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Conserved domains on  [gi|6005786|ref|NP_009214|]
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monoglyceride lipase isoform 1 [Homo sapiens]

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 4.84e-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: 4.84e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    32 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 111
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   112 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVlaNPESATTFKVLAAKVLNLVLPNLSLGPIDS 191
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   192 SVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSqDKTL 271
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 6005786   272 KIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 304
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 32-304 4.84e-105

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 307.97  E-value: 4.84e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    32 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 111
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   112 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVlaNPESATTFKVLAAKVLNLVLPNLSLGPIDS 191
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   192 SVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSqDKTL 271
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 6005786   272 KIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 304
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 51-285 1.33e-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: 274.86  E-value: 1.33e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786     51 PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLG 130
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    131 HSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSL-GPIDSSVLSRNKTEVDIYNSDPL 209
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005786    210 ICRaGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKEL 285
Cdd:pfam12146 163 VHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
31-302 1.54e-51

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 169.41  E-value: 1.54e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   31 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 110
Cdd:COG2267   7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  111 LQHVDSMQKDyPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAkvlnlvlpnlslgpid 190
Cdd:COG2267  87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  191 ssvlsrnktevdiynsdplicraglkvcfgiqllnavSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAkSQDKT 270
Cdd:COG2267 150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVE 191

                       250       260       270
                ....*....|....*....|....*....|..
gi 6005786  271 LKIYEGAYHVLHKELPEvtNSVFHEINMWVSQ 302
Cdd:COG2267 192 LVLLPGARHELLNEPAR--EEVLAAILAWLER 221
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 82-284 1.16e-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: 46.31  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786     82 VFAHDHVGHGQSEGE---RMVVSDFHVFVRDVLQHVDSMQK-------------DY-------PGLPVFLLGHSMGGAIA 138
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYdivntkeNRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    139 iLTAAERPGH---------------FAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSsvLSRNKTEVDI 203
Cdd:TIGR01607 157 -LRLLELLGKsnenndklnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTFRISKKIR--YEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    204 YNSDPLICRAGLKVCFGIQLLNAVSRVE---RALPKlTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHV 280
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHV 312


                  ....
gi 6005786    281 LHKE 284
Cdd:TIGR01607 313 ITIE 316
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 103-144 2.05e-05

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: 44.77  E-value: 2.05e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 6005786  103 FHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 144
Cdd:cd00519 107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 32-304 4.84e-105

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 307.97  E-value: 4.84e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    32 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 111
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   112 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVlaNPESATTFKVLAAKVLNLVLPNLSLGPIDS 191
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   192 SVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSqDKTL 271
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 6005786   272 KIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 304
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 51-285 1.33e-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: 274.86  E-value: 1.33e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786     51 PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLG 130
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    131 HSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSL-GPIDSSVLSRNKTEVDIYNSDPL 209
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005786    210 ICRaGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKEL 285
Cdd:pfam12146 163 VHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
31-302 1.54e-51

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 169.41  E-value: 1.54e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   31 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 110
Cdd:COG2267   7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  111 LQHVDSMQKDyPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAkvlnlvlpnlslgpid 190
Cdd:COG2267  87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  191 ssvlsrnktevdiynsdplicraglkvcfgiqllnavSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAkSQDKT 270
Cdd:COG2267 150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVE 191

                       250       260       270
                ....*....|....*....|....*....|..
gi 6005786  271 LKIYEGAYHVLHKELPEvtNSVFHEINMWVSQ 302
Cdd:COG2267 192 LVLLPGARHELLNEPAR--EEVLAAILAWLER 221
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 33-303 1.48e-38

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 139.12  E-value: 1.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    33 VNADGQYLFCRYWKP-TGTPKALIFVSHGAGEHSGRY-EELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 110
Cdd:PLN02385  67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFfEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   111 LQHVDSMQ--KDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLV-----LANPESATTFKVLAAKVLnlvlPN 183
Cdd:PLN02385 147 IEHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCkiaddVVPPPLVLQILILLANLL----PK 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   184 LSLGP----IDSSVLSRNKTEVDIYNsdpLIC---RAGLKVcfGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKG 256
Cdd:PLN02385 223 AKLVPqkdlAELAFRDLKKRKMAEYN---VIAykdKPRLRT--AVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSV 297

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 6005786   257 AYLLMELAKSQDKTLKIYEGAYH-VLHKELPEVTNSVFHEINMWVSQR 303
Cdd:PLN02385 298 SKFLYEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 37-311 2.38e-37

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 135.67  E-value: 2.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    37 GQYLFCRYWKPTGT--PKALIFVSHGAG-EHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQH 113
Cdd:PLN02298  42 GLSLFTRSWLPSSSspPRALIFMVHGYGnDISWTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   114 VDSMQKD--YPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVlaAKVLNLV---LPNLSLGP 188
Cdd:PLN02298 122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPI--PQILTFVarfLPTLAIVP 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   189 ----IDSSVLSRNKTEVDIYNsdPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELA 264
Cdd:PLN02298 200 tadlLEKSVKVPAKKIIAKRN--PMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEA 277

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 6005786   265 KSQDKTLKIYEGAYH-VLHKELPEVTNSVFHEINMWVSQRTATAGTAS 311
Cdd:PLN02298 278 KSEDKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKATPS 325
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 35-303 4.68e-36

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 133.48  E-value: 4.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    35 ADGQYLFCRYWKP-TGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQH 113
Cdd:PLN02652 118 ARRNALFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   114 VDSMQKDYPGLPVFLLGHSMGGAIaILTAAERP---GHFAGMVLISPLVLANPESATTFKVlaAKVLNLVLPNLSLGPID 190
Cdd:PLN02652 198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPsieDKLEGIVLTSPALRVKPAHPIVGAV--APIFSLVAPRFQFKGAN 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   191 SS--VLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQD 268
Cdd:PLN02652 275 KRgiPVSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRH 354

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 6005786   269 KTLKIYEGAYHVLHKElPEvTNSVFHEINMWVSQR 303
Cdd:PLN02652 355 KDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKR 387
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
49-292 2.41e-26

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 104.25  E-value: 2.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   49 GTPKALIFVsHG--AGEHSGRYeeLARMLMGLDLLVFAHDHVGHGQSEGErMVVSDFHVFVRDVLQHVDSMQKDYPglPV 126
Cdd:COG1647  13 GGRKGVLLL-HGftGSPAEMRP--LAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  127 FLLGHSMGGAIAILTAAERPgHFAGMVLISPLVLANPESAttfkvLAAKVLNLVLPNLSLGPIDssvLSRNKTEVDIYNS 206
Cdd:COG1647  87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-----PLLPLLKYLARSLRGIGSD---IEDPEVAEYAYDR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  207 DPLICraglkvcfGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLH--KE 284
Cdd:COG1647 158 TPLRA--------LAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKD 229


                ....*...
gi 6005786  285 LPEVTNSV 292
Cdd:COG1647 230 REEVAEEI 237
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 30-295 7.59e-22

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: 91.60  E-value: 7.59e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   30 PHLVNADGQYLFCRYWKPTGTPkaLIFVsHGAGEHSGRYEELARMLMGlDLLVFAHDHVGHGQSEGERMVVSdFHVFVRD 109
Cdd:COG0596   4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYT-LDDLADD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  110 VLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVlanpesattfKVLAAkvlNLVLPNLSLGPI 189
Cdd:COG0596  79 LAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL----------AALAE---PLRRPGLAPEAL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  190 DSSVLSRNKTEvdiynsdplicraglkvcfgiqllnavsrVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKsqDK 269
Cdd:COG0596 142 AALLRALARTD-----------------------------LRERLARITVPTLVIWGEKDPIVPPALARRLAELLP--NA 190

                       250       260
                ....*....|....*....|....*.
gi 6005786  270 TLKIYEGAYHVLHKELPEVTNSVFHE 295
Cdd:COG0596 191 ELVVLPGAGHFPPLEQPEAFAAALRD 216
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 23-280 4.07e-20

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 87.66  E-value: 4.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   23 SIPYQDLpHLVNADGQYLFCRYWKPTGTPKAL--IFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGE-RMV 99
Cdd:COG1073   7 KVNKEDV-TFKSRDGIKLAGDLYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEpREE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  100 VS----DFHVFVRDVLQhvdsmQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLISPlvLANPESAttFKVLAAK 175
Cdd:COG1073  86 GSperrDARAAVDYLRT-----LPGVDPERIGLLGISLGGGYALNAAATDPR-VKAVILDSP--FTSLEDL--AAQRAKE 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  176 VLNLVLPNLSLGPIDSSVLSRNKtEVDIYNsdplicraglkvcfgiqllnavsrverALPKLTVPFLLLQGSADRLCDSK 255
Cdd:COG1073 156 ARGAYLPGVPYLPNVRLASLLND-EFDPLA---------------------------KIEKISRPLLFIHGEKDEAVPFY 207

                       250       260
                ....*....|....*....|....*
gi 6005786  256 GAYLLMELAkSQDKTLKIYEGAYHV 280
Cdd:COG1073 208 MSEDLYEAA-AEPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
34-284 1.54e-17

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 80.06  E-value: 1.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   34 NADGQYLFCRYWKPTGTPKA-LIFVSHGAGEH-SGRYEELARMLMGLDLLVFAHDHVGHGQSEGERmvvsdFHVFVRDVL 111
Cdd:COG1506   4 SADGTTLPGWLYLPADGKKYpVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVDDVL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  112 QHVDSM--QKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPlvlanpesattfkvlaakVLNLVlpnlslgpi 189
Cdd:COG1506  79 AAIDYLaaRPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG------------------VSDLR--------- 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  190 dsSVLSRNKTEVDIYNSDPLICRAGLKvcfgiqllnAVSRVERAlPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQ-- 267
Cdd:COG1506 132 --SYYGTTREYTERLMGGPWEDPEAYA---------ARSPLAYA-DKLKTPLLLIHGEADDRVPPEQAERLYEALKKAgk 199

                       250
                ....*....|....*..
gi 6005786  268 DKTLKIYEGAYHVLHKE 284
Cdd:COG1506 200 PVELLVYPGEGHGFSGA 216
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 52-284 5.96e-14

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: 70.23  E-value: 5.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786     52 KALIFVsHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGeRMVVSDFHV--FVRDVLQHVDSMQKDypglPVFLL 129
Cdd:pfam00561   1 PPVLLL-HGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTddLAEDLEYILEALGLE----KVNLV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    130 GHSMGGAIAILTAAERPGHFAGMVLISPLVLAN-------------PESATTFKVLAAKVLNLVLPNLSLGPI---DSSV 193
Cdd:pfam00561  75 GHSMGGLIALAYAAKYPDRVKALVLLGALDPPHeldeadrfilalfPGFFDGFVADFAPNPLGRLVAKLLALLllrLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    194 LSRNKTEVDIYNSDPLIcrAGLKVCFGIQLLNAVSRVERA--LPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSqdKTL 271
Cdd:pfam00561 155 KALPLLNKRFPSGDYAL--AKSLVTGALLFIETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPN--ARL 230

                         250
                  ....*....|...
gi 6005786    272 KIYEGAYHVLHKE 284
Cdd:pfam00561 231 VVIPDAGHFAFLE 243
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 54-282 2.29e-09

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 56.33  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786     54 LIFVsHGAGEHSGRYEELARmlmgLDLLVFAHDHVGHGQSEGERMVVSDfhvfVRDVLQHVDSMQKDYPglpVFLLGHSM 133
Cdd:pfam12697   1 VVLV-HGAGLSAAPLAALLA----AGVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    134 GGAIAILTAAerpGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRA 213
Cdd:pfam12697  69 GGAVALAAAA---AALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAA 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005786    214 GLKVCFGIQLlnavsrveRALPKLTVPFLLLqGSADRLCDskgAYLLMELAKSQDKTLKIYEGAYHVLH 282
Cdd:pfam12697 146 LLAALALLPL--------AAWRDLPVPVLVL-AEEDRLVP---ELAQRLLAALAGARLVVLPGAGHLPL 202
YpfH COG0400
Predicted esterase [General function prediction only];
48-164 1.66e-08

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 53.76  E-value: 1.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   48 TGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFA------HDHVGHG----QSEGERMVVSDFHVFVRDVLQHVDSM 117
Cdd:COG0400   1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDEL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6005786  118 QKDYpGLP---VFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPE 164
Cdd:COG0400  81 EARY-GIDperIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEA 129
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
31-177 5.66e-08

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 52.66  E-value: 5.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   31 HLVNADGQYLFCRYWKPTGT-PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFA---HDHVGHGQSEGE---RMVVSDF 103
Cdd:COG0412   7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDP 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005786  104 HVFVRDVLQHVD--SMQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLISPLVLANPESATTFKVlAAKVL 177
Cdd:COG0412  87 ELLAADLRAALDwlKAQPEVDAGRVGVVGFCFGGGLALLAAARGPD-LAAAVSFYGGLPADDLLDLAARI-KAPVL 160
PRK10749 PRK10749
lysophospholipase L2; Provisional
 67-296 2.45e-07

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 51.54  E-value: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    67 RYEELARMLMGLDLLVFAHDHVGHGQS-----EGERMVVSDFHVFVRDV----LQHVDSmqkdYPGLPVFLLGHSMGGAI 137
Cdd:PRK10749  69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLaafwQQEIQP----GPYRKRYALAHSMGGAI 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   138 AILTAAERPGHFAGMVLISPL---VLANPESATTFKVLAAKVLNLVLPNLSLG-------PIDSSVLS----RNKTEVDI 203
Cdd:PRK10749 145 LTLFLQRHPGVFDAIALCAPMfgiVLPLPSWMARRILNWAEGHPRIRDGYAIGtgrwrplPFAINVLThsreRYRRNLRF 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   204 YNSDPLI---------CRAGLKVcfGIQLLNAVsrveralPKLTVPFLLLQGSADRLCDSkgayllmelaKSQDKTLKIY 274
Cdd:PRK10749 225 YADDPELrvggptyhwVRESILA--GEQVLAGA-------GDITTPLLLLQAEEERVVDN----------RMHDRFCEAR 285

                        250       260
                 ....*....|....*....|..
gi 6005786   275 EGAYHVLHKELPEVTNSVFHEI 296
Cdd:PRK10749 286 TAAGHPCEGGKPLVIKGAYHEI 307
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 43-157 3.69e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 51.10  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    43 RYWK-PTGTPKALIFVsHG-AGEHS---GRYEELARmlmglDLLVFAHDHVGHGQSeGERMVVSDFHVFVRDVLQHVDSM 117
Cdd:PRK14875 122 RYLRlGEGDGTPVVLI-HGfGGDLNnwlFNHAALAA-----GRPVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAL 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 6005786   118 QKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISP 157
Cdd:PRK14875 195 GIE----RAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
47-279 9.56e-06

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 46.64  E-value: 9.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   47 PTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGH--GQSEGERMVVSDFHVF---------VRDVLQHVD 115
Cdd:COG4188  57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaADLSAALDGLADALDPeelwerpldLSFVLDQLL 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  116 SMQKDYPGLP-------VFLLGHSMGGAIAILTAAERPghfagmvlisplvlanpeSATTFKVLAAKVLNLVLPNLSLGP 188
Cdd:COG4188 137 ALNKSDPPLAgrldldrIGVIGHSLGGYTALALAGARL------------------DFAALRQYCGKNPDLQCRALDLPR 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786  189 IDSSVlsrnktevdiynSDPLIcRAGLkvcfgiqLLNAVSR---VERALPKLTVPFLLLQGSADRlcDSKGAY---LLME 262
Cdd:COG4188 199 LAYDL------------RDPRI-KAVV-------ALAPGGSglfGEEGLAAITIPVLLVAGSADD--VTPAPDeqiRPFD 256

                       250
                ....*....|....*..
gi 6005786  263 LAKSQDKTLKIYEGAYH 279
Cdd:COG4188 257 LLPGADKYLLTLEGATH 273
COG4099 COG4099
Predicted peptidase [General function prediction only];
54-170 1.13e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 45.73  E-value: 1.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   54 LIFVSHGAGEhsgRYEELARMLM-GLDLLVfahdhvghGQSEGER---MVVS---------DFHVFVRDVLQHVDSMQKD 120
Cdd:COG4099  51 LVLFLHGAGE---RGTDNEKQLThGAPKFI--------NPENQAKfpaIVLApqcpeddywSDTKALDAVLALLDDLIAE 119

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 6005786  121 YPGLP--VFLLGHSMGGAIAILTAAERPGHFAGMVLISPlvLANPESATTFK 170
Cdd:COG4099 120 YRIDPdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 82-284 1.16e-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: 46.31  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786     82 VFAHDHVGHGQSEGE---RMVVSDFHVFVRDVLQHVDSMQK-------------DY-------PGLPVFLLGHSMGGAIA 138
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYdivntkeNRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    139 iLTAAERPGH---------------FAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSsvLSRNKTEVDI 203
Cdd:TIGR01607 157 -LRLLELLGKsnenndklnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTFRISKKIR--YEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    204 YNSDPLICRAGLKVCFGIQLLNAVSRVE---RALPKlTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHV 280
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHV 312


                  ....
gi 6005786    281 LHKE 284
Cdd:TIGR01607 313 ITIE 316
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 49-167 2.05e-05

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 45.38  E-value: 2.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   49 GTPKALIFVSHGAG------EHSGRYEELARmlmGLDLLV----------------FAHDHVGHGQSEgermvvsdfHVF 106
Cdd:COG3509  50 GAPLPLVVALHGCGgsaadfAAGTGLNALAD---REGFIVvypegtgrapgrcwnwFDGRDQRRGRDD---------VAF 117

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005786  107 VRDVlqhVDSMQKDYPGLP--VFLLGHSMGGAIAILTAAERPGHFAGMVLIS--PLVLANPESAT 167
Cdd:COG3509 118 IAAL---VDDLAARYGIDPkrVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACA 179
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 103-144 2.05e-05

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: 44.77  E-value: 2.05e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 6005786  103 FHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 144
Cdd:cd00519 107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 125-158 2.06e-05

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: 45.29  E-value: 2.06e-05
                        10        20        30
                ....*....|....*....|....*....|....
gi 6005786  125 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISPL 158
Cdd:cd12809 172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
109-158 3.35e-05

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


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 44.10  E-value: 3.35e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 6005786  109 DVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLIS-PL 158
Cdd:COG3571  65 AWRAVIAALRARLAGLPLVIGGKSMGGRVASMLAAEGGG-AAGLVCLGyPF 114
PLN02578 PLN02578
hydrolase
 49-301 4.57e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 44.45  E-value: 4.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    49 GTPKALIfvsHGAGEHS--GRYE--ELARMLMgldllVFAHDHVGHGQSEgERMVVSDFHVFVRDVLQHVDSMQKDypgl 124
Cdd:PLN02578  86 GLPIVLI---HGFGASAfhWRYNipELAKKYK-----VYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE---- 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   125 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISPL------------VLANPESA-TTFKVLAAK------VLNLVLPNLS 185
Cdd:PLN02578 153 PAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAgqfgsesrekeeAIVVEETVlTRFVVKPLKewfqrvVLGFLFWQAK 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   186 LGPIDSSVLS---RNKTEVDIY--------NSDP--------LICRAglkvcfgiqLLNAvSR--VERALPKLTVPFLLL 244
Cdd:PLN02578 233 QPSRIESVLKsvyKDKSNVDDYlvesitepAADPnagevyyrLMSRF---------LFNQ-SRytLDSLLSKLSCPLLLL 302

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6005786   245 QGSADRLCDSKGAYLLMELakSQDKTLkIYEGAYHVLHKELPEVTNSVFHEinmWVS 301
Cdd:PLN02578 303 WGDLDPWVGPAKAEKIKAF--YPDTTL-VNLQAGHCPHDEVPEQVNKALLE---WLS 353
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 108-144 1.00e-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: 41.72  E-value: 1.00e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6005786  108 RDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 144
Cdd:cd00741  12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
106-157 5.76e-04

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 40.74  E-value: 5.76e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6005786  106 FVRDVLQ-HVDsmqKDYPGLPVF--LLGHSMGGAIAILTAAERPGHFAGMVLISP 157
Cdd:COG2819 112 FLEEELKpYID---KRYRTDPERtgLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 47-157 1.07e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 37.89  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   47 PTGTPKALIFVsHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERmvvsdfhvfVRDVLQHVDSMQKDYPGLPV 126
Cdd:COG1075   1 YAATRYPVVLV-HGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDS---------AEQLAAFVDAVLAATGAEKV 70

                        90       100       110
                ....*....|....*....|....*....|...
gi 6005786  127 FLLGHSMGGAIA--ILTAAERPGHFAGMVLISP 157
Cdd:COG1075  71 DLVGHSMGGLVAryYLKRLGGAAKVARVVTLGT 103
Abhydrolase_5 pfam12695
Alpha/beta hydrolase family; This family contains a diverse range of alpha/beta hydrolase ...
 114-203 2.22e-03

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


Pssm-ID: 315383 [Multi-domain]  Cd Length: 164  Bit Score: 38.20  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786    114 VDSMQKDYPGLPVFLL-GHSMGGAIAILTAAERpGHFAGMVLisplvLANPESATTFKVLAAKVLNLVLPNLSLGPIDSS 192
Cdd:pfam12695  46 ALSIIKAHPKIQKWVVgGHSLGGVMASRFAADN-ELIKGVVF-----LASYPDKDSLSNLSFPVLSIYGTNDGVLNWKSY 119

                          90
                  ....*....|....*.
gi 6005786    193 V-----LSRNKTEVDI 203
Cdd:pfam12695 120 QknkqfLPKDTTYVSI 135
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
15-161 2.80e-03

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 38.97  E-value: 2.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   15 SSPRRTPQsIPYQ----DLPhlvnaDGQYLFCRYWKPTGTPKALIFVSHG-AGEHSGRY-EELARMLMGLDLLVFAHDHV 88
Cdd:COG0429  26 SLFRRRPA-LPYRrerlELP-----DGDFVDLDWSDPPAPSKPLVVLLHGlEGSSDSHYaRGLARALYARGWDVVRLNFR 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   89 GHGQSE---------GErmvVSDfhvfVRDVLQHVdsmQKDYPGLPVFLLGHSMGGAIAILTAAERPGH---FAGMVLIS 156
Cdd:COG0429 100 GCGGEPnllprlyhsGD---TED----LVWVLAHL---RARYPYAPLYAVGFSLGGNLLLKYLGEQGDDappLKAAVAVS 169


                ....*.
gi 6005786  157 -PLVLA 161
Cdd:COG0429 170 pPLDLA 175
Lipase_3 pfam01764
Lipase (class 3);
121-169 3.07e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 37.24  E-value: 3.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 6005786    121 YPGLPVFLLGHSMGGAIAILTAAerpghfagMVLISPLVLANPESATTF 169
Cdd:pfam01764  60 YPDYSIVVTGHSLGGALASLAAL--------DLVENGLRLSSRVTVVTF 100
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 47-144 3.88e-03

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 37.91  E-value: 3.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005786   47 PTGTPKALIFVSHGAGEHSGRYEELARmLMGLDLLVFAHDHVGHGQSEGERMVvSDFHVFVRDVLQHVdsmqKDYPGLPV 126
Cdd:COG3208   1 PRPDARLRLFCFPYAGGSASAYRPWAA-ALPPDIEVLAVQLPGRGDRLGEPPL-TSLEELADDLAEEL----APLLDRPF 74

                        90
                ....*....|....*...
gi 6005786  127 FLLGHSMGGAIAILTAAE 144
Cdd:COG3208  75 ALFGHSMGALLAFELARR 92
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
83-144 3.97e-03

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 38.20  E-value: 3.97e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005786   83 FAHDHVGHGQSEGerMVVSDFHVFVRDVLQHVDSM-QKDYPGLPVFLLGHSMGGAIAILTAAE 144
Cdd:COG3675  48 AAQVPYPFAKTGG--KVHRGFYRALQSLRELLEDAlRPLSPGKRLYVTGHSLGGALATLAAAD 108
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 128-159 4.83e-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: 37.83  E-value: 4.83e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 6005786    128 LLGHSMGGAIAILTAAERPGHFAGMVLISPLV 159
Cdd:pfam00756 114 LAGQSMGGLGALYLALKYPDLFGSVSSFSPIL 145
PRK10673 PRK10673
esterase;
90-155 6.04e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 37.79  E-value: 6.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005786    90 HGQSEgeRMVVSDFHVFVRDVLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLI 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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