP 147
Cdd:PLN02578  153 -PAVLVGNSLGGFTALSTAVGYPELVAGVALLNS 185
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 115-148 1.20e-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: 1.20e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1868363337 115 PVFLLGHSMGGAISILAAAERPAHFSGMVLISPL 148
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 99-134 1.33e-04

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


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 42.08  E-value: 1.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1868363337  99 DVLQHVDTIQKDYPGVPVFLLGHSMGGAISILAAAE 134
Cdd:cd00519   113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
4-151 1.68e-04

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 42.05  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337   4 ASSPRRTPQnVPYQ----DLPhlvnaDGQYLFCRYWKPTGTPKALIFVSHG-AGEHCGRY-DELAQMLKGLGMMVFAHDH 77
Cdd:COG0429    25 PSLFRRRPA-LPYRrerlELP-----DGDFVDLDWSDPPAPSKPLVVLLHGlEGSSDSHYaRGLARALYARGWDVVRLNF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  78 VGHGQSE---------GErmvVSDfqvfVRDVLQHvdtIQKDYPGVPVFLLGHSMGGAISILAAAERPAH---FSGMVLI 145
Cdd:COG0429    99 RGCGGEPnllprlyhsGD---TED----LVWVLAH---LRARYPYAPLYAVGFSLGGNLLLKYLGEQGDDappLKAAVAV 168


                  ....*..
gi 1868363337 146 S-PLVLA 151
Cdd:COG0429   169 SpPLDLA 175
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
107-147 2.56e-04

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 41.12  E-value: 2.56e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1868363337 107 IQKDYPGVPVF--LLGHSMGGAISILAAAERPAHFSGMVLISP 147
Cdd:COG2819   121 IDKRYRTDPERtgLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 98-134 4.21e-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: 39.79  E-value: 4.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1868363337  98 RDVLQHVDTIQKDYPGVPVFLLGHSMGGAISILAAAE 134
Cdd:cd00741    12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 92-149 1.31e-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: 38.98  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  92 DFQVFVRDVLqhVDTIQKDYP--GVPVFLLGHSMGGAISILAAAERPAHFSGMVLISPLV 149
Cdd:pfam00756  88 AYETFLTQEL--PPLLDANFPtaPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPIL 145
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
73-134 2.26e-03

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 38.58  E-value: 2.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1868363337  73 FAHDHVGHGQSEGerMVVSDFQVFVRDVLQH-VDTIQKDYPGVPVFLLGHSMGGAISILAAAE 134
Cdd:COG3675    48 AAQVPYPFAKTGG--KVHRGFYRALQSLRELlEDALRPLSPGKRLYVTGHSLGGALATLAAAD 108
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 69-129 2.85e-03

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: 38.61  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  69 GMMVFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPGV-------PVFLLGHSMGG 125
Cdd:TIGR01607  74 GYSVYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGG 153


                  ....
gi 1868363337 126 AISI 129
Cdd:TIGR01607 154 NIAL 157
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 39-157 2.91e-03

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 38.06  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868363337  39 GTPKALIFVSHGAG------EHCGRYDELAQmlkGLGMMV----------------FAHDHVGHGQSEgermvVSdfqvF 96
Cdd:COG3509    50 GAPLPLVVALHGCGgsaadfAAGTGLNALAD---REGFIVvypegtgrapgrcwnwFDGRDQRRGRDD-----VA----F 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1868363337  97 VRDVlqhVDTIQKDYPGVP--VFLLGHSMGGAISILAAAERPAHFSGMVLIS--PLVLANPESAS 157
Cdd:COG3509   118 IAAL---VDDLAARYGIDPkrVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACA 179
PRK10673 PRK10673
esterase;
80-145 8.17e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 36.63  E-value: 8.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1868363337  80 HGQSEgeRMVVSDFQVFVRDVLQHVDTIQKDypgvPVFLLGHSMGGAISILAAAERPAHFSGMVLI 145
Cdd:PRK10673   53 HGLSP--RDPVMNYPAMAQDLLDTLDALQIE----KATFIGHSMGGKAVMALTALAPDRIDKLVAI 112
Lipase_3 pfam01764
Lipase (class 3);
111-159 8.51e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 35.70  E-value: 8.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1868363337 111 YPGVPVFLLGHSMGGAISILAAAerpahfsgMVLISPLVLANPESASTF 159
Cdd:pfam01764  60 YPDYSIVVTGHSLGGALASLAAL--------DLVENGLRLSSRVTVVTF 100
 
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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